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3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
4,6-benzylidene-alpha-D-4-nitrophenylmaltoheptaose + D-glucose
4,6-benzylidene-maltopentaose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose
-
blocked p-nitrophenyl-(alpha-1,4-glucopyranosyl)6-D-glucose , weak cleavage
-
-
?
4,6-O-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + maltose
?
4-nitrophenyl alpha-D-maltoheptaoside-4-6-O-ethylidene + maltose
?
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
alpha-1,4-glucan + glycosyl acceptor
cyclohexaamylose + cycloheptaamylose + cyclooctaamylose
alpha-cyclodextrin + ascorbic acid
L-ascorbic acid-2-O-alpha-D-glucoside + L-ascorbic acid-2-O-alpha-D-oligoglucoside
-
-
-
-
r
alpha-cyclodextrin + D-glucose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + glucose
alpha-cyclodextrin + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
alpha-cyclodextrin + isoascorbic acid
L-isoascorbic acid-2-O-alpha-D-glucoside + L-isoascorbic acid-2-O-alpha-D-oligoglucoside
-
-
-
-
r
alpha-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
alpha-cyclodextrin + maltohexaose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltotetraose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltotriose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + sucrose
?
-
ATCC 21783
-
-
r
alpha-cyclodextrin + sucrose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
amylopectin + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
alpha-cyclodextrin is preferentially produced. With a longer incubation period, the alpha-cyclodextrin to beta-cyclodextrin ratio declines
larger cyclodextrins (>8 glucose units) are formed in the initial reaction period
-
?
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
amylopectin beta-limit dextrin + glycosyl acceptor
?
-
-
-
-
r
amylose
alpha-cyclodextrin
amylose + glycosyl acceptor
?
amylose + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
alpha-cyclodextrin is preferentially produced. With a longer incubation period, the alpha-cyclodextrin to beta-cyclodextrin ratio declines
larger cyclodextrins (>8 glucose units) are formed in the initial reaction period
-
?
amylose + glycosyl acceptor
cyclodextrin
-
-
higher yield of large-ring cyclodextrins are ontained with a reaction temperature of 60°C compared to 40°C
-
?
amylose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
beta-cyclodextrin + 4-nitrophenyl-beta-D-glucopyranose
?
beta-cyclodextrin + D-glucose
?
beta-cyclodextrin + D-glucose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
beta-cyclodextrin + maltohexaose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + maltose
?
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
beta-cyclodextrin + maltotetraose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
beta-cyclodextrin + salicin
?
beta-cyclodextrin + sucrose
?
-
ATCC 21783
-
-
r
beta-cyclodextrin + sucrose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
cassava starch
beta-cyclodextrin
cassava starch + D-glucose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin + maltooligosaccharides
corn flour + ?
beta-cyclodextrins
corn starch + ?
beta-cyclodextrins
corn starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the major product
-
?
corn starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
corn starch + maltose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin + malto-oligosaccharides
-
-
-
-
?
cycloamylose + D-glucose
?
cyclodextrins + acceptor
linear maltooligosaccharide
cycloheptaamylose + glycosyl acceptor
?
-
-
-
-
r
cyclohexaamylose + D-glucose
linear oligosaccharide
-
-
-
r
cyclohexaamylose + glycosyl acceptor
?
-
-
-
-
r
cyclohexaamylose + maltose
linear oligosaccharide
-
-
-
r
cyclohexaamylose + sucrose
linear oligosaccharide
-
-
-
r
cyclomaltohexaose + cyclo-[alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-alpha-D-Glp-(1-6)]
cyclo-[alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-[alpha-D-Glcp-(1-4)]-alpha-D-Glp-(1-6)] + ?
-
-
-
-
?
cyclomaltohexaose + cyclo-[alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-alpha-D-Glp-(1-6)]
cyclo-[alpha-D-Glcp-(1-3)-[alpha-D-Glcp-(1-4)]-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-[alpha-D-Glcp-(1-4)]-alpha-D-Glp-(1-6)] + ?
-
-
-
-
?
cyclomaltohexaose + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + maltooligosyl sugars
cyclomaltohexaose + methyl alpha-D-glucopyranoside
maltodextrin glycoside
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5-1.0 give a wide range of sizes from d.p. 2-17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + methyl beta-D-glucopyranoside
maltodextrin glycoside
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5-1.0 give a wide range of sizes from d.p. 2-17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + phenyl alpha-D-glucopyranoside
maltodextrin glycoside
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.51.0 give a wide range of sizes from d.p. 217 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + phenyl beta-D-glucopyranoside
maltodextrin glycoside
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.51.0 give a wide range of sizes from d.p. 217 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
dextrin
beta-cyclodextrin + alpha-cyclodextrin
-
the maximum conversion of dextrin to beta-cyclodextrin and alpha-cyclodextrin is 29% both for the soluble and immobilized enzymes
-
-
?
dextrin + glycosyl acceptor
beta-cyclodextrin
dextrin + glycosyl acceptor
cyclodextrins
-
-
-
-
r
dextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
dodecyl-beta-D-maltoside + alpha-cyclodextrin
dodecyl-beta-D-maltooctaoside + ?
gamma-cyclodextrin + glycosyl acceptor
maltooligosaccharide
-
-
-
-
r
gamma-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
genistein + alpha-cyclodextrin
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
genistein + beta-cyclodextrin
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
genistein + D-glucose
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
very low activity with D-glucose als glysosyl donor
-
-
?
genistein + maltodextrin
alpha-cyclodextrins
less than 20% conversion ratio
-
-
?
genistein + maltodextrin
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
genistein + maltose
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
genistein + starch
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
genistein + sucrose
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
very low activity with sucrose als glysosyl donor
-
-
?
Glucidex 12 + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
Glucidex 2B + glycosyl acceptor
beta-cyclodextrin
glycogen + acceptor
beta-cyclodextrin
glycogen + H2O
cyclodextrins
-
-
-
?
hydrolyzed cassava starch
beta-cyclodextrin
hydrolyzed corn starch
beta-cyclodextrin
hydrolyzed potato starch
beta-cyclodextrin
hydrolyzed potato starch + (-)-epigallocatechin gallate
epigallocatechin gallate 3'-O-alpha-D-glucopyranoside + epigallocatechin gallate 7-O-alpha-D-glucopyranoside
-
-
-
-
?
L-ascorbic acid + beta-cyclodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
-
-
-
?
L-ascorbic acid + maltodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + glycosyl acceptor
L-ascorbic acid alpha-D-glucoside + D-glucosyl-[glycosyl acceptor]
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + H2O
L-ascorbic acid-2-O-alpha-D-glucoside + D-glucose
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + glycosyl acceptor
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + D-glucosyl-[glycosyl acceptor]
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + H2O
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + D-glucose
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)4 + glycosyl acceptor
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + glucosyl-[glycosyl acceptor]
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)4 + H2O
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + D-glucose
-
-
-
r
L-ascorbic acid-2-O-alpha-D-glucoside + H2O
L-ascorbic acid + D-glucose
-
-
-
?
linear alpha-(1,4)-glucan DP 29 + sucrose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
linear alpha-(1,4)-glucan DP 38 + sucrose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
linear alpha-(1,4)-glucan DP 44 + sucrose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
linear alpha-(1,4)-glucan DP 53,116 + sucrose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
linear alpha-(1,4)-glucan DP 65,166 + sucrose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
linear maltooligosaccharide + acceptor
?
maltodextrin
beta-cyclodextrin
maltodextrin + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
maltodextrin + glycosyl acceptor
alpha-cyclodextrin
maltodextrin + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
maltodextrin + glycosyl acceptor
beta-cyclodextrin
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
maltodextrin + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin + alpha-cyclodextrin
maltodextrin + glycosyl acceptor
cyclodextrins
maltodextrin + L-ascorbic acid
2-O-D-glucopyranosyl-L-ascorbic acid + ?
maltodextrin DE 4-7 + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
maltoheptaose + glycosyl acceptor
beta-cyclodextrin
maltoheptaose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
maltohexaose + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
maltohexaose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid + ?
-
-
-
-
?
maltohexaose + L-ascorbic acid
L-ascorbic acid-(2-O-alpha-D-glucosyl)6
-
-
-
r
maltooligosaccharides + glycosyl acceptor
cyclodextrins
maltopentaose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
r
maltopentaose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltose + acceptor
?
-
-
-
-
r
maltose + ascorbic acid
L-ascorbic acid-2-O-alpha-D-glucoside + D-glucose
-
-
-
r
maltose + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
maltose + glycosyl acceptor
beta-cyclodextrin
maltose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
maltotetraose + glycosyl acceptor
beta-cyclodextrin
maltotetraose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltotriose + glycosyl acceptor
beta-cyclodextrin
maltotriose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
maltotriose + maltotetraose
maltopentaose
-
-
-
r
methanol + maltodextrin
alpha-methyl-D-glucopyranoside + beta-cyclodextrin
-
-
-
-
?
methyl-alpha-D-glucoside + glycosyl acceptor
cyclodextrins
-
-
-
-
?
naringin + maltodextrin
?
native starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
alpha-cyclodextrin is preferentially produced. With a longer incubation period, the alpha-cyclodextrin to beta-cyclodextrin ratio declines
larger cyclodextrins (>8 glucose units) are formed in the initial reaction period
-
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + glycosyl acceptor
p-nitrophenyl-D-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + ?
-
E 192
main product p-nitrophenyl-glucose when chain length of substrate is 4 glucose or less, p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose when substrate chain length is 5 or more glucose residues
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + ?
-
E 192
product proportions 48:31:21
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)6-D-glucose + glycosyl acceptor
p-nitrophenyl-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(glucose)3 + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)4-D-glucose + ?
-
E 192
product proportions 33:27:16:6:17
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)7-D-glucose + glycosyl acceptor
p-nitrophenyl-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)4-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)5-D-glucose + ?
-
E 192
product proportions 16:51:12:13:4:4
?
p-nitrophenyl-(glucose)5 + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + p-nitrophenyl-(alpha-1,4-D-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-D-glucopyranosyl)3-D-glucose
-
E 192
product proportions 32:50:12 6
?
p-nitrophenyl-(glucose)6 + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + ?
-
E 192
product proportions 18:53:21:8
?
Paselli starch
beta-cyclodextrin
potato starch + ?
beta-cyclodextrins
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
potato starch + glycosyl acceptor
beta-cyclodextrin
potato starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
potato starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
raw corn starch
beta-cyclodextrin + gamma-cyclodextrin
raw starch
beta-cyclodextrin + gamma-cyclodextrin
rice flour + ?
beta-cyclodextrins
rice starch + glycosyl acceptor
beta-cyclodextrin
rice starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
sago starch + ?
beta-cyclodextrins
soluble corn starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
soluble potato starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
soluble potato starch + sucrose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
soluble potoato starch
cyclodextrin
soluble starch
alpha-cyclodextrin
-
poly-lysine fused immobilization increases the Vmax of the immobilized CGTase by 40% without a change in Km. Maximum alpha-cyclodextrin productivity of 539.4 g/l*h is obtained with 2% soluble starch solution which is constantly fed at a flow rate of 4.0 ml/min in a continuous operation mode of a packed-bed reactor
-
-
?
soluble starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
soluble starch
beta-cyclodextrin
soluble starch + ?
beta-cyclodextrins
-
11.7 mg/l of cyclodextrins produced after 1 h of incubation at 60°C
-
-
?
soluble starch + cellobiose
?
-
-
-
-
r
soluble starch + D-fructose
?
soluble starch + D-galactose
?
soluble starch + D-glucose
cyclodextrins
soluble starch + D-maltose
cyclodextrins
soluble starch + D-rhamnose
?
-
-
-
-
r
soluble starch + D-sorbose
?
soluble starch + D-xylose
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
beta-cyclodextrin
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
soluble starch + glycosyl acceptor
cycloheptaamylose
soluble starch + glycosyl acceptor
cyclohexaamylose
-
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
soluble starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
soluble starch + glycosyl acceptor
maltose + maltotriose + maltotetraose + maltopentaose
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
soluble starch + glycosyl acceptor
Schardinger dextrins
soluble starch + H2O
cyclodextrins
soluble starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
soluble starch + L-sorbose
?
-
-
-
-
r
soluble starch + maltose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin + malto-oligosaccharides
-
-
-
-
?
soluble starch + maltotriose
cyclodextrins
soluble starch + myo-inositol
?
-
-
-
-
r
soluble starch + ribose
?
-
-
-
-
r
soluble starch + sucrose
?
soluble starch + sucrose
maltosylfructose
-
-
-
r
sophoricoside + maltodextrin
Glc-sophoricoside + Glc2-sophoricoside + Glc3-sophoricoside + Glc4-sophoricoside + Glc5-sophoricoside + Glc6-sophoricoside
more than 40% conversion ratio
-
-
?
starch
alpha-cyclodextrin
-
-
-
-
?
starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
starch
gamma-cyclodextrin
starch + ascorbic acid
2-O-alpha-glucopyranosyl L-ascorbic acid
-
-
-
-
r
starch + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
alpha-cyclodextrin, beta-cyclodextrin and gamma-cyclodextrin in the ratio of 0.26:1.0:0.86
-
?
starch + glycosyl acceptor
beta-cyclodextrin
starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
starch + glycosyl acceptor
cyclodextrin
-
the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase
-
-
?
starch + glycosyl acceptor
cyclodextrins
starch + hesperidin
glycosyl hesperidin
-
-
-
-
r
starch + maltose
beta-cyclodextrin + gamma-cyclodextrin + maltooligosaccharides
-
-
-
-
?
starch + maltose
cyclodextrins
-
-
-
-
?
starch + rutin
glycosyl rutin
-
-
-
-
r
starch + salicin
glycosyl salicin
-
-
-
-
r
starch + stevioside
glycosyl stevioside
starch + sucrose
maltooligosyl sucrose
stevioside + beta-cyclodextrin
4'-O-alpha-D-glycosyl stevioside + 4''-O-alpha-D-maltosyl stevioside + ?
stevioside + maltodextrin
?
sweet potato starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
wheat flour + polyphenol
gallic acid-4-O-beta-D-glucopyranoside + ellagic acid-4-O-beta-D-glucopyranoside + catechin-4'-O-glucopyranoside
-
polyphenols derived from Moringa oleifera leaves extract
-
-
?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
additional information
?
-
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
-
strain 1011, disproportionation
-
-
?
4,6-O-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + maltose
?
-
maltose as donor and acceptor, overview
-
-
?
4,6-O-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + maltose
?
-
maltose as donor and acceptor, overview
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4-6-O-ethylidene + maltose
?
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4-6-O-ethylidene + maltose
?
-
-
-
?
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
strain 1011
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
strain 1011
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
strain 1011
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
strain 1011
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
?
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
?
alpha-1,4-glucan + glycosyl acceptor
cyclohexaamylose + cycloheptaamylose + cyclooctaamylose
-
-
product ratio 1: 2.4: 1
r
alpha-1,4-glucan + glycosyl acceptor
cyclohexaamylose + cycloheptaamylose + cyclooctaamylose
-
-
product ratio 1: 2.4: 1
r
alpha-cyclodextrin + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + glucose
-
-
oligosaccharide A
r
alpha-cyclodextrin + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + glucose
-
-
oligosaccharide A
r
alpha-cyclodextrin + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
highest activity with alpha-cyclodextrin as glycosyl donor
-
-
?
alpha-cyclodextrin + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
highest activity with alpha-cyclodextrin as glycosyl donor
-
-
?
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
-
r
alpha-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
highest activity, 40% conversion rate
-
-
?
alpha-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
highest activity
-
-
?
alpha-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
alpha-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
30% conversion rate
-
-
?
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
-
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
ATCC 21783
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
C31
-
-
?
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
C31
-
-
?
amylose
alpha-cyclodextrin
-
catalyzes the conversion of amylose to cyclodextrins, circular alpha-(1,4)-linked glucopyranose oligosaccharides of different ring sizes, the cyclodextrin containing 12 alpha-D-glucopyranose residues is preferentially synthesized by the enzyme. Interactions at oligosaccharide-binding subsites located close to the catalytic site apparently play a more important role in the determination of the size of the cyclodextrin formed
product identification by amperometric detection, overview
-
?
amylose
alpha-cyclodextrin
-
catalyzes the conversion of amylose to cyclodextrins, circular alpha-(1,4)-linked glucopyranose oligosaccharides of different ring sizes, the cyclodextrin containing 12 alpha-D-glucopyranose residues is preferentially synthesized by the enzyme. Interactions at oligosaccharide-binding subsites located close to the catalytic site apparently play a more important role in the determination of the size of the cyclodextrin formed
product identification by amperometric detection, overview
-
?
amylose + glycosyl acceptor
?
-
-
-
-
?
amylose + glycosyl acceptor
?
-
-
-
-
r
amylose + glycosyl acceptor
?
-
NO2, spiral amylose
-
-
r
amylose + glycosyl acceptor
?
-
NO2, spiral amylose
-
-
r
amylose + glycosyl acceptor
?
-
NO2, spiral amylose
-
-
r
amylose + glycosyl acceptor
?
-
-
-
-
r
amylose + glycosyl acceptor
?
-
ATCC 21783
-
-
r
amylose + glycosyl acceptor
?
-
C31
-
-
?
amylose + glycosyl acceptor
?
-
-
-
-
r
amylose + glycosyl acceptor
?
-
C31
-
-
?
beta-cyclodextrin + 4-nitrophenyl-beta-D-glucopyranose
?
-
beta-cyclodextrin as a glycosyl donor and 4-nitrophenyl-beta-D-glucopyranose as a glycosyl acceptor
-
-
?
beta-cyclodextrin + 4-nitrophenyl-beta-D-glucopyranose
?
-
beta-cyclodextrin as a glycosyl donor and 4-nitrophenyl-beta-D-glucopyranose as a glycosyl acceptor
-
-
?
beta-cyclodextrin + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
r
beta-cyclodextrin + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
r
beta-cyclodextrin + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
r
beta-cyclodextrin + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
beta-cyclodextrin + genistein
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
-
-
-
?
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
1% conversion rate
-
-
?
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
1% conversion rate
-
-
?
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
30% conversion rate
-
-
?
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
37% conversion rate
-
-
?
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
37% conversion rate
-
-
?
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
9% conversion rate
-
-
?
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
beta-cyclodextrin + maltose
?
-
-
-
-
?
beta-cyclodextrin + maltose
?
-
-
-
-
?
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
ATCC 21783
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
ATCC 21783
-
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
beta-cyclodextrin + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
beta-cyclodextrin + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cassava starch
beta-cyclodextrin
-
-
-
-
?
cassava starch
beta-cyclodextrin
-
-
-
-
?
cassava starch + D-glucose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin + maltooligosaccharides
-
the native and recombinant enzymes show 48.8% and 47.8% conversion, respectively
-
-
?
cassava starch + D-glucose
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin + maltooligosaccharides
-
the native and recombinant enzymes show 48.8% and 47.8% conversion, respectively
-
-
?
corn flour + ?
beta-cyclodextrins
-
-
-
-
?
corn flour + ?
beta-cyclodextrins
-
-
-
-
?
corn starch + ?
beta-cyclodextrins
-
0.17 mg/l of cyclodextrins produced after 1 h of incubation at 60°C
-
-
?
corn starch + ?
beta-cyclodextrins
-
0.17 mg/l of cyclodextrins produced after 1 h of incubation at 60°C
-
-
?
corn starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
corn starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
cycloamylose + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cyclodextrins + acceptor
linear maltooligosaccharide
-
strain 1011, cyclodextrin ring opening
-
r
cyclodextrins + acceptor
linear maltooligosaccharide
-
strain 1011, cyclodextrin ring opening
-
r
cyclodextrins + acceptor
linear maltooligosaccharide
-
strain 1011, cyclodextrin ring opening
-
r
cyclodextrins + acceptor
linear maltooligosaccharide
-
strain 1011, cyclodextrin ring opening
-
r
cyclomaltohexaose + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + maltooligosyl sugars
-
-
oligosaccharide A
r
cyclomaltohexaose + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + maltooligosyl sugars
-
-
oligosaccharide A
r
dextrin + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
dextrin + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
dextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
dextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
dextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
highest activity, 17% conversion rate
-
-
?
dodecyl-beta-D-maltoside + alpha-cyclodextrin
dodecyl-beta-D-maltooctaoside + ?
-
the equilibrium lays to 80% on the side of dodecyl-beta-D-maltooctaoside production when the enzyme from Bacillus macerans is used as biocatalyst
-
-
r
dodecyl-beta-D-maltoside + alpha-cyclodextrin
dodecyl-beta-D-maltooctaoside + ?
-
-
-
-
r
gamma-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
gamma-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
gamma-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
genistein + alpha-cyclodextrin
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
highest activity with alpha-cyclodextrin as glycosyl donor
-
-
?
genistein + alpha-cyclodextrin
genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside
-
highest activity with alpha-cyclodextrin as glycosyl donor
-
-
?
Glucidex 2B + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
Glucidex 2B + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
Glucidex 2B + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
glycogen + acceptor
beta-cyclodextrin
-
-
-
-
?
glycogen + acceptor
beta-cyclodextrin
-
ATCC 21783
-
-
r
glycogen + acceptor
beta-cyclodextrin
-
C31
-
-
?
glycogen + acceptor
beta-cyclodextrin
-
E 192
-
r
glycogen + acceptor
beta-cyclodextrin
-
C31
-
-
?
glycogen + acceptor
beta-cyclodextrin
-
-
-
-
?
glycogen + acceptor
beta-cyclodextrin
-
-
-
-
r
hydrolyzed cassava starch
beta-cyclodextrin
-
-
-
-
?
hydrolyzed cassava starch
beta-cyclodextrin
-
-
-
-
?
hydrolyzed corn starch
beta-cyclodextrin
-
-
-
-
?
hydrolyzed corn starch
beta-cyclodextrin
-
-
-
-
?
hydrolyzed potato starch
beta-cyclodextrin
-
-
-
-
?
hydrolyzed potato starch
beta-cyclodextrin
-
-
-
-
?
L-ascorbic acid + maltodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
-
-
-
?
L-ascorbic acid + maltodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
-
-
-
?
L-ascorbic acid + maltodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
-
-
-
?
linear maltooligosaccharide + acceptor
?
-
strain 1011, disproportionation reaction
-
-
r
linear maltooligosaccharide + acceptor
?
-
strain 1011, disproportionation reaction
-
-
r
linear maltooligosaccharide + acceptor
?
-
strain 1011, disproportionation reaction
-
-
r
linear maltooligosaccharide + acceptor
?
-
strain 1011, disproportionation reaction
-
-
r
maltodextrin
beta-cyclodextrin
-
-
main product
-
?
maltodextrin
beta-cyclodextrin
-
-
main product
-
?
maltodextrin
beta-cyclodextrin
-
intramolecular transglycosylation
-
-
?
maltodextrin
beta-cyclodextrin
-
intramolecular transglycosylation
-
-
?
maltodextrin
beta-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase is optimal with maltose as the acceptor substrate. Cyclization reaction and beta-cyclodextrin formation are significantly promoted in the presence of CaCl2. The salt allows the cyclization reaction to be performed at higher temperature
the product of cyclization reaction is predominantly beta-cyclodextrin along with alpha-cyclodextrin as a minor product. The CDs profile is influenced by the reaction conditions. At pH 10, alpha-cyclodextrin is replaced by gamma-cyclodextrin formation
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase is optimal with maltose as the acceptor substrate. Cyclization reaction and beta-cyclodextrin formation are significantly promoted in the presence of CaCl2. The salt allows the cyclization reaction to be performed at higher temperature
the product of cyclization reaction is predominantly beta-cyclodextrin along with alpha-cyclodextrin as a minor product. The CDs profile is influenced by the reaction conditions. At pH 10, alpha-cyclodextrin is replaced by gamma-cyclodextrin formation
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin + alpha-cyclodextrin
38% conversion
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin + alpha-cyclodextrin
38% conversion
-
-
?
maltodextrin + glycosyl acceptor
cyclodextrins
-
-
-
-
?
maltodextrin + glycosyl acceptor
cyclodextrins
-
-
-
-
?
maltodextrin + L-ascorbic acid
2-O-D-glucopyranosyl-L-ascorbic acid + ?
-
-
-
-
?
maltodextrin + L-ascorbic acid
2-O-D-glucopyranosyl-L-ascorbic acid + ?
-
-
-
-
?
maltoheptaose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
-
?
maltoheptaose + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
maltoheptaose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltoheptaose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
-
-
-
r
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
ATCC 21783
-
-
r
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
C31
-
-
?
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
-
-
-
?
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
-
-
-
r
maltose + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
maltose + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
maltose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
-
?
maltose + glycosyl acceptor
beta-cyclodextrin
-
E 192, poor substrate
-
r
maltose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
20% conversion rate
-
-
?
maltose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltotetraose + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
maltotetraose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
r
maltotriose + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
maltotriose + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
maltotriose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
-
?
maltotriose + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
maltotriose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
maltotriose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
naringin + maltodextrin
?
cyclization reaction with naringin as acceptor and maltodextrin as donor
-
-
?
naringin + maltodextrin
?
cyclization reaction with naringin as acceptor and maltodextrin as donor
-
-
?
Paselli starch
beta-cyclodextrin
-
-
78% conversion, 1.9fold higher activity with Paselli starch than with soluble starch
-
?
Paselli starch
beta-cyclodextrin
-
-
78% conversion, 1.9fold higher activity with Paselli starch than with soluble starch
-
?
potato starch + ?
beta-cyclodextrins
-
best substrate giving 13.46 mg/l of cyclodextrins after 1 h of incubation at 60°C
-
-
?
potato starch + ?
beta-cyclodextrins
-
best substrate giving 13.46 mg/l of cyclodextrins after 1 h of incubation at 60°C
-
-
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
worst substrate
-
-
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
worst substrate
-
-
?
potato starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
potato starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
potato starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
potato starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
potato starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
raw corn starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio of beta- to gamma-cyclodextrin products is about 4:1
-
?
raw corn starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio of beta- to gamma-cyclodextrin products is about 4:1
-
?
raw starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
sole products, beta- and gamma-cyclodextrin in a ratio of 80%:20%
-
?
raw starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
sole products, beta- and gamma-cyclodextrin in a ratio of 80%:20%
-
?
rice flour + ?
beta-cyclodextrins
-
-
-
-
?
rice flour + ?
beta-cyclodextrins
-
-
-
-
?
rice starch + glycosyl acceptor
beta-cyclodextrin
-
highest activity
-
-
?
rice starch + glycosyl acceptor
beta-cyclodextrin
-
highest activity
-
-
?
rice starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
rice starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
sago starch + ?
beta-cyclodextrins
-
second best substrate giving 12.96 mg/l of cyclodextrins after 1 h of incubation at 60°C
-
-
?
sago starch + ?
beta-cyclodextrins
-
second best substrate giving 12.96 mg/l of cyclodextrins after 1 h of incubation at 60°C
-
-
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
ratio of products is alpha-cyclodextrin to beta-cyclodextrin to gamma-cyclodextrin 1:0.6:0.3
-
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio for alpha- to beta- to gamma-cyclodextrin 1:1.3:0.5
-
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio for alpha- to beta- to gamma-cyclodextrin 1:1.3:0.5
-
?
soluble potato starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
the native and recombinant enzymes show 45.2% and 43.2% conversion, respectively
-
-
?
soluble potato starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
the native and recombinant enzymes show 45.2% and 43.2% conversion, respectively
-
-
?
soluble potoato starch
cyclodextrin
-
-
-
-
?
soluble potoato starch
cyclodextrin
-
-
-
-
?
soluble starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
at the initial stage of the reaction, alpha-cyclodextrin is the main product. Subsequently, the proportion of beta-cyclodextrin increases and becomes the main product after prolonged incubation. After 10 h or 40 h of incubation, the conversion rates of starch into cyclodextrins are 36.8% or 42.3%, respectively
-
?
soluble starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
at the initial stage of the reaction, alpha-cyclodextrin is the main product. Subsequently, the proportion of beta-cyclodextrin increases and becomes the main product after prolonged incubation. After 10 h or 40 h of incubation, the conversion rates of starch into cyclodextrins are 36.8% or 42.3%, respectively
-
?
soluble starch
beta-cyclodextrin
-
main product
-
?
soluble starch
beta-cyclodextrin
-
main product
-
?
soluble starch
beta-cyclodextrin
-
-
-
-
?
soluble starch
beta-cyclodextrin
-
-
-
-
?
soluble starch
beta-cyclodextrin
-
51.5% conversion
71% of total cyclodextrin formed
-
?
soluble starch
beta-cyclodextrin
-
51.5% conversion
71% of total cyclodextrin formed
-
?
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-fructose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
sufficient activity
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
sufficient activity
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
sufficient activity
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
sufficient activity
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
-
-
-
r
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-galactose
?
-
sufficient activity
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
Bacillus autolyticus
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
Bacillus autolyticus 11149
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
?
soluble starch + D-glucose
cyclodextrins
-
-
-
-
?
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
Bacillus autolyticus
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
Bacillus autolyticus 11149
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-sorbose
?
-
-
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
-
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
-
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
INMIA 1919
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
INMIA 1919
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
INMIA 1919
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
INMIA 1919
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
INMIA 1919
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
INMIA 1919
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
INMIA 1919
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 0.0: 4.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 0.0: 0.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 0.0: 0.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 0.2:9.2:0.6 from gelatinized tapioca starch, 0.2:8.6:1.2 from raw wheat starch
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 4.2: 5.9: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 5.5: 8.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 4.2: 5.9: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 5.5: 8.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 1: 67: 1.6
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain ATCC 21783, pH 4.5-4.7, producing ratio 23.5: 1.0: 1.0, pH 7.0 0.2: 6.0: 1.0, product ratio 2.0:5.0:1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
21783, neutral CGTase, 0.4, 14 and 2.5%
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain 251, product proportions 9: 82: 9 with addition of tert-butanol, 15: 65: 20 without solvent
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
ATCC 21783
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
ATCC 21783
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain 251, product proportions 9: 82: 9 with addition of tert-butanol, 15: 65: 20 without solvent
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
ratio 12: 82: 6
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
ratio 12: 82: 6
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
IFO 3490, product proportions 2.7: 1: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
potato starch, sweet potato starch, rice starch, corn starch, wheat starch
producing ratio 5.0: 2.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
IFO 3490, product proportions 2.7: 1: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product ratio 2.0:5.0:1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 1: 2.4: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 1: 2.4: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product ratios 43% alpha-cyclodextrin, 46% beta-cyclodextrin and 11% gamma-cyclodextrin
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product ratios 43% alpha-cyclodextrin, 46% beta-cyclodextrin and 11% gamma-cyclodextrin
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
potato starch, sweet potato starch, rice starch, corn starch, wheat starch
potato starch, 20 h at 50°C, ratio 8.1: 8.9: 1.0, various conditions, product proportions 1.0: 1.0: 0.3
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
strain NO2
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
strain NO2
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
C31
product ratio 1: 10.5
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
C31
product ratio 1: 10.5
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
60.3% conversion rate with 3% (w/v) soluble starch
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
60.3% conversion rate with 3% (w/v) soluble starch
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
Bacillus autolyticus
-
potato starch, small amounts of alpha- and gamma-cyclodextrin
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
Bacillus autolyticus 11149
-
potato starch, small amounts of alpha- and gamma-cyclodextrin
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
INMIA T42, INMIA A7/1
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
Bacillus sp. (in: Bacteria) Ha3-3-2 / ATCC 39612
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
E 192, waxy maize starch is the best substrate, wheat starch, corn starch, potato starch
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
C31
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
E 192, waxy maize starch is the best substrate, wheat starch, corn starch, potato starch
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
C31
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
E 192, waxy maize starch is the best substrate, wheat starch, corn starch, potato starch
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
INMIA 3849
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
INMIA 3849
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
41.6% conversion
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
45.2% conversion yield
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
45.2% conversion yield
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
tapioca starch is the best substrate
production ratio of beta-cyclodextrin to gamma-cyclodextrin is 0.11/0.89 after 24 h at 60°C, without presence of any selective agents
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
tapioca starch is the best substrate
production ratio of beta-cyclodextrin to gamma-cyclodextrin is 0.11/0.89 after 24 h at 60°C, without presence of any selective agents
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
tapioca starch, wheat starch
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
corn starch
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
corn starch
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
alpha-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
alpha-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cycloheptaamylose
-
No. 5 strain
-
r
soluble starch + glycosyl acceptor
cycloheptaamylose
-
No. 5 strain
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
strain no.313
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
strain no.313
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
-
alpha-cyclodextrin production is not observed at any pH examined. The enzyme produces gamma-cyclodextrin principally at any pH and the ratio of gamma-cyclodextrin to beta-cyclodextrin is always more than 1.7 and 4.7 with 1% and 10% substrate
-
?
soluble starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
-
alpha-cyclodextrin production is not observed at any pH examined. The enzyme produces gamma-cyclodextrin principally at any pH and the ratio of gamma-cyclodextrin to beta-cyclodextrin is always more than 1.7 and 4.7 with 1% and 10% substrate
-
?
soluble starch + glycosyl acceptor
maltose + maltotriose + maltotetraose + maltopentaose
-
-
-
r
soluble starch + glycosyl acceptor
maltose + maltotriose + maltotetraose + maltopentaose
-
-
-
r
soluble starch + glycosyl acceptor
maltose + maltotriose + maltotetraose + maltopentaose
-
-
-
r
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
-
-
?
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
ATCC 21783
-
-
?
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
ATCC 21783
-
-
r
soluble starch + glycosyl acceptor
Schardinger dextrins
-
-
-
?
soluble starch + glycosyl acceptor
Schardinger dextrins
-
-
-
-
r
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
-
?
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
?
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
-
?
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
?
soluble starch + H2O
cyclodextrins
-
-
-
-
?
soluble starch + H2O
cyclodextrins
-
potato starch
-
-
?
soluble starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
soluble starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
soluble starch + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
-
?
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
soluble starch + sucrose
?
-
-
-
-
r
starch
beta-cyclodextrin
-
intramolecular transglycosylation
-
-
?
starch
beta-cyclodextrin
-
intramolecular transglycosylation
-
-
?
starch
beta-cyclodextrin
-
-
-
?
starch
beta-cyclodextrin
-
-
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
86% beta-cyclodextrin and 14% of gamma-cyclodextrin are produced after 24 h incubation at 60°C, without adding any selective agent, in 0.1 M phosphate buffer
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
86% beta-cyclodextrin and 14% of gamma-cyclodextrin are produced after 24 h incubation at 60°C, without adding any selective agent, in 0.1 M phosphate buffer
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
-
the maximum starch conversion to beta-cyclodextrin and gamma-cyclodextrin is 29% and 38%, for the immobilized and soluble enzyme, respectively
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar production profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
to manipulate the product specificity of the Paenibacillus sp. A11 and Bacillus macerans cyclodextrin glycosyltransferases towards the preferential formation of gamma-cyclodextrin (CD8), crosslinked imprinted protein of cyclodextrin glycosyltransferase is prepared by applying enzyme imprinting and immobilization methodologies. The native enzyme produces CD6:CD7:CD8:CD9 ratios of 43:36:21:0 at 40°C. The size of the synthesis products formed bythe crosslinked imprinted cyclodextrin glycosyltransferases is shifted towards CD8 and CD9, and the overall cyclodextrin yield is increased by 12% compared to the native enzymes
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
to manipulate the product specificity of the Paenibacillus sp. A11 and Bacillus macerans cyclodextrin glycosyltransferases towards the preferential formation of gamma-cyclodextrin (CD8), crosslinked imprinted protein of cyclodextrin glycosyltransferase is prepared by applying enzyme imprinting and immobilization methodologies. The native enzyme produces CD6:CD7:CD8:CD9 ratios of 15:65:20:0 at 40°C. The size of the synthesis products formed by the crosslinked imprinted cyclodextrin glycosyltransferases is shifted towards CD8 and CD9, and the overall cyclodextrin yield is increased by 12% compared to the native enzymes
-
-
?
starch
cyclodextrin
-
to manipulate the product specificity of the Paenibacillus sp. A11 and Bacillus macerans cyclodextrin glycosyltransferases towards the preferential formation of gamma-cyclodextrin (CD8), crosslinked imprinted protein of cyclodextrin glycosyltransferase is prepared by applying enzyme imprinting and immobilization methodologies. The native enzyme produces CD6:CD7:CD8:CD9 ratios of 15:65:20:0 at 40°C. The size of the synthesis products formed by the crosslinked imprinted cyclodextrin glycosyltransferases is shifted towards CD8 and CD9, and the overall cyclodextrin yield is increased by 12% compared to the native enzymes
-
-
?
starch
cyclodextrin
-
in acetatebuffer, pH 6.0, 60°C, the CGTase produces pre dominantly beta-cyclodextrin from either raw or gelatinized sago (Cycas revoluta) starch. Changing the buffer from acetate to phosphate reduces the yield of beta-cyclodextrin from 2.48 to 1.42 mg/ml, production of both alpha- and beta-cyclodextrins are more pronounced. The decrease in the production of cyclodextrins in phosphate buffer is significant at both pH 6.0 and 7.0. Changing the buffer to Tris/HCl (pH 7.0) shows a significant increase in beta-cyclodextrin production
-
-
?
starch
gamma-cyclodextrin
-
-
-
-
?
starch
gamma-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
-
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
-
?
starch + stevioside
glycosyl stevioside
-
-
-
-
r
starch + stevioside
glycosyl stevioside
-
-
-
-
r
starch + stevioside
glycosyl stevioside
-
extrusion starch, raw starch and liquefied starch as glucosyl donor
-
-
r
starch + sucrose
maltooligosyl sucrose
-
-
-
r
starch + sucrose
maltooligosyl sucrose
-
-
-
r
stevioside + beta-cyclodextrin
4'-O-alpha-D-glycosyl stevioside + 4''-O-alpha-D-maltosyl stevioside + ?
-
1,4-intermolecular transglycosylation, the substrate is an entkaurene diterpene glycoside, and is a constituent in Stevia rebaudiana leaves. It has therapeutic importance as substitute of sugar for diabetics. Enhancement of thre reaction under microwave assisted reaction, overview
formed to 66% and 24%, respectively, product identification by detailed NMR, LC-MS/MS studies
-
?
stevioside + beta-cyclodextrin
4'-O-alpha-D-glycosyl stevioside + 4''-O-alpha-D-maltosyl stevioside + ?
-
1,4-intermolecular transglycosylation, the substrate is an entkaurene diterpene glycoside, and is a constituent in Stevia rebaudiana leaves. It has therapeutic importance as substitute of sugar for diabetics. Enhancement of thre reaction under microwave assisted reaction, overview
formed to 66% and 24%, respectively, product identification by detailed NMR, LC-MS/MS studies
-
?
stevioside + maltodextrin
?
-
the enzyme from strain BL-12 is more suitable for transglycosylation than the cyclization reaction, and is specific for the intermolecular transglycosylation of stevioside with maltodextrin as the most suitable glycosyl donor
-
-
?
stevioside + maltodextrin
?
-
the enzyme from strain BL-12 is more suitable for transglycosylation than the cyclization reaction, and is specific for the intermolecular transglycosylation of stevioside with maltodextrin as the most suitable glycosyl donor
-
-
?
stevioside + starch
?
-
soluble, extrusion, or potato starch
-
-
?
stevioside + starch
?
-
soluble, extrusion, or potato starch
-
-
?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
best substrate, the enzyme is preferentially forming alpha- (50%) and beta-cyclodextrin (40%) in the cyclization reaction using wheat starch as substrate
-
-
?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
best substrate, the enzyme is preferentially forming alpha- (50%) and beta-cyclodextrin (40%) in the cyclization reaction using wheat starch as substrate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
D-glucuronate is ineffective as acceptor
-
-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
D-glucuronate is ineffective as acceptor
-
-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
D-glucuronate is ineffective as acceptor
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces beta-cyclodextrins
-
-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces beta-cyclodextrins
-
-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
additional information
?
-
-
no activity with D-glucose
-
-
?
additional information
?
-
-
no activity with D-glucose
-
-
?
additional information
?
-
-
the immobilized enzyme, of both strains, as membrane biocatalysts forms mainly beta- and gamma-cyclodextrins after 6 h enzyme reaction at pH 9.0 of the reaction mixture, 35-37% of the reaction products formed are gamma-cyclodextrins
-
-
?
additional information
?
-
-
increasing substrate concentrations (0.5%-20.0%) and glucans containing branching points (alpha-1,6-glycosidic linkages) shift the product pattern to: beta-cyclodextrin > alpha-cyclodextrin > gamma-cyclodextrin
-
-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Anaerobranca gottschalkii produces alpha-cyclodextrins
-
-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
-
-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
additional information
?
-
Bacillus autolyticus
-
sorbitol, mannitol, xylulose, galactose, fructose, lactose, glycerol and arabinose are not acceptors
-
-
?
additional information
?
-
Bacillus autolyticus 11149
-
sorbitol, mannitol, xylulose, galactose, fructose, lactose, glycerol and arabinose are not acceptors
-
-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus lichenifoormis produces alpha- and beta-cyclodextrins
-
-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus obhensis produces beta-cyclodextrins
-
-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
additional information
?
-
-
isolation of alkaliphilic Bacillus strains and determination of their phylogenetic and phenotypic characteristics, overview
-
-
?
additional information
?
-
-
glycosyl donor specificity for intermolecular transglycosylation of stevioside, overview, cyclization reaction with soluble starch as substrate
-
-
?
additional information
?
-
the enzyme from strain BL-31 is highly specific for the intermolecular transglycosylation of bioflavonoids, with high specificities for glycosyl acceptor bioflavonoids, including naringin, rutin, and hesperidin, and especially naringin
-
-
?
additional information
?
-
-
the enzyme from strain BL-31 is highly specific for the intermolecular transglycosylation of bioflavonoids, with high specificities for glycosyl acceptor bioflavonoids, including naringin, rutin, and hesperidin, and especially naringin
-
-
?
additional information
?
-
-
the enzyme produces cyclodextrins from starch, enzymes from strains 20RF and 8SB Bacillus strains form only two types of cyclodextrins, beta and gamma
-
-
?
additional information
?
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
?
additional information
?
-
-
production of beta-cyclodextrin
-
-
?
additional information
?
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview
-
-
?
additional information
?
-
-
substrate is soluble starch, formation of beta-cyclodextrins
-
-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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glycosyl donor specificity for intermolecular transglycosylation of stevioside, overview, cyclization reaction with soluble starch as substrate
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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?
additional information
?
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-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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the enzyme from strain BL-31 is highly specific for the intermolecular transglycosylation of bioflavonoids, with high specificities for glycosyl acceptor bioflavonoids, including naringin, rutin, and hesperidin, and especially naringin
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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substrate is soluble starch, formation of beta-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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?
additional information
?
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-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Brevibacillus brevis produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Brevibacillus brevis produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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the enzyme shows cyclization activity on different raw and hydrolyzed starches, hydrolyzed cornstarch gives the highest activity. The enzyme from strain 7b mainly forms beta-cyclodextrin, but also alpha- and gamma-cyclodextrins, from maltodextrin, influence of substrate concentration on CGTase activity, overview
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produce beta-cyclodextrins, except for strain 290-3 that also produces gamma-cyclodextrins
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additional information
?
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the extracelluar enzyme converts starch into non-reducing, cyclic malto-oligosacchrarides called cyclodextrins
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additional information
?
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assay method optimization, the optimum ratio of stevioside to beta-cyclodextrin for optimum transglycosylation is 1:2, overview
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?
additional information
?
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substrate is gelatinized soluble starch
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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-
assay method optimization, the optimum ratio of stevioside to beta-cyclodextrin for optimum transglycosylation is 1:2, overview
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?
additional information
?
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the enzyme shows cyclization activity on different raw and hydrolyzed starches, hydrolyzed cornstarch gives the highest activity. The enzyme from strain 7b mainly forms beta-cyclodextrin, but also alpha- and gamma-cyclodextrins, from maltodextrin, influence of substrate concentration on CGTase activity, overview
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?
additional information
?
-
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when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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?
additional information
?
-
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces 80% gamma-cyclodextrins with an overall conversion of starch into cyclodextrins of 14%
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?
additional information
?
-
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces 80% gamma-cyclodextrins with an overall conversion of starch into cyclodextrins of 14%
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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?
additional information
?
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?
additional information
?
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?
additional information
?
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?
additional information
?
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?
additional information
?
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?
additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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?
additional information
?
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disaccharides are not substrates, except maltose
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additional information
?
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isomaltose, sucrose, melibiose, phenyl-alpha-D-glucoside, cellobiose and lactose are not acceptors, L-ascorbic acid-2-O-phosphate and, L-ascorbic acid-2-O-sulfate are not substrates
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?
additional information
?
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CGTase catalyzes the transfer of dextrin units from cyclodextrins or longer dextrins to polyols, such as glycerol, sugars, and flavonoids
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?
additional information
?
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces alpha- and beta-cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Geobacillus stearothermophilus produces beta-cyclodextrins
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?
additional information
?
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CGTase transfers glycosyl residues from dextrin, maltosides with an alkyl side chain of C4, C8, C12, to the maltosides of butanol, octanol, and lauryl alcohol generating maltosides with 3-4 glucose units, substrate specificity, overview. Product identification with TLC, NMR, and ESI mass spectrometry
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?
additional information
?
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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-
no activity with D-glucose as glycosyl donor
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-
additional information
?
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-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces alpha- and beta-cyclodextrins
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?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Geobacillus stearothermophilus produces beta-cyclodextrins
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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?
additional information
?
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
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?
additional information
?
-
cyclization is the predominant activity, followed by hydrolysis and to a lesser extent coupling and disproportionation activities
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?
additional information
?
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-
cyclization is the predominant activity, followed by hydrolysis and to a lesser extent coupling and disproportionation activities
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?
additional information
?
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-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Klebsiella pneumoniae produces alpha-cyclodextrins
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-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview
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-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview
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?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Klebsiella pneumoniae produces alpha-cyclodextrins
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
in addition to the intramolecular transglycosylation and cyclization producing beta-cyclodextrins, using maltodextrin and starch as substrates, the CGTase shows disproportionation and coupling activities, intermolecular transglycosylation reactions. The enzyme produces alpha-, beta-, and gamma-cyclodextrins in the ratio of 0.40:1:0.45. Activity with different starch types, overview
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?
additional information
?
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?
additional information
?
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-
?
additional information
?
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-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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-
?
additional information
?
-
-
ATCC 21783 contains 3 types of enzymes, acid, neutral and alcaline
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?
additional information
?
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-
glucose is no substrate
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?
additional information
?
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-
no reaction with p-nitrophenyl-glucose and p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose, heptakis(2,6-di-O-methyl)-beta cyclodextrin is not transformed
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?
additional information
?
-
beta-cyclodextrin-forming activity from partially hydrolyzed potato starch with an average degree of polymerization of 50. Disproportionation activity is determined using 4-nitrophenyl-beta-D-maltoheptaoside-4-6-O-ethylidene, i.e. pNPG7, as substrate
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-
?
additional information
?
-
conversion of starch into beta- and gamma-cyclodextrins in a ratio 73:27
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-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Bacillus circulans strans produce beta-cyclodextrins, except for strain DF 9R that also produces alpha-cyclodextrins
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?
additional information
?
-
CGTase catalyzes the formation of cyclomaltooligosaccharides, cyclic molecules formed by alpha-(1,4)-linked D-glucopyranosyl units with an apolar central cavity and a hydrophilic outer surface. alpha-, beta-Cyclizing and amylolytic activities withpotato starch as substrate, enzyme structure-function relationship, overview
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-
?
additional information
?
-
-
formation of alpha-, beta-, and gamma-cyclodextrins from starch and matotriose
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-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme from strain BC251 also shows hydrolytic activity on potato starch. Substrate binding structure of the strain BC251 enzyme, overview
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-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
?
additional information
?
-
-
-
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-
?
additional information
?
-
-
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-
?
additional information
?
-
beta-cyclodextrin-forming activity from partially hydrolyzed potato starch with an average degree of polymerization of 50. Disproportionation activity is determined using 4-nitrophenyl-beta-D-maltoheptaoside-4-6-O-ethylidene, i.e. pNPG7, as substrate
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additional information
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glucose is no substrate
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additional information
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no reaction with p-nitrophenyl-glucose and p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose, heptakis(2,6-di-O-methyl)-beta cyclodextrin is not transformed
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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formation of alpha-, beta-, and gamma-cyclodextrins from starch and matotriose
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additional information
?
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CGTase catalyzes the formation of cyclomaltooligosaccharides, cyclic molecules formed by alpha-(1,4)-linked D-glucopyranosyl units with an apolar central cavity and a hydrophilic outer surface. alpha-, beta-Cyclizing and amylolytic activities withpotato starch as substrate, enzyme structure-function relationship, overview
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additional information
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glucose is no substrate
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additional information
?
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no reaction with p-nitrophenyl-glucose and p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose, heptakis(2,6-di-O-methyl)-beta cyclodextrin is not transformed
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additional information
?
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CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional
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additional information
?
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cyclization with maltodextrin as substrate
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus campinasensis produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional
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additional information
?
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cyclization with maltodextrin as substrate
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus campinasensis produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus graminis produces alpha- and beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus graminis produces alpha- and beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus illinoisensis produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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the native enzyme does not convert king oyster mushroom powder and enoki mushroom powder, while recombinant enzyme converts king oyster mushroom powder and enoki mushroom powder to beta-cyclodextrin
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus illinoisensis produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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the native enzyme does not convert king oyster mushroom powder and enoki mushroom powder, while recombinant enzyme converts king oyster mushroom powder and enoki mushroom powder to beta-cyclodextrin
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additional information
?
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additional information
?
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additional information
?
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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D-galactose, D-ribose, D-mannose, D-arabinose and D-fructose do not contribute as glucosyl acceptor
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additional information
?
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when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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additional information
?
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CGTase produces alpha-, beta-, and gamma-cyclodextrins from soluble starch, overview
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additional information
?
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CGTase produces alpha-, beta-, and gamma-cyclodextrins from soluble starch, overview
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additional information
?
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CGTase is an extracellular enzyme capable of converting starch or starch derivatives into cyclodextrins through an intramolecular transglycosylation reaction. Cyclodextrins are cyclic, nonreducing oligoglucopyranose molecules linked via alpha(1,4)-glycosidic bonds
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus macerans produces alpha-cyclodextrins
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additional information
?
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Asp372 and Tyr89 at subsite -3 play important roles in cyclodextrin product specificity of CGTase. Comparison of alpha-, beta- and gamma-cyclization specificity of wild-type and mutant enzymes, overview
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?
additional information
?
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CGTases function according to an alpha-retaining double displacement mechanism with a covalent glycosyl-enzyme intermediate. Efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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synthesis of 3-O-alpha-D-glucopyranosyl dopamine and 4-O-alpha-D-glucopyranosyl dopamine, and of 3-O-alpha-D-glucopyranosyl L-DOPA and 4-O-alpha-D-glucopyranosyl L-DOPA by reaction with cyclomaltohexaose catalyze by the CGTase using dopamine-HCl or imidazolium-HCl and glucose or maltose as substrates, maltodextrin chains attached to dopamine, overview. Determination of the reaction products by MALDI-TOF MS and NMR, molecular structure of the dopamine-glycosides, overview
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additional information
?
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the enzyme performs formation of alpha-, beta- and gamma-cyclodextrin. Lys47 is important for the alpha-cyclization reaction. Enhancement of beta-cyclodextrin specificity might be due to weakening or removal of hydrogen-bonding interactions between the side chain of residue 47 and the bent intermediate specific for alpha-cyclodextrin formation
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additional information
?
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the enzyme shows alpha-cyclodextrin forming activity with soluble starch
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additional information
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no activity with D-glucose as glycosyl donor
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additional information
?
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when using genistein plus D-glucose and sucrose as glycosyl donors, there is hardly detected any transglycosylation product
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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when using genistein plus D-glucose and sucrose as glycosyl donors, there is hardly detected any transglycosylation product
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additional information
?
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when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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?
additional information
?
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CGTase is an extracellular enzyme capable of converting starch or starch derivatives into cyclodextrins through an intramolecular transglycosylation reaction. Cyclodextrins are cyclic, nonreducing oligoglucopyranose molecules linked via alpha(1,4)-glycosidic bonds
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additional information
?
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the enzyme shows alpha-cyclodextrin forming activity with soluble starch
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?
additional information
?
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the enzyme performs formation of alpha-, beta- and gamma-cyclodextrin. Lys47 is important for the alpha-cyclization reaction. Enhancement of beta-cyclodextrin specificity might be due to weakening or removal of hydrogen-bonding interactions between the side chain of residue 47 and the bent intermediate specific for alpha-cyclodextrin formation
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additional information
?
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production of beta-cyclodextrin from potato starch
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additional information
?
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the main amino acid residues of cyclization activity are Lys47, Tyr89, Asn94, Phe183, Asn193, Leu194, Tyr195, Asp196, Phe259, Phe283, and Asp371
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus pabuli produces beta-cyclodextrins
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?
additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus pabuli produces beta-cyclodextrins
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?
additional information
?
-
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
production of beta-cyclodextrin from potato starch
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?
additional information
?
-
the main amino acid residues of cyclization activity are Lys47, Tyr89, Asn94, Phe183, Asn193, Leu194, Tyr195, Asp196, Phe259, Phe283, and Asp371
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?
additional information
?
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the main amino acid residues of cyclization activity are Lys47, Tyr89, Asn94, Phe183, Asn193, Leu194, Tyr195, Asp196, Phe259, Phe283, and Asp371
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?
additional information
?
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soluble potato starch, cellobiose, and cyclodextrins as substrates, cyclodextrin product spectrum of native and recombinant enzymes, overview
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus sp. strains produce alpha- and beta-cyclodextrins
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
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no activity with D-glucose as glycosyl donor
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-
-
additional information
?
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the enzyme preforms cyclization of different alpha-1,4-glucans, e.g. soluble potato starch, or amylopectin, and amylose, the enzyme forms preferably beta-cyclodextrins, the ratio of products is 27:68:5 for alpha, beta, and gamma cyclodextrins
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?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus megaterium produces beta-cyclodextrins
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
the enzyme produces alpha-, beta-, and gamma-cyclodextrins from starch
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?
additional information
?
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the enzyme produces alpha-, beta-, and gamma-cyclodextrins from starch, product ratios depend on the duration of the process. The enzyme also shows coupling activity and is able to degrade high concentrations of beta-cyclodextrin and to transform different types of cyclodextrins one into another. Native corn starch and soluble potato starch as substrates, product determination by thin layer chromatography
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?
additional information
?
-
reversible cyclization reaction with alpha-1,4-glucans, e.g. starch, the major final product of PFCGT cyclization is beta-cyclodextrin, and thus the enzyme is a beta-CGTase
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?
additional information
?
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reversible cyclization reaction with alpha-1,4-glucans, e.g. starch, the major final product of PFCGT cyclization is beta-cyclodextrin, and thus the enzyme is a beta-CGTase
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?
additional information
?
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-
cyclization activity forming cyclodextrins from starch
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?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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-
?
additional information
?
-
-
D-glucuronate is ineffective as acceptor
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?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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?
additional information
?
-
-
D-glucuronate is ineffective as acceptor
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?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus agaradhaerens produces beta-cyclodextrins
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus agaradhaerens produces beta-cyclodextrins
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?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Thermoanaerobacter sp. strains produce alpha- and beta-cyclodextrins
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?
additional information
?
-
-
CGTases function according to an alpha-retaining double displacement mechanism with a covalent glycosyl-enzyme intermediate. Synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase
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?
additional information
?
-
-
cyclodextrin glycosyltransferase produces a mixture of alpha-, beta-, and gamma-cyclodextrins from starch
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?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high also shows hydrolytic activity on potato starch
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-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
?
additional information
?
-
-
the enzyme primarily catalyses the formation of cyclic alpha-1,4-linked cyclodextrins from starch. This enzyme also possesses unusually high hydrolytic activity as a side reaction, thought to be due to partial retention of ancestral enzyme function. Product formation, alpha-, beta-, and gamma-cyclodextrins, of wild-type and mutant enzymes, substrate-binding subsites of CGTase, and sugar binding structure, overview
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-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
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-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high hydrolytic activity on potato starch
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-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
?
additional information
?
-
-
the enzyme primarily catalyses the formation of cyclic alpha-1,4-linked cyclodextrins from starch. This enzyme also possesses unusually high hydrolytic activity as a side reaction, thought to be due to partial retention of ancestral enzyme function. Product formation, alpha-, beta-, and gamma-cyclodextrins, of wild-type and mutant enzymes, substrate-binding subsites of CGTase, and sugar binding structure, overview
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-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high hydrolytic activity on potato starch
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-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
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-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
?
additional information
?
-
pullulan is no substrate
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-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
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-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
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reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
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additional information
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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F183L
-
strain 1011, decreases affinity of acarbose
F259L
-
strain 1011, decreases affinity of acarbose
F283Y
-
mutation decreases the enzymatic activity in the basic pH range
H233Y
the mutant primarily produces maltoheptaose using beta-cyclodextrin via a hydrolysis reaction. The mutant enzyme also shows hydrolyzing activity against gamma-cyclodextrin but is unable to catalyze the hydrolysis of alpha-cyclodextrin
N132R
introduction of an ionic interaction at the first Ca2+ site, disruption of catalytic activity
N28R
introduction of an additional ionic interaction at the second Ca2+ site, mutant displays increased cyclization activity
S182E
mutation adjacent to the first Ca2+ site and the active site cleft. Mutant shows enhanced thermostability, and decreased catalytic activity
S182G
mutation adjacent to the first Ca2+ site and the active site cleft. Increase in half-life at 60°C to 94 min
Y195I
-
the mutant produces less alpha-cyclodextrin, slightly more beta-cyclodextrin, and 3-4times more gamma-cyclodextrin than the wild type enzyme
Y93F
-
the substitution causes no alpha-cyclodextrin formation, but produces 6% more beta-cyclodextrin, 16% less gamma-cyclodextrin, and decreases its kcat and kcat/Km values
F183L
-
strain 1011, decreases affinity of acarbose
-
F259L
-
strain 1011, decreases affinity of acarbose
-
F283L
-
starch degrading activity is similar to that of wild-type enzyme between the acidic and neutral pH ranges but decreases to 10% at pH 10.0. The pH-value of half-maximal activity at basic pH side is shifted to 8.6 from 10.0 of the wild-type. 23%-67% decrease in KM-value for 3-ketobutylidene-beta-2-chloro-4-nitrophenylmalto-pentaoside in the disproportionation reaction. The turnover-number for the disproportionating reaction at various pH conditions decreases to 1.6% to 4.4% compared with those of wild-type enzyme
-
F283Y
-
mutation decreases the enzymatic activity in the basic pH range
-
F183L
-
strain 1011, decreases affinity of acarbose
-
F259L
-
strain 1011, decreases affinity of acarbose
-
Y195I
-
the mutant produces less alpha-cyclodextrin, slightly more beta-cyclodextrin, and 3-4times more gamma-cyclodextrin than the wild type enzyme
-
Y93F
-
the substitution causes no alpha-cyclodextrin formation, but produces 6% more beta-cyclodextrin, 16% less gamma-cyclodextrin, and decreases its kcat and kcat/Km values
-
F183L
-
strain 1011, decreases affinity of acarbose
-
F259L
-
strain 1011, decreases affinity of acarbose
-
N132R
-
introduction of an ionic interaction at the first Ca2+ site, disruption of catalytic activity
-
N28R
-
introduction of an additional ionic interaction at the second Ca2+ site, mutant displays increased cyclization activity
-
S182E
-
mutation adjacent to the first Ca2+ site and the active site cleft. Mutant shows enhanced thermostability, and decreased catalytic activity
-
S182G
-
mutation adjacent to the first Ca2+ site and the active site cleft. Increase in half-life at 60°C to 94 min
-
H233Y
-
the mutant primarily produces maltoheptaose using beta-cyclodextrin via a hydrolysis reaction. The mutant enzyme also shows hydrolyzing activity against gamma-cyclodextrin but is unable to catalyze the hydrolysis of alpha-cyclodextrin
-
D358R
the mutant forms mainly cyclodextrins with 8-12 glucose units during a reaction time of 24 h from soluble starch
Y183R
the mutant has completely lost its ability to synthesize beta-cyclodextrin from soluble starch, and gamma-cyclodextrin and the larger cyclodextrins are the only cyclic oligosaccharides produced
Y183R/D358R
the mutant almost completely loses its cyclization activity (1.3% activity compared to the wild type enzyme)
Y183W
the mutant mainly produces gamma-cyclodextrin from soluble starch
Y183W/D358R
the mutant shows very low beta-cyclodextrin cyclization activity and an increased formation of the larger cyclodextrins
D355R
the mutant shows 164% of wild type activity, and the mutation does not have significant negative effect on stability when compared to the wild type
R254F
the mutant shows 196% of wild type activity, and the mutation does not have significant negative effect on stability when compared to the wild type
Y127F
the mutant shows 210% of wild type activity, and the mutation does not have significant negative effect on stability when compared to the wild type
P176I
-
the mutant is increased by 9.4 % on cyclodextrin production, indicating replacement of hydrophobic amino acids significantly improve in cyclization activity
P176K
-
the substrate affinity of the mutant is increased by 14% and the catalytic efficiency is increased by 14% compared to the wild type
P176L
-
the mutant is increased by 7.9 % on cyclodextrin production, indicating replacement of hydrophobic amino acids significantly improve in cyclization activity
DELTA154160
-
mutation increases cyclization activity around 1.5times without any significant reduction of coupling and hydrolyzing activities, conversion yield into cyclodextrins is 39% higher than that of wild-type enzyme without any recognizable change in cyclodextrin ratio. pH-Stability decreases drastically in acidic pH region. Decrease in thermal stability
Y96M
-
mutation increases cyclization activity around 1.5times without any significant reduction of coupling and hydrolyzing activities, conversion yield into cyclodextrins is 28.6% higher than that of wild-type enzyme without any recognizable change in cyclodextrin ratio. Decrease in thermal stability
A223H
-
mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223K
-
mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223R
-
mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5
A223H
-
mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
-
A223K
-
mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
-
A223R
-
mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5
-
F191Y
-
Phe at position 191 replaced by Tyr
F255I
-
cyclodextrins undetectable
I631T
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
I641T
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
K647E
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
F191Y
-
Phe at position 191 replaced by Tyr
-
I631T
-
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
-
I641T
-
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
-
K647E
-
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
-
F191Y
-
Phe at position 191 replaced by Tyr
-
A230V
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
A315D
-
the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability
D577E
-
the mutant displays an 11.2% increase in the beta-cyclization activity compared to the wild type enzyme
D577H
-
the mutant displays a slight decrease in the beta-cyclization activity compared to the wild type enzyme
F283L
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
H140Q
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 11.6 min for the mutant enzyme
K232E
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
K427S/V615L
reduction of cyclodextrin-forming activity
L600E
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600I
the mutant shows decreased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600R
the mutant shows increased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600Y
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
N188D
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 35 min for the mutant enzyme
N188D/K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 56 min for the mutant enzyme
Q179G
-
mutation to residue G which is conserved in all the corresponding enzymes except in that from Bacillus circulans Df 9R. Activity and kinetic parameters remain unchanged
Q179L
-
mutation results in a different ratio of cyclodextrin products with a ratio for alpha- to beta- to gamma-cyclodextrin 1:1.7:0.7, a lower catalytic efficiency, and a decreased ability to convert starch into cyclodextrins
T185S
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 14.8 min for the mutant enzyme
T186Y
-
decrease in half-life at 60°C from 9.7 min for the wild-type enzyme to 8 min for the mutant enzyme
Y89D
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14.3% and 17.6%, respectively
Y89D/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14% and 35.1%, respectively
Y89G
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 10.6% and 14.6%, respectively
Y89G/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 25% and 29.3%, respectively
Y89N
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 8.9% and 13%, respectively
Y89N/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 19.4% and 25.2%, respectively
A230V
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
F283L
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
H140Q
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
K232E
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
K427S/V615L
-
reduction of cyclodextrin-forming activity
-
Q179G
-
mutation to residue G which is conserved in all the corresponding enzymes except in that from Bacillus circulans Df 9R. Activity and kinetic parameters remain unchanged
-
Q179L
-
mutation results in a different ratio of cyclodextrin products with a ratio for alpha- to beta- to gamma-cyclodextrin 1:1.7:0.7, a lower catalytic efficiency, and a decreased ability to convert starch into cyclodextrins
-
D577E
-
the mutant displays an 11.2% increase in the beta-cyclization activity compared to the wild type enzyme
-
D577H
-
the mutant displays a slight decrease in the beta-cyclization activity compared to the wild type enzyme
-
D577K
-
the mutant displays a 1.5% increase in the beta-cyclization activity compared to the wild type enzyme
-
L600E
-
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
L600I
-
the mutant shows decreased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
L600R
-
the mutant shows increased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
L600Y
-
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
Y89D
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14.3% and 17.6%, respectively
-
Y89D/D577R
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14% and 35.1%, respectively
-
Y89G/D577R
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 25% and 29.3%, respectively
-
Y89N
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 8.9% and 13%, respectively
-
A137V
-
the mutation produces a perturbation in the catalytic site of the enzyme which correlates with a 10fold reduction in its catalytic efficiency. Moreover, this mutant shows increased production of maltooligosaccharides with a high degree of polymerization, mostly maltopentaose to maltoheptaose
A144V
-
the mutant shows slightly reduced activity compared to the wild type enzyme
L280A
-
the mutant displays an about 30% reduction in its catalytic efficiency as compared to the wild type enzyme
M329I
-
the mutant shows slightly reduced activity compared to the wild type enzyme
A137V
-
the mutation produces a perturbation in the catalytic site of the enzyme which correlates with a 10fold reduction in its catalytic efficiency. Moreover, this mutant shows increased production of maltooligosaccharides with a high degree of polymerization, mostly maltopentaose to maltoheptaose
-
A144V
-
the mutant shows slightly reduced activity compared to the wild type enzyme
-
L280A
-
the mutant displays an about 30% reduction in its catalytic efficiency as compared to the wild type enzyme
-
M329I
-
the mutant shows slightly reduced activity compared to the wild type enzyme
-
A156V
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A156V/A166Y
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A156V/L174P
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A156V/L174P/A166Y
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A166Y
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A166Y/L174P
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
D372K
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
D372K/Y89R
-
site-directed mutagenesis, the mutant enzyme shows a 1.5fold increase in the production of alpha-cyclodextrin, with a concomitant 43% decrease in the production of beta-cyclodextrin compared to the wild-type CGTase
K47F
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 30% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47H
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47R
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47S
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47T
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47V
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 48% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47W
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 24% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
L174P
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
Q265K/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme
R146A/D147P
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 75.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
R146P/D147A
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 76.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
Y195I
-
the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins
Y195S/Q265K
-
compared with the wild type enzyme, the mutant has no cyclization activity and 498% hydrolysis and disproportionation activity
Y195S/Y260R
-
compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y260R/Q265K
-
compared with the wild type enzyme, the mutant has 8% cyclization activity and 213% hydrolysis activity
Y260R/Q265K/Y195S
-
the mutant shows 12% cyclization (alpha-cyclodextrin-forming) and 557% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y260R/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 492% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y89D
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89K
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89N
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89R
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
Y195I
-
the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins
-
K47H
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47L
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47R
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47S
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47T
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
Q265K
-
the mutant shows 15% cyclization (alpha-cyclodextrin-forming) and 236% hydrolysis (starch-degrading) activities compared to the wild type enzyme
-
A315D
the mutation decreases starch conversion activity. The mutant exhibits the highest thermostability at 60-70°C for 30 min compared to the wild type enzyme
A315H
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
A315R
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
A315S
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
H233D
the mutation decreases starch conversion activity
S145D
the mutation decreases starch conversion activity
S145G
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
S145P
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y100A
the mutation decreases starch conversion activity
Y100D
the mutation decreases starch conversion activity
Y100I
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y100T
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y167H
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y195A
the mutation strongly decreases starch conversion activity
Y195E
the mutation decreases starch conversion activity
Y195T
the mutation decreases starch conversion activity
Y195V
the mutation decreases starch conversion activity
Y89S
the mutation decreases starch conversion activity
synthesis
-
immobilization of enzyme on mesoporous silica microspheres produces high yields of immobilization, up to 83%, and activity recoveries, up to 73%. The soluble enzyme and its immobilized form show similar values for the optimal pH activity, while optimal reaction temperatures are 100°C and 80°C, respectively. The immobilized enzyme shows similar values for Km and thermal stabilities as the soluble form, while its Vmax is lower. The immobilized enzyme was tested in repeated batches in order to simulate recovery and reuse, keeping about 60% of the initial catalytic activity after 15 cycles
S77P
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, molecular modelling of the location and effect of S77P mutation on the Tabium CGTase active-site conformation
W239L
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
W239R
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
S77P
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, molecular modelling of the location and effect of S77P mutation on the Tabium CGTase active-site conformation
-
W239L
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
-
W239R
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
-
F283L
-
strain 1011, decreases affinity of acarbose
F283L
-
starch degrading activity is similar to that of wild-type enzyme between the acidic and neutral pH ranges but decreases to 10% at pH 10.0. The pH-value of half-maximal activity at basic pH side is shifted to 8.6 from 10.0 of the wild-type. 23%-67% decrease in KM-value for 3-ketobutylidene-beta-2-chloro-4-nitrophenylmalto-pentaoside in the disproportionation reaction. The turnover-number for the disproportionating reaction at various pH conditions decreases to 1.6% to 4.4% compared with those of wild-type enzyme
Y195L
-
strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
Y195L
-
strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
-
Y195L
-
strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
-
Y195L
-
strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
-
P176G
-
compared to the wild type, the mutant shows 10.4% improvement in conversion from starch to cyclodextrins, whose beta-cyclodextrin yield increases by 6% and alpha-cyclodextrin yield decreases by 8%
P176G
-
the substrate affinity of the mutant is increased by 13% compared to the wild type
D577A
-
the mutation increases the beta-cyclization activity of the enzyme with 23% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
D577A
the mutation increases the beta-cyclization activity of the enzyme (23% higher catalytic efficiency compared to the wild type)
D577G
-
the mutation increases the beta-cyclization activity of the enzyme with 43.9% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
D577G
the mutation increases the beta-cyclization activity of the enzyme (43.9% higher catalytic efficiency compared to the wild type)
D577I
-
the mutation decreases the beta-cyclization activity of the enzyme
D577I
the mutation decreases the beta-cyclization activity of the enzyme (14.5% lower catalytic efficiency compared to the wild type)
D577K
-
the mutant displays a 1.5% increase in the beta-cyclization activity compared to the wild type enzyme
D577K
-
the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability
D577L
-
the mutation decreases the beta-cyclization activity of the enzyme
D577L
the mutation decreases the beta-cyclization activity of the enzyme (8.8% lower catalytic efficiency compared to the wild type)
D577R
-
the mutant displays a 30.7% increase in the beta-cyclization activity compared to the wild type enzyme
D577R
the mutant exhibits beta-cyclization activity that is greater than that of the wild type by 3.3%
D577V
-
the mutation decreases the beta-cyclization activity of the enzyme
D577V
the mutation decreases the beta-cyclization activity of the enzyme (18.8% lower catalytic efficiency compared to the wild type)
D577A
-
the mutation increases the beta-cyclization activity of the enzyme with 23% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
-
D577A
-
the mutation increases the beta-cyclization activity of the enzyme (23% higher catalytic efficiency compared to the wild type)
-
D577G
-
the mutation increases the beta-cyclization activity of the enzyme with 43.9% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
-
D577G
-
the mutation increases the beta-cyclization activity of the enzyme (43.9% higher catalytic efficiency compared to the wild type)
-
D577I
-
the mutation decreases the beta-cyclization activity of the enzyme
-
D577I
-
the mutation decreases the beta-cyclization activity of the enzyme (14.5% lower catalytic efficiency compared to the wild type)
-
D577L
-
the mutation decreases the beta-cyclization activity of the enzyme
-
D577L
-
the mutation decreases the beta-cyclization activity of the enzyme (8.8% lower catalytic efficiency compared to the wild type)
-
D577R
-
the mutant displays a 30.7% increase in the beta-cyclization activity compared to the wild type enzyme
-
D577R
-
the mutant exhibits beta-cyclization activity that is greater than that of the wild type by 3.3%
-
D577V
-
the mutation decreases the beta-cyclization activity of the enzyme
-
D577V
-
the mutation decreases the beta-cyclization activity of the enzyme (18.8% lower catalytic efficiency compared to the wild type)
-
K47L
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47L
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, highest titer of product among the mutants tested, 57% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
Q265K
-
the mutant shows 15% cyclization (alpha-cyclodextrin-forming) and 236% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Q265K
-
the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y167H
the mutant shows enhanced alpha-cyclodextrin specificity
Y167H
-
the mutations increases the alpha:beta ratio in cyclodextrin product mixture from 3.4 to 7.8 in comparison with the wild type enzyme
Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 200% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y195S
-
the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y260R
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y260R
-
the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y167H
-
the mutations increases the alpha:beta ratio in cyclodextrin product mixture from 3.4 to 7.8 in comparison with the wild type enzyme
-
Y167H
-
the mutant shows enhanced alpha-cyclodextrin specificity
-
Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 200% hydrolysis (starch-degrading) activities compared to the wild type enzyme
-
Y195S
-
the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
-
Y260R
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme
-
Y260R
-
the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
-
additional information
-
immobilization of the enzyme by three different techniques: on two types of polysulfone membranes; entrapped in agar-gel beads containing magnetite, and by nano-particles of silanized magnetite covalently bound on the cell surface. The enzyme immobilized on membrane shows highest enzyme activity and high stability, overview
additional information
-
enzyme production, method optimization by usage of fed-batch fermentation, CGTase activity and cell density are increased 360% and 510%, respectively, compared to those values achieved with batch fermentation, overview
additional information
replacement of B domain by corresponding domain from Thermococcus kodakarensis, Anaerobacter gottschalkii and Pyrococcus furiosus leads to complete loss of catalytic function. Replacement of B domain by corresponding domain from Bacillus stearothermophilus ET1 enzyme leads to a mutant protein with retained activity. The mutant has the wild-type temperature optimum of 60°C with increase in half-life to 57 min. Introduction of mutation F188Y to the mutant results in a half-life of 28 min at 60°C. Bith mutant strains display improved ability to form cyclodextrin and a faster turnover rate
additional information
-
replacement of B domain by corresponding domain from Thermococcus kodakarensis, Anaerobacter gottschalkii and Pyrococcus furiosus leads to complete loss of catalytic function. Replacement of B domain by corresponding domain from Bacillus stearothermophilus ET1 enzyme leads to a mutant protein with retained activity. The mutant has the wild-type temperature optimum of 60°C with increase in half-life to 57 min. Introduction of mutation F188Y to the mutant results in a half-life of 28 min at 60°C. Bith mutant strains display improved ability to form cyclodextrin and a faster turnover rate
-
additional information
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
additional information
error-prone PCR mutagenesis for searching the sequence space of CGTase for acarbose-insensitive variants, overview
additional information
-
position 179 is involved in enzyme product specificity and must be occupied by Gly or by amino acid residues able to interact with the substrate through hydrogen bonds in a way that the cyclization process occurs efficiently
additional information
-
error-prone PCR mutagenesis for searching the sequence space of CGTase for acarbose-insensitive variants, overview
-
additional information
-
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
-
additional information
-
position 179 is involved in enzyme product specificity and must be occupied by Gly or by amino acid residues able to interact with the substrate through hydrogen bonds in a way that the cyclization process occurs efficiently
-
additional information
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
additional information
method development for production of alpha-, beta-, and gamma-cyclodextrins from soluble starch by Bacillus macerans Lys10-tagged cyclodextrin glycosyltransferase using a reactor with installed ultrafiltration membrane and immobilized enzyme in a repeated-batch process, overview
additional information
-
method development for production of alpha-, beta-, and gamma-cyclodextrins from soluble starch by Bacillus macerans Lys10-tagged cyclodextrin glycosyltransferase using a reactor with installed ultrafiltration membrane and immobilized enzyme in a repeated-batch process, overview
additional information
-
generation of a modified enzyme with increased alpha-cyclization specificity by mutations of Asp372 and Tyr89 at subsite -3 in the CGTase, obverview
additional information
-
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
-
additional information
-
molecular imprinting of the CGTase with cyclomaltododecaose, CD12, as the template molecule followed by cross-linking of the derivatized protein stabilizes the enzyme, overview
additional information
-
expression of cyclodextrin glycosyltransferase gene fused with thioredoxin, hexa-histidine and S-protein at the N-terminus and a proline-rich peptide at the C-terminus, in Escherichia coli. The maximum specific activity for enzyme is 2.7fold higher than that of the non-fusion form, leading to a specific activity of 2268 units/mg protein at a 61% yield. The fusion enzyme is superior than its wild-type counterpart in terms of stability against high temperature and organic solvents. The fusion enzyme catalyzes the synthesis of cyclodextrins in 20% v/v dimethylformamide with a higher product yield of cyclodextrins CD7 and CD8 compared to that of the wild-type enzyme in the same buffer-solvent system
additional information
-
expression of cyclodextrin glycosyltransferase gene fused with thioredoxin, hexa-histidine and S-protein at the N-terminus and a proline-rich peptide at the C-terminus, in Escherichia coli. The maximum specific activity for enzyme is 2.7fold higher than that of the non-fusion form, leading to a specific activity of 2268 units/mg protein at a 61% yield. The fusion enzyme is superior than its wild-type counterpart in terms of stability against high temperature and organic solvents. The fusion enzyme catalyzes the synthesis of cyclodextrins in 20% v/v dimethylformamide with a higher product yield of cyclodextrins CD7 and CD8 compared to that of the wild-type enzyme in the same buffer-solvent system
-
additional information
-
molecular imprinting of the CGTase with cyclomaltododecaose, CD12, as the template molecule followed by cross-linking of the derivatized protein stabilizes the enzyme, overview
-
additional information
-
2fold enhancement and optimization of cyclodextrin production by the enzyme in a membrane process, development of a process for simultaneous production and isolation of beta-cyclodextrin in the presence of complexing agents, e.g. trichloroethylene or toluene, overview
additional information
-
engineering of yeast cells to display the enzyme on the cell surface with reduced cyclodextrin formation activity and enhanced hydrolysis activity towards starch, integration of deltaCGTase into the chromosome, overview, optimzation of starch hydrolysis by the recombinant enzyme for for enhancing of bread-baking process, overview
additional information
-
immobilization of the heat stable enzyme using different supports and immobilization methods, encapsulation of the enzyme in a sol-gel matrix, effects on activity recovery, method optimizations, overview
additional information
-
engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exospecificity. the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase
additional information
-
mutations in two residues, Ser-77 and Trp-239, on the outer region of the active site, lowers the hydrolytic activity up to 15fold with retention of cyclization activity
additional information
-
mutations in two residues, Ser-77 and Trp-239, on the outer region of the active site, lowers the hydrolytic activity up to 15fold with retention of cyclization activity
-
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agriculture
-
cyclodextrin production, agriculture chemistry
agriculture
-
cyclodextrin production, agriculture chemistry
-
food industry
the enzyme can be used in the bread-baking process since its addition in the dough mix improved significantly the loaf volume and decreased the firmness of bread during storage
food industry
-
the enzyme improves the sweetness and edulcorant quality of stevioside
food industry
-
the enzyme leads to an improvement in the technological quality of gluten-free laminated baked products
food industry
cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing
food industry
-
the enzyme can be used in the bread-baking process since its addition in the dough mix improved significantly the loaf volume and decreased the firmness of bread during storage
-
food industry
-
the enzyme improves the sweetness and edulcorant quality of stevioside
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
nutrition
-
-
nutrition
-
application as antistaling agent, retards the deterioration process in bread
nutrition
important enzyme in food industry
nutrition
-
important enzyme in food industry
nutrition
important enzyme in food industry
nutrition
-
important enzyme in food industry
nutrition
important enzyme in food industry
nutrition
-
important enzyme in food industry
nutrition
important enzyme in food industry
nutrition
-
important enzyme in food industry
nutrition
important enzyme in food industry
nutrition
-
important enzyme in food industry
nutrition
-
important enzyme in food industry
nutrition
-
important enzyme in food industry
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
important enzyme in food industry
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
important enzyme in food industry
-
nutrition
-
application as antistaling agent, retards the deterioration process in bread
-
nutrition
-
important enzyme in food industry
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
important enzyme in food industry
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
application as antistaling agent, retards the deterioration process in bread
-
pharmacology
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
pharmacology
-
important enzyme in pharmaceutical industry
-
synthesis
-
-
synthesis
-
application of immobilized enzyme is practically important for continous production of cyclodextrins, broad activity maximum is advantageous for industrial operations, immobilized enzyme is able to work at maximum efficiency at lower temperatures
synthesis
-
ATCC 21783, enzyme is becoming commercially important since cyclodextrins have found various practical applications
synthesis
thermostable, useful for industrial utilization
synthesis
-
thermostable, useful for industrial utilization
synthesis
-
industrial strain E 192, industrial production of cyclodextrins
synthesis
Bacillus autolyticus
-
used in industrial applications
synthesis
-
strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
chemical industry
synthesis
-
enzymatic synthesis of glycosides such as maltooligosyl sucrose, glycosyl stevioside and glycosyl ascorbic acid
synthesis
-
enzymatic synthesis of salicin prodrugs by the reaction of cyclomaltodextrin glucanyltransferase from Bacillus macerans with cyclomaltohexaose and salicyl alcohol which gives a salicin as a major product and the reaction of Leuconostoc mesenteroides B-742CB dextransucrase with sucrose and salicyl alcohol which gives a isosalicin as the major product
synthesis
-
production of alpha-cyclodextrin. Cyclodextrins serve as molecular hosts, are used in the food industry for capturing and retaining flavors and are also used in the formulation of pharmaceuticals.
synthesis
-
potential industrial application of this CGTase in processes in which thermal stability is required. This enzyme could be used after starch gelatinization without cooling the solution to temperatures lower than 60°C
synthesis
-
synthesis of cyclodextrins with multiple applications in the food, pharmaceutical, cosmetic, agricultural and chemical industries. Conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs
synthesis
-
the CGTase-glyoxyl derivative allow the production of cyclodextrin at 85°C, giving twice the production rate compared to the free enzyme, 17.5% higher mass selectivity for beta-cyclodextrin and may help avoid microbial contamination. These characteristics are important considerations for the development of an industrial CD production continuous process
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme is of interest for industrial cyclodextrin production
synthesis
-
the enzyme is useful for industrial production of cyclodextrins
synthesis
the enzyme is useful for production of alpha-, beta-, and gamma-cyclodextrins from soluble starch
synthesis
-
CGTase is an important industrial enzyme, unique in its capacity to convert starch and related substrates into cyclodextrins through cyclization, an intramolecular transglycosylation reaction
synthesis
CGTases is used to catalyze cyclomaltooligosaccharides/cyclodextrins production in important industrial processes
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase, the equilibrium lays to 80% on the side of dodecyl-beta-D-maltooctaoside production when the enzyme from Bacillus macerans is used as biocatalyst, method evaluation, overview
synthesis
-
manipulation of the enzyme by molecular imprinting to preferentially produce large-ring cyclodextrins, overview
synthesis
-
synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase, the equilibrium lays to 80% on the side of dodecyl-beta-D-maltooctaoside production when the enzyme from Bacillus macerans is used as biocatalyst, method evaluation, overview
synthesis
-
the enzyme as membrane biocatalyst is applied for a direct cyclodextrin production
synthesis
-
the enzyme is used for cyclodextrin production, generation of a modified enzyme with increased alpha-cyclization specificity, overview
synthesis
-
enzyme achieves 47% conversion of an insoluble raw commercial corn starch into cyclodextrins with production of only beta- and gamma-cyclodextrins, in a ratio of 80%:20% in alkaline pH 9.0
synthesis
-
enzyme achieves 50.7% conversion of raw corn starch into 81.6% beta- and 18.4% gamma-cyclodextrins after 24 h enzyme reaction at 60°C and pH 8.0
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
enzyme achieves 50.7% conversion of raw corn starch into 81.6% beta- and 18.4% gamma-cyclodextrins after 24 h enzyme reaction at 60°C and pH 8.0
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
Bacillus autolyticus 11149
-
used in industrial applications
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
manipulation of the enzyme by molecular imprinting to preferentially produce large-ring cyclodextrins, overview
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
potential industrial application of this CGTase in processes in which thermal stability is required. This enzyme could be used after starch gelatinization without cooling the solution to temperatures lower than 60°C
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
enzyme achieves 47% conversion of an insoluble raw commercial corn starch into cyclodextrins with production of only beta- and gamma-cyclodextrins, in a ratio of 80%:20% in alkaline pH 9.0
-
synthesis
-
strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use
-
synthesis
-
chemical industry
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
industrial strain E 192, industrial production of cyclodextrins
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
synthesis of cyclodextrins with multiple applications in the food, pharmaceutical, cosmetic, agricultural and chemical industries. Conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs
-
synthesis
-
CGTases is used to catalyze cyclomaltooligosaccharides/cyclodextrins production in important industrial processes
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
enzymatic synthesis of glycosides such as maltooligosyl sucrose, glycosyl stevioside and glycosyl ascorbic acid
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
industrial strain E 192, industrial production of cyclodextrins
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-