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4-nitrophenyl alpha-D-maltohexaoside + H2O
4-nitrophenol + maltohexaose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
poor substrate
-
-
?
4-nitrophenyl maltopyranoside + H2O
4-nitrophenol + maltose
excellent substrate
-
-
?
acarbose + alpha-D-glucose
isoacarbose
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
acarbose + H2O
acarviosine-glucose + D-glucose
-
-
-
-
?
acarbose + H2O
alpha-maltose + ?
acarbose + H2O
D-glucose + acarviosine-glucose
acarbose + H2O
glucose + acarviosine-glucose
-
-
-
-
?
alpha-(1,4)-glycosidic linked cyclodextrins + H2O
maltooligosaccharide
-
main depolymerization of outer amylopectin branches
-
-
?
alpha-cyclodextrin + H2O
?
alpha-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 10:1
?
alpha-cyclodextrin + H2O
maltose + ?
-
-
-
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
-
-
?
alpha-Schardinger dextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
amylopectin + H2O
alpha-maltose + ?
-
hydrolytic release of maltose residues, wild-type, double and triple mutant enzymes studied to determine substrate size and geometric shape of catalytic site
-
-
?
amylopectin + H2O
fragments of amylopectin
-
main depolymerization of outer amylopectin branches
mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained
-
?
amylopectin + H2O
fragments of amylopectin + dextrin
-
main depolymerization of outer amylopectin branches
mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained
-
?
amylopectin + H2O
maltose + ?
amylopectin + H2O
maltose + alpha-D-glucose
-
-
in the initial stages of hydrolysis enzyme produces maltotetraose, maltotriose and maltose, as the reaction progresses, the maltotriose and maltotetraose disappears, glucose being formed by the splitting of maltotriose into equimolar amounts of maltose and glucose
?
amylopectin + H2O
maltose + D-glucose
amylopectin + H2O
maltose + maltotriose
amylose + H2O
alpha-maltose + ?
-
substrate size and geometric shape of catalytic site analyzed, wild-type, double and triple mutant enzymes tested, wild-type enzyme hydrolyzed amylose more favourably than amylopectin
-
-
?
amylose + H2O
maltose + ?
amylose + H2O
maltose + D-glucose
azurine cross-linked amylose + H2O
maltose + ?
-
-
-
-
?
beta-cyclodextrin + H2O
?
beta-cyclodextrin + H2O
alpha-maltose + ?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
beta-cyclodextrin + H2O
alpha-maltose + glucose
beta-cyclodextrin + H2O
D-glucose + maltose + maltotriose + maltooligosaccharides
100% activity
-
-
?
beta-cyclodextrin + H2O
maltooligosaccharide
-
-
-
-
?
beta-cyclodextrin + H2O
maltose + ?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
-
?
cyclomaltodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
D-tagatose + maltotriose
maltosyl-tagatose
-
transglycosylation
-
-
?
gamma-cyclodextrin + H2O
?
gamma-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
maximal activity (100%)
-
-
?
gamma-cyclodextrin + H2O
maltose + ?
-
-
-
?
gelatinised starch + H2O
maltose + ?
-
-
-
-
?
gelatinised waxy maize starch + H2O
alpha-maltose + ?
-
-
main product
-
?
gelatinized corn starch + H2O
?
-
-
-
-
?
gelatinized rice starch + H2O
maltose + ?
-
-
-
-
?
glycogen + H2O
maltose + ?
maize starch + H2O
maltose + ?
-
-
-
-
?
maltoheptaose + H2O
maltose + ?
-
-
-
-
?
maltoheptaose + H2O
maltose + D-glucose + ?
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (32.8%) as well as maltose
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
maltose + ?
-
-
-
-
?
maltopentaose + H2O
2 maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
alpha-maltose + ?
-
-
-
-
?
maltopentaose + H2O
maltose + D-glucose + ?
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltotetraose + H2O
2 maltose
maltotetraose + H2O
alpha-maltose + ?
-
-
-
-
?
maltotetraose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltose + 2 D-glucose
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (24.8%) as well as maltose
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
maltotriose + H2O
alpha-maltose + glucose
-
-
-
?
maltotriose + H2O
isomaltose + isopanose + panose + branched glucooligosaccharides
-
-
transfer products of transglycosylation
-
?
maltotriose + H2O
maltose + D-glucose
polished rice grain + H2O
maltose + ?
-
-
-
-
?
puerarin + beta-cyclodextrin
daidzein 8-C-glucosyl-(alpha-glucosyl)n-1
-
transglycosylation activity
-
-
?
pullulan + H2O
alpha-maltose + ?
pullulan + H2O
maltose + D-glucose + panose
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
mainly maltose and glucose with relatively minor quantity of panose and other maltooligosaccharides
-
?
pullulan + H2O
panose + ?
rice meal + H2O
maltose + ?
-
-
-
-
?
simmondsin + acarviosine-glucose
acarviosine-simmondsin + alpha-D-glucose
-
transglycosylation
novel compound in which acarviosine is attached to the glucose-moiety of simmondsin by an alpha-(1,6)-glycosidic linkage, with both antiobesity and hypoglycemic activity
?
soluble starch + H2O
alpha-maltose + ?
-
-
-
-
?
soluble starch + H2O
maltose + ?
starch + H2O
alpha-maltose + ?
starch + H2O
maltooligosaccharide
-
-
-
-
?
wheat starch + H2O
maltose + ?
-
-
-
-
?
additional information
?
-
acarbose + alpha-D-glucose
isoacarbose
-
transglycosylation
-
-
?
acarbose + alpha-D-glucose
isoacarbose
-
-
-
-
?
acarbose + alpha-D-glucose
isoacarbose
-
transglycosylation
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
acarbose + H2O
alpha-maltose + ?
-
-
-
-
?
acarbose + H2O
alpha-maltose + ?
-
-
-
-
?
acarbose + H2O
D-glucose + acarviosine-glucose
-
-
-
-
?
acarbose + H2O
D-glucose + acarviosine-glucose
-
-
-
-
?
acarbose + H2O
D-glucose + acarviosine-glucose
-
-
-
?
alpha-cyclodextrin + H2O
?
80% activity compared to beta-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
high specificity for alpha-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
?
alpha-cyclodextrin + H2O
?
-
64.7% activity compared to gamma-cyclodextrin
-
-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
the maltogenic Bacillus stearothermophilus alpha-amylase preferentially hydrolyses the exterior chains of amylopectin. However, during the later phases, the enzyme also hydrolyses inner chains, presumably with a high multiple attack action
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
amylopectin + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
amylopectin + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltose + maltotriose
-
-
wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P, wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% matotriose of mutant F188L/D261G/T288P
-
?
amylopectin + H2O
maltose + maltotriose
-
-
wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P, wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% matotriose of mutant F188L/D261G/T288P
-
?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O
maltose + ?
-
-
-
-
?
amylose + H2O
maltose + ?
-
-
-
?
amylose + H2O
maltose + ?
-
high preference toward amylose compared to amylopectin
-
-
?
amylose + H2O
maltose + ?
-
-
-
?
amylose + H2O
maltose + D-glucose
-
-
-
?
amylose + H2O
maltose + D-glucose
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
78.1% activity compared to gamma-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 3:1
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
hydrolytic activity
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
prefers cyclodextrins to starch or pullulan as substrate
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O
maltose + ?
the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + ?
the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
preference of cyclodextrin as substrate over starch or pullulan
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
-
-
?
gamma-cyclodextrin + H2O
?
10% activity compared to beta-cyclodextrin
-
-
?
gamma-cyclodextrin + H2O
?
10% activity compared to beta-cyclodextrin
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
?
glycogen + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
glycogen + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
glycogen + H2O
maltose + ?
-
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
-
-
-
?
maltotetraose + H2O
2 maltose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotriose + H2O
?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
maltotriose + H2O
?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
maltotriose + H2O
?
-
-
-
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
potato starch + H2O
?
-
-
-
?
potato starch + H2O
?
-
-
-
?
pullulan + H2O
?
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
preference of cyclodextrin as substrate over starch or pullulan
-
-
?
pullulan + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
pullulan + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
pullulan + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
pullulan + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
pullulan + H2O
alpha-maltose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
mainly hydrolyzed to panose
-
?
pullulan + H2O
panose + ?
main product panose
-
-
?
pullulan + H2O
panose + ?
-
-
mainly hydrolyzed to panose
-
?
pullulan + H2O
panose + ?
main product panose
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
soluble starch + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
soluble starch + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
soluble starch + H2O
maltose + ?
-
-
-
-
?
soluble starch + H2O
maltose + ?
the enzyme displays less hydrolytic action on raw starches than on soluble starch
-
-
?
soluble starch + H2O
maltose + ?
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
-
-
?
soluble starch + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
starch + H2O
?
-
-
-
?
starch + H2O
?
-
the enzyme shows a substrate hydrolysis preference for cyclodextrins over starch
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
carbohydrate metabolism in the cytoplasm
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
carbohydrate metabolism in the cytoplasm
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
exo-acting maltogenic alpha-amylase, removes maltose units from the non-reducing chain ends
-
?
starch + H2O
alpha-maltose + ?
utilization of BSMA for production of highly branched amylopectin and amylose from enzymatically modified rice starch, branching by transglycosylation mediated by BSMA, increased number of branched side chains in modified amylopectin clusters determined
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
wild-type LGMA and recombinant rLGMA, reaction products determined by thin-layer chromatography and gel filtration
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
wild-type LGMA and recombinant rLGMA, reaction products determined by thin-layer chromatography and gel filtration
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
transglycosylation pattern opposite to that of bacterial maltogenic amylases, predominant formation of alpha-1,4-glycosidic linked transfer products than of alpha-1,6-linked products
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
transglycosylation pattern opposite to that of bacterial maltogenic amylases, predominant formation of alpha-1,4-glycosidic linked transfer products than of alpha-1,6-linked products
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
catalyzes the hydrolysis of starch material, central role in carbohydrate metabolism
-
?
starch + H2O
maltose + ?
-
the enzyme shows higher affinity to the starch at negative pressure (-200 mbar) compared to the atmospheric pressure
-
-
?
starch + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
starch + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
starch + H2O
maltose + ?
-
preference of cyclodextrin as substrate over starch or pullulan
-
-
?
starch + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
starch + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
additional information
?
-
the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above
-
-
?
additional information
?
-
the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above
-
-
?
additional information
?
-
-
BSMA preferentially hydrolyzes longer branch chains, releasing maltose and glucose from the non-reducing end of the branch chains, and transfers the resulting maltooligosaccharides to the non-reducing ends of the shorter branch chains by forming alpha-1,6-glucosidic linkages
-
-
?
additional information
?
-
-
the enzyme forms highly branched products from branched glucan and branching enzyme-treated tapioca starch
-
-
?
additional information
?
-
the dimeric enzyme transglycosylates hydrolytic products of G4/G5 and acarbose, while the monomeric form does not because of the lack of extra sugar-binding space formed due to dimerization
-
-
?
additional information
?
-
-
enzyme shows hydrolytic activity towards alpha-1,6-glycosidic linkage
-
-
?
additional information
?
-
an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points
-
-
?
additional information
?
-
acarbose is not cleaved by the enzyme
-
-
?
additional information
?
-
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner
-
-
?
additional information
?
-
an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points
-
-
?
additional information
?
-
acarbose is not cleaved by the enzyme
-
-
?
additional information
?
-
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner
-
-
?
additional information
?
-
-
maltooligosaccharides G3-G7 show 5.4-24.1% relative activity compared to gamma-cyclodextrin
-
-
?
additional information
?
-
does not hydrolyze cyclodextrin, pullulan and acarbose
-
-
?
additional information
?
-
-
exhibits dual activity of alpha-D-(1,4)- and alpha-D-(1,6)- glycosidic bond cleavages, shows activity of alpha-D(1,4)- to alpha-D-(1,3), alpha-D-(1,4), or alpha-D-(1,6)-transglycosylation and cleaves acarbose, a pseudotetrasaccharide competitive inhibitor of alpha-amylases
-
-
?
additional information
?
-
-
nearly indistinguishable from cyclomaltodextrinase from Bacillus sp. and Bacillus stearothermophilus neopullulanase, distinguished from typicsl alpha-amylases by containing a novel N-terminal domain and exhibiting preferential substrate specificities for cyclomaltodextrins over starch
-
-
?
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0.43
alpha-cyclodextrin
pH and temperature not specified in the publication
0.05 - 2.03
beta-cyclodextrin
2.68
gamma-cyclodextrin
pH and temperature not specified in the publication
4.1 - 13
soluble starch
-
additional information
additional information
-
0.426
acarbose
-
pH 6.0, 60°C, hydrolysis, wild-type
0.545
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332D
1
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332Q
1.08
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332H
0.05
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant DM
0.09
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 4B74
0.128
beta-cyclodextrin
-
-
0.16
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type and variants 3C71, 4B78 and 4A48
0.17
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variants 1B76, 1B100
0.174
beta-cyclodextrin
-
pH 6.0, 60°C, wild-type
0.19
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 2A39
0.263
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type
0.308
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl
0.36
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA DELTA124, 1M KCl
0.461
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124
1.48
beta-cyclodextrin
pH and temperature not specified in the publication
2.03
beta-cyclodextrin
-
pH 6.0, 60°C, mutant W47A
1.5
maltoheptaose
-
kinetic parameters for C14-labelled maltooligosaccharides
8.18
maltoheptaose
-
50°C, pH 6.0, mutant enzyme A290I
9.21
maltoheptaose
-
50°C, pH 6.0, wild-type enzyme
3.8
maltohexaose
-
kinetic parameters for C14-labelled maltooligosaccharides
7.16
maltohexaose
-
50°C, pH 6.0, wild-type enzyme
7.53
maltohexaose
-
50°C, pH 6.0, mutant enzyme A290I
3.5
maltopentaose
-
50°C, pH 6.0, mutant enzyme A290I
3.97
maltopentaose
-
50°C, pH 6.0, wild-type enzyme
4.4
maltopentaose
-
kinetic parameters for C14-labelled maltooligosaccharides
16.2
maltopentaose
pH 5.0, 85°C
21.2
maltopentaose
pH 5.0, 90°C
63.43
maltose
-
50°C, pH 6.0, wild-type enzyme
427
maltose
-
50°C, pH 6.0, mutant enzyme A290I
1.6
maltotetraose
-
kinetic parameters for C14-labelled maltooligosaccharides
2.95
maltotetraose
-
50°C, pH 6.0, mutant enzyme A290I
3.38
maltotetraose
-
50°C, pH 6.0, wild-type enzyme
18.2
maltotetraose
pH 5.0, 85°C
18.8
maltotetraose
pH 5.0, 90°C
1.13
maltotriose
-
50°C, pH 6.0, wild-type enzyme
2.52
maltotriose
-
50°C, pH 6.0, mutant enzyme A290I
3.6
maltotriose
-
kinetic parameters for C14-labelled maltooligosaccharides
4.25
maltotriose
pH 5.0, 85°C
8.4
maltotriose
pH 5.0, 90°C
12.3
maltotriose
pH 5.5, 60°C, wild-type enzyme
16.4
maltotriose
pH 5.5, 60°C, mutant enzyme W177F
22
maltotriose
pH 5.5, 60°C, mutant enzyme W177Y
28
maltotriose
pH 5.5, 60°C, mutant enzyme W177L
31.7
maltotriose
pH 5.5, 60°C, mutant enzyme W177N
35.3
maltotriose
pH 5.5, 60°C, mutant enzyme W177S
4.1
soluble starch
-
estimated for monomeric conformation, in presence of 1 M NaCl
-
13
soluble starch
-
estimated for the high oligomer conformation
-
additional information
additional information
-
Km 5.34 mg mL-1, starch as substrate, pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124
-
additional information
additional information
-
Km 49.7 mg/ml, starch as substrate, pH 6.0, 60°C, wild-type, 1 M KCl
-
additional information
additional information
-
Km 7.72 mg/ml, starch as substrate, pH 6.0, 60°C, truncated mutant ThMA-DELTA124, 1M KCl
-
additional information
additional information
-
Km 131 mg/ml, starch as substrate, mutant W47A
-
additional information
additional information
-
Km 73.5 mg/ml, starch as substrate, wild-type
-
additional information
additional information
-
Km 61.0 mg/ml, starch as substrate, pH 6.0, 60°C, hydrolysis, wild-type
-
additional information
additional information
-
lower affinity for binding of amylopectin but higher affinity for amylose in mutant enzymes demonstrated, sterospecific substrate binding properties of triple mutant enzyme determined by molecular modelling
-
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0.1 - 500
alpha-cyclodextrin
0.005 - 15.38
amylopectin
0.00000343 - 280.8
beta-cyclodextrin
29.1 - 225.6
gamma-cyclodextrin
0.0017 - 197
maltopentaose
0.0033 - 574.1
maltotetraose
0.037 - 652.5
maltotriose
0.021 - 9.9
soluble starch
-
18.7
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332H
41.4
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332Q
45.4
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332D
67.8
acarbose
-
pH 6.0, 60°C, hydrolysis, wild-type
0.1
alpha-cyclodextrin
monomeric enzyme form, at pH 7.0 and 80°C
0.75
alpha-cyclodextrin
mutant enzyme D109A, at pH 7.0 and 80°C
1.39
alpha-cyclodextrin
mutant enzyme D109E, at pH 7.0 and 80°C
1.45
alpha-cyclodextrin
pH and temperature not specified in the publication
2.78
alpha-cyclodextrin
dimeric enzyme form, at pH 7.0 and 80°C
500
alpha-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
0.005
amylopectin
mutant enzyme D109E, at pH 7.0 and 80°C
0.04
amylopectin
dimeric enzyme form, at pH 7.0 and 80°C
0.1
amylopectin
mutant enzyme D109A, at pH 7.0 and 80°C
0.17
amylopectin
monomeric enzyme form, at pH 7.0 and 80°C
0.8
amylopectin
pH and temperature not specified in the publication
4.01
amylopectin
-
at pH 5.5 and 90°C
15.38
amylopectin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
0.022
amylose
mutant enzyme D109E, at pH 7.0 and 80°C
0.04
amylose
dimeric enzyme form, at pH 7.0 and 80°C
0.13
amylose
mutant enzyme D109A, at pH 7.0 and 80°C
0.21
amylose
monomeric enzyme form, at pH 7.0 and 80°C
0.59
amylose
pH and temperature not specified in the publication
4.21
amylose
-
at pH 5.5 and 90°C
62.82
amylose
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
0.00000343
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124
0.00000367
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl
0.12
beta-cyclodextrin
monomeric enzyme form, at pH 7.0 and 80°C
0.49
beta-cyclodextrin
mutant enzyme D109A at pH 7.0 and 80°C
0.66
beta-cyclodextrin
mutant enzyme D109E at pH 7.0 and 80°C
1.33
beta-cyclodextrin
dimeric enzyme form, at pH 7.0 and 80°C
5.36
beta-cyclodextrin
pH and temperature not specified in the publication
12.5
beta-cyclodextrin
at pH 7.0 and 40°C
20
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variants DM and 4B74
110
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 4B78
120
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 3C71
126
beta-cyclodextrin
-
-
126
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl
130
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 4A48
160
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type
167
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type
170
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 2A39
180
beta-cyclodextrin
-
pH 6.0, 60°C, mutantW47A
190
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 1B100
200
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 1B76
280.8
beta-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
29.1
gamma-cyclodextrin
pH and temperature not specified in the publication
225.6
gamma-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
2
maltoheptaose
-
50°C, pH 6.0, mutant enzyme A290I
42.5
maltoheptaose
-
50°C, pH 6.0, wild-type enzyme
72.08
maltoheptaose
-
50°C, pH 6.0, mutant enzyme A290I
384.1
maltoheptaose
-
50°C, pH 6.0, wild-type enzyme
9.2
maltohexaose
-
50°C, pH 6.0, wild-type enzyme
20 - 50
maltohexaose
-
50°C, pH 6.0, mutant enzyme A290I
88.45
maltohexaose
-
50°C, pH 6.0, mutant enzyme A290I
160.3
maltohexaose
-
50°C, pH 6.0, wild-type enzyme
0.0017
maltopentaose
pH 5.0, 90°C
3.85
maltopentaose
pH 5.0, 85°C
69.01
maltopentaose
-
50°C, pH 6.0, mutant enzyme A290I
197
maltopentaose
-
50°C, pH 6.0, wild-type enzyme
0.04
maltose
-
50°C, pH 6.0, mutant enzyme A290I
0.29
maltose
-
50°C, pH 6.0, wild-type enzyme
0.0033
maltotetraose
pH 5.0, 90°C
3.95
maltotetraose
pH 5.0, 85°C
29.8
maltotetraose
-
50°C, pH 6.0, wild-type enzyme
173.5
maltotetraose
-
50°C, pH 6.0, mutant enzyme A290I
574.1
maltotetraose
-
50°C, pH 6.0, wild-type enzyme
0.037 - 0.23
maltotriose
-
50°C, pH 6.0, mutant enzyme A29I
6.35
maltotriose
pH 5.0, 90°C
11.45
maltotriose
pH 5.0, 85°C
70.97
maltotriose
pH 5.5, 60°C, mutant enzyme W177F
79.07
maltotriose
-
50°C, pH 6.0, mutant enzyme A29I
108.25
maltotriose
pH 5.5, 60°C, mutant enzyme W177Y
126.2
maltotriose
pH 5.5, 60°C, mutant enzyme W177L
137.2
maltotriose
pH 5.5, 60°C, wild-type enzyme
150.98
maltotriose
pH 5.5, 60°C, mutant enzyme W177N
182.82
maltotriose
pH 5.5, 60°C, mutant enzyme W177S
652.5
maltotriose
-
50°C, pH 6.0, wild-type enzyme
0.021
soluble starch
mutant enzyme D109E, at pH 7.0 and 80°C
-
0.04
soluble starch
dimeric enzyme form, at pH 7.0 and 80°C
-
0.12
soluble starch
mutant enzyme D109A, at pH 7.0 and 80°C
-
0.2
soluble starch
monomeric enzyme form, at pH 7.0 and 80°C
-
9.9
soluble starch
at pH 7.0 and 40°C
-
0.000245
starch
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124
0.000332
starch
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl
249
starch
-
pH 6.0, 60°C, wild-type
301
starch
-
pH 6.0, 60°C, hydrolysis, wild-type
335
starch
-
pH 6.0, 60°C, mutant W47A
457
starch
-
pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl
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0.2
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant DM
0.3
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B74
1
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B78
1.25
pH 5.0, 90°C, substrate: maltotriose
1.5
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, wild-type
1.7
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variants 2A39, 4A48 and 3C71
14.2
-
starch as substrate
177.4
-
cell extract, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5)
194.1
-
beta-cyclodextrin as substrate, monomer
2
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B100
2.1
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B76
206.8
-
beta-cyclodextrin as substrate, 1.0 M KCl
21.1
-
starch as substrate, 0.2 M KCl
210
-
beta-cyclodextrin as substrate, 0.8 M KCl
227.2
-
beta-cyclodextrin as substrate, 0.6 M KCl
24
-
starch as substrate, 0.4 M KCl
242.9
-
beta-cyclodextrin as substrate, 0.4 M KCl
257.8
-
beta-cyclodextrin as substrate, 0.2 M KCl
26
-
starch as substrate, 0.6 M KCl
26.3
-
starch as substrate, 0.8 M KCl
268.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MnCl2
27.6
-
starch as substrate, 1.0 M KCl
278
-
beta-cyclodextrin as substrate
30.5
-
soluble starch as substrate, monomer
342.7
-
beta-cyclodextrin as substrate, dimer
413.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM BaCl2
5.4
-
beta-cyclodextrin as substrate, dimer
535.1
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5)
558.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) methanol
568.8
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CoCl2
58.7
-
hydrolysis of beta-cyclodextrin
592.9
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) DMSO
604.7
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) ethanol
695.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MgCl2
728.8
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CaCl2
785.5
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM AlCl3
91
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CuCl2
93.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM HgCl2
95.2
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM ZnCl2
98.5
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM FeSO4
additional information
kinetic mechanism for recombinant enzyme MAUS149 shown, determined by measuring the amount of reducing sugars released during incubation with starch using the dinitrosalicylic acid method, substrate concentrations ranging from 1 to 7.5 g/ml for starch and from 0.5 to 4 g/l for cyclodextrin and pullulan
additional information
-
kinetic mechanism for recombinant enzyme MAUS149 shown, determined by measuring the amount of reducing sugars released during incubation with starch using the dinitrosalicylic acid method, substrate concentrations ranging from 1 to 7.5 g/ml for starch and from 0.5 to 4 g/l for cyclodextrin and pullulan
additional information
kinetic properties determined in wild-type and mutant enzymes, relative activity indicated for several mutants from different lineages of DNA shuffling
additional information
kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method
additional information
-
catalytic activity of wild-type LGMA and recombinant rLGMA tested in liquid and solid media, kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method, reaction at pH 6.5 for 13.5 h at 50°C, yields of 53.1% obtained
additional information
-
specific activity of starch hydrolysis estimated for the high oligomer conformation is about 7 U/mg and for monomeric state about 110 U/mg
additional information
-
kinetic properties determined towards amylose and amylopectin in wild-type, double and triple mutant enzymes, bicinchonimate method, determination of reducing sugars
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D46G
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The Km values of the mutant for all substrates are strongly increased compared to the wild type enzyme
D46N
the mutant behaves similar to the wild type enzyme regarding kinetic parameters, thermoactivity, thermostability and pH profile
D46V
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The affinity and catalytic efficiency of the mutant toward beta-cyclodextrin are increased 5fold as compared with the wild type enzyme
D46V/P78L/V145A/K548E
the half-life times for the mutant at 50°C and 55°C are 70 min and 25 min, compared to 30 min and 13 min for the wild type, respectively
G312A
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
G312A/K436R
the half-life time at 55°C increase from 15 to 25 min for the double mutant
K436R
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
T142A/D261G/N327S/K425E/K520R/N5951
-
variant NM404, medium thermotolerance due to D261G mutation
T142A/D261G/N327S/K425E/K520R/N595I
-
Novamyl variant NM404, similar to wild-type at pH 4.0
D46G
-
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The Km values of the mutant for all substrates are strongly increased compared to the wild type enzyme
-
D46N
-
the mutant behaves similar to the wild type enzyme regarding kinetic parameters, thermoactivity, thermostability and pH profile
-
D46V
-
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The affinity and catalytic efficiency of the mutant toward beta-cyclodextrin are increased 5fold as compared with the wild type enzyme
-
D46V/P78L/V145A/K548E
-
the half-life times for the mutant at 50°C and 55°C are 70 min and 25 min, compared to 30 min and 13 min for the wild type, respectively
-
G312A
-
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
-
G312A/K436R
-
the half-life time at 55°C increase from 15 to 25 min for the double mutant
-
K436R
-
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
-
N147D/F195L/N263S/D311G/A344V/F397S/N508D
mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated
N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T
additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown
N147D/F195L/N263S/D311G/A344V/F397S/N508D
-
mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated
-
N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T
-
additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown
-
W177F
transglycosylation activities of the mutant enzyme decreases by 18% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177L
transglycosylation activities of the mutant enzyme decreases by 37% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177N
transglycosylation activities of the mutant enzyme decreases by 45% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177S
transglycosylation activities of the mutant enzyme decreases by 52% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177Y
transglycosylation activities of the mutant enzyme decreases by 20% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
D109A
the mutant shows increased affinity towards amylose, amylopectin and starch, and a decreased affinity towards alpha- and beta-cyclodextrin
D109E
the mutant does not show any effect on the binding affinity and substrate hydrolytic efficiency towards alpha- and beta-cyclodextrin but a strong decline in the affinity and substrate hydrolytic efficiency of the mutant enzyme towards amylopectin
E580Q
strongly reduced activity compared to the wild type enzyme
F218A
the mutant shows wild type activity with alpha-1,6-glycosidic bond hydrolysis and about 4fold increased activity with alpha-1,4-glycosidic bond hydrolysis compared to the wild type enzyme
W453A
strongly reduced activity compared to the wild type enzyme
E580Q
-
strongly reduced activity compared to the wild type enzyme
-
F218A
-
the mutant shows wild type activity with alpha-1,6-glycosidic bond hydrolysis and about 4fold increased activity with alpha-1,4-glycosidic bond hydrolysis compared to the wild type enzyme
-
W453A
-
strongly reduced activity compared to the wild type enzyme
-
A290I
-
mutant enzyme A290I produces mostly maltose from maltotetraose, while wild-type enzyme produces glucose as well as maltose. kcat/KM of mutant enzyme 290I for maltose is 48times less than that of wild-type enzyme. kcat/Km for maltotriose is 18.5fold lower than wild-type enzyme. kcat/Km for maltotetraose is 2.9fold lower than wild-type enzyme. kcat/Km for maltopentaose is 2.5fold lower than wild-type enzyme. kcat/Km for maltohexaose is 1.9fold lower than wild-type enzyme. kcat/Km for maltoheptaose is 4.7fold lower than wild-type enzyme
A330G/N331C/E332C
-
F-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331G/E332C
-
C-20, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331G/E332G
-
G-91, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose
A330G/N331G/E332S
-
G-22, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331P/E332G
-
C-43, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331V/E332G
-
G-90, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330M/N331G/E332C
-
B-96, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330S/N331A
-
F-80, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose
A330S/N331G/E332T
-
K-37, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodexxtrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A398V
-
random mutagenesis, using DNA shuffling
E332D
-
site-directed mutagenesis, significantly decreased transglycosylation activity
E332H
-
site-directed mutagenesis, replacing Glu 332 with histidine reduces transglycosylation activity significantly, but enhances hydrolysis activity on alpha-(1,3)-, alpha-(1,4)- and alpha-(1,6) glycosidic bonds relative to the wild-type
E332Q
-
site-directed mutagenesis
E357L
-
site-directed mutagenesis
G50I/D109E
-
double mutation, two main residues of the catalytic binding pocket, site-directed mutagenesis
G50I/D109E/V431I
-
triple mutation of three main residues of the catalytic binding pocket, site-directed mutagenesis
I333V
-
random mutagenesis, using DNA shuffling
M375T
-
random mutagenesis, using DNA shuffling
N331S/E332G
-
I-69, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
P453L
-
random mutagenesis, using DNA shuffling
Q411L
-
random mutagenesis, using DNA shuffling
R26Q
-
random mutagenesis, using DNA shuffling
R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L
-
mutant enzyme shows highly improved thermostability and catalytic activity in presence of Ca2+
S169N
-
random mutagenesis, using DNA shuffling
V329A/A330C/N331G/E332V
-
A-39, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329A/A330G/N331V/E332A
-
G-13, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329A/N331L
-
B-4, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type
V329C/N331H/E332R
-
D-3, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329F/A330T/N331G/E332W
-
I-70, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329G/A330L/N331V/E332Y
-
H-16, slightly higher activity with cyclodextrin, pullulan, and starch, reduced activities with maltotriose, and acarbose, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type, similar transglysocylation pattern as wild-type
V329I/A330G/N331W
-
C-56, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329S/A330C/N331S/E332P
-
A-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329S/A330G/N331D
-
K-33, strong reduction of all substrate hydrolyzing activities, products of acarbose hydrolization are glucose, maltose, and acarviosine instead of only glucose and carviosine-glucose as in the wild-type reaction, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: very little amount of transfer products, with acarbose significant amount of acarviosine and maltose
V329S/A330G/N331G/E332V
-
E-74, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
V329T/A330C/N331T/E332V
-
E-50, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
W47A
-
site-directed mutagenesis
A398V
-
random mutagenesis, using DNA shuffling
-
I333V
-
random mutagenesis, using DNA shuffling
-
M375T
-
random mutagenesis, using DNA shuffling
-
R26Q
-
random mutagenesis, using DNA shuffling
-
S169N
-
random mutagenesis, using DNA shuffling
-
D30A/K40R/D261G
-
Novamyl variant NM398, similar to wild-type at pH 4.0
D30A/K40R/D261G
-
variant NM398, medium thermotolerance due to D261G mutation
F188L/D261G/T288P
-
Novamyl variant NM447, outperform wild-type Novamyl in bread at pH 4.3. Wild-type Novamyl requires a nearly 30fold protein dosage increase over NM447 to obtain anti-staling bread properties. NM447 appears to have a broad pH functionality profile and performs better than wild-type Novamyl in standard bread to pH 5.9. It seems to be be generally tehrmally stabilized, both at pH 4.0 and 5.0.
F188L/D261G/T288P
-
variant NM447, most thermotolerant, probably due to F188L mutation, but reduced activity, medium thermotolerance due to D261G mutation, improved anti-staling performance in application test, about 70% activity retained after incubation at 80°C at pH 4.3 for 25 min
N115D/F188L
-
Novamyl variant NM319, similar to wild-type at pH 4.0, at pH 5.5 the variant outperform wild-type Novamyl, significantly more thermally stable that wild-type
N115D/F188L
-
variant NM319, most thermotolerant, probably due to F188L mutation, but reduced activity, improved anti-staling performance in application test, about 40% activity retained after incubation at 80°C at pH 4.3 for 25 min
T142A
-
Novamyl variant NM326, similar to wild-type at pH 4.0
T142A
-
variant NM326, inducing 20% activity increase and 50% thermal stability increase
F188L/D261G/T288P
-
Novamyl variant NM447, outperform wild-type Novamyl in bread at pH 4.3. Wild-type Novamyl requires a nearly 30fold protein dosage increase over NM447 to obtain anti-staling bread properties. NM447 appears to have a broad pH functionality profile and performs better than wild-type Novamyl in standard bread to pH 5.9. It seems to be be generally tehrmally stabilized, both at pH 4.0 and 5.0.
-
F188L/D261G/T288P
-
variant NM447, most thermotolerant, probably due to F188L mutation, but reduced activity, medium thermotolerance due to D261G mutation, improved anti-staling performance in application test, about 70% activity retained after incubation at 80°C at pH 4.3 for 25 min
-
T142A
-
Novamyl variant NM326, similar to wild-type at pH 4.0
-
T142A
-
variant NM326, inducing 20% activity increase and 50% thermal stability increase
-
additional information
-
mutagenesis is induced by error-prone PCR, mutagenic fragments screened for thermostable variants (80°C) at low pH 4.3, most thermostable variants show a decreased activity to the wild-type enzyme
additional information
-
mutagenesis is induced by error-prone PCR, mutagenic fragments screened for thermostable variants (80°C) at low pH 4.3, most thermostable variants show a decreased activity to the wild-type enzyme
-
additional information
-
tapioca starch is modified using branching enzyme, BE, isolated from, Bacillus subtilis strain 168, and Bacillus stearothermophilus maltogenic amylase, BSMA. BE cleaves alpha-1,4 linkages of amylose and amylopectin, and moiety of glycosyl residues are transferred to another amylose and amylopectin to produce branched glucan and branching enzyme-treated tapioca starch by forming alpha-1,6 branch linkages. The product is further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points, overview
additional information
-
Random substitutions of amino acid residues Val329, Ala330, Asn331, and Glu332 that are forming an extra sugar-binding space with combinatorial saturation mutagenesis technique: substrate specificity, hydrolysis pattern, and transglycosylation activity of ThMA are modulated by these mutations. Activity assays with substrates: soluble starch, pullulan, beta-cyclodextrin, maltotriose, and acarbose at 60°C, pH 6.0 sodium-acetate buffer
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Outtrup, H.; Norman, B.E.
Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques
Starch Staerke
36
405-411
1984
Geobacillus stearothermophilus
-
brenda
Diderichsen, B.; Christiansen, L.
Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus
FEMS Microbiol. Lett.
56
53-60
1988
Geobacillus stearothermophilus, Geobacillus stearothermophilus C599
-
brenda
Dauter, Z.; Dauter, M.; Brzozowski, A.M.; Christensen, S.; Borchert, T.V.; Beier, L.; Wilson, K.S.; Davies, G.J.
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution
Biochemistry
38
8385-8392
1999
Geobacillus stearothermophilus (P19531), Geobacillus stearothermophilus
brenda
Kim, J.S.; Cha, S.S.; Kim, H.J.; Kim, T.J.; Ha, N.C.; Oh, S.T.; Cho, H.S.; Cho, M.J.; Kim, M.J.; Lee, H.S.; Kim, J.W.; Choi, K.Y.; Park, K.H.; Oh, B.H.
Crystal structure of a maltogenic amylase provides insights into a catalytic versatility
J. Biol. Chem.
274
26279-26286
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Geobacillus stearothermophilus, Thermus sp.
brenda
Kim, M.J.; Lee, S.B.; Lee, H.S.; Lee, S.Y.; Baek, J.S.; Kim, D.; Moon, T.W.; Robyt, J.F.; Park, K.H.
Comparative study of the inhibition of alpha-glucosidase, alpha-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucose
Arch. Biochem. Biophys.
371
277-283
1999
Geobacillus stearothermophilus
brenda
Cho, H.Y.; Kim, Y.W.; Kim, T.J.; Lee, H.S.; Kim, D.Y.; Kim, J.W.; Lee, Y.W.; Leed, S.; Park, K.H.
Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2
Biochim. Biophys. Acta
1478
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2000
Bacillus subtilis, Bacillus subtilis SUH4-2
brenda
Kim, T.J.; Park, C.S.; Cho, H.Y.; Cha, S.S.; Kim, J.S.; Lee, S.B.; Moon, T.W.; Kim, J.W.; Oh, B.H.; Park, K.H.
Role of the glutamate 332 residue in the transglycosylation activity of ThermusMaltogenic amylase
Biochemistry
39
6773-6780
2000
Thermus sp.
brenda
Kim, T.J.; Nguyen, V.D.; Lee, H.S.; Kim, M.J.; Cho, H.Y.; Kim, Y.W.; Moon, T.W.; Park, C.S.; Kim, J.W.; Oh, B.H.; Lee, S.B.; Svensson, B.; Park, K.H.
Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium
Biochemistry
40
14182-14190
2001
Thermus sp.
brenda
Lee, H.S.; Auh, J.H.; Yoon, H.G.; Kim, M.J.; Park, J.H.; Hong, S.S.; Kang, M.H.; Kim, T.J.; Moon, T.W.; Kim, J.W.; Park, K.H.
Cooperative action of alpha-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production
J. Agric. Food Chem.
50
2812-2817
2002
Geobacillus stearothermophilus
brenda
Lee, H.S.; Kim, M.S.; Cho, H.S.; Kim, J.I.; Kim, T.J.; Choi, J.H.; Park, C.; Oh, B.H.; Park, K.H.
Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other
J. Biol. Chem.
277
21891-21897
2002
Thermus sp.
brenda
Baek, J.S.; Kim, H.Y.; Abbott, T.P.; Moon, T.W.; Lee, S.B.; Park, C.S.; Park, K.H.
Acarviosine-simmondsin, a novel compound obtained from acarviosine-glucose and simmondsin by Thermus maltogenic amylase and its in vivo effect on food intake and hyperglycemia
Biosci. Biotechnol. Biochem.
67
532-539
2003
Thermus sp.
brenda
Kim, Y.W.; Choi, J.H.; Kim, J.W.; Park, C.; Cha, H.; Lee, S.B.; Oh, B.H.; Moon, T.W.; Park, K.H.
Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance
Appl. Environ. Microbiol.
69
4866-4874
2003
Thermus sp., Thermus sp. IM6501
brenda
Jung, H.M.; Park, K.H.; Kim, S.Y.; Lee, J.K.
L-Glutamate enhances the expression of Thermus maltogenic amylase in Escherichia coli
Biotechnol. Prog.
20
26-31
2004
Thermus sp., Thermus sp. IM6501
brenda
Cheong, K.; Tang, S.; Cheong, T.; Cha, H.; Kim, J.; Park, K.
Thermostable and alkalophilic maltogenic amylase of Bacillus thermoalkalophilus ET2 in monomer-dimer equilibrium
Biocatal. Biotransform.
23
79-87
2005
Bacillus thermoalkalophilus, Bacillus thermoalkalophilus ET2
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Park, S.; Cha, H.; Kang, H.; Shim, J.; Woo, E.; Kim, J.; Park, K.
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Thermus sp.
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Li, D.; Park, S.H.; Shim, J.H.; Lee, H.S.; Tang, S.Y.; Park, C.S.; Park, K.H.
In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase
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Geobacillus stearothermophilus
brenda
Oh, K.W.; Kim, M.J.; Kim, H.Y.; Kim, B.Y.; Baik, M.Y.; Auh, J.H.; Park, C.S.
Enzymatic characterization of a maltogenic amylase from Lactobacillus gasseri ATCC 33323 expressed in Escherichia coli
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Lactobacillus gasseri
brenda
Kim, Y.; Kim, D.; Kim, M.; Cha, H.; Park, C.; Moon, T.; Park, K.
Engineering Thermus maltogenic amylase with improved thermostability: Probing the role of the conserved calcium binding site in cyclodextrin-degrading enzymes
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Roh, H.; Kang, S.; Lee, H.; Kim, D.; Byun, S.; Lee, S.; Park, K.
Transglycosylation of tagatose with maltotriose by Bacillus stearothermophilus maltogenic amylase (BSMA)
Tetrahedron
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Geobacillus stearothermophilus
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Kim, J.W.; Kim, Y.H.; Lee, H.S.; Yang, S.J.; Kim, Y.W.; Lee, M.H.; Kim, J.W.; Seo, N.S.; Park, C.S.; Park, K.H.
Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1
Biochim. Biophys. Acta
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Thermoplasma volcanium, Thermoplasma volcanium GSS1
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Park, S.H.; Kang, H.K.; Shim, J.H.; Woo, E.J.; Hong, J.S.; Kim, J.W.; Oh, B.H.; Lee, B.H.; Cha, H.; Park, K.H.
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Tang, S.Y.; Le, Q.T.; Shim, J.H.; Yang, S.J.; Auh, J.H.; Park, C.; Park, K.H.
Enhancing thermostability of maltogenic amylase from Bacillus thermoalkalophilus ET2 by DNA shuffling
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Bacillus thermoalkalophilus (Q68KL3), Bacillus thermoalkalophilus ET2 (Q68KL3)
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Enzymatic synthesis and properties of highly branched rice starch amylose and amylopectin cluster
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Geobacillus stearothermophilus (P19531)
brenda
Cho, M.H.; Park, S.E.; Lee, M.H.; Ha, S.J.; Kim, H.Y.; Kim, M.J.; Lee, S.J.; Madsen, S.M.; Park, C.S.
Extracellular secretion of a maltogenic amylase from Lactobacillus gasseri ATCC33323 in Lactococcus lactis MG1363 and its application on the production of branched maltooligosaccharides
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Lactobacillus gasseri, Lactobacillus gasseri ATCC 33323
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Mabrouk, S.B.; Messaoud, E.B.; Ayadi, D.; Jemli, S.; Roy, A.; Mezghani, M.; Bejar, S.
Cloning and sequencing of an original gene encoding a maltogenic amylase from Bacillus sp. US149 strain and characterization of the recombinant activity
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Bacillus sp. (in: Bacteria) (A7DWA8), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) US149 (A7DWA8)
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Jones, A.; Lamsa, M.; Frandsen, T.P.; Spendler, T.; Harris, P.; Sloma, A.; Xu, F.; Nielsen, J.B.; Cherry, J.R.
Directed evolution of a maltogenic alpha-amylase from Bacillus sp. TS-25
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Goesaert, H.; Leman, P.; Bijttebier, A.; Delcour, J.A.
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brenda
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Thermus sp.
brenda
Li, X.; Li, D.; Yin, Y.; Park, K.H.
Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity
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Thermofilum pendens, Thermofilum pendens Hrk 5 (DSM 2475)
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Li, D.; Park, J.T.; Li, X.; Kim, S.; Lee, S.; Shim, J.H.; Park, S.H.; Cha, J.; Lee, B.H.; Kim, J.W.; Park, K.H.
Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100 degrees C, from the hyperthermophilic archaeon Staphylothermus marinus
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Geobacillus stearothermophilus
brenda
Kolcuoglu, Y.; Colak, A.; Faiz, O.; Belduz, A.
Cloning, expression and characterization of highly thermo- and pH-stable maltogenic amylase from a thermophilic bacterium Geobacillus caldoxylosilyticus TK4
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Parageobacillus caldoxylosilyticus (C0LZ63), Parageobacillus caldoxylosilyticus TK4 (C0LZ63)
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brenda
Ben Mabrouk, S.; Aghajari, N.; Ben Ali, M.; Ben Messaoud, E.; Juy, M.; Haser, R.; Bejar, S.
Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions
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Bacillus sp. (in: Bacteria) (A7DWA8), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) US149 (A7DWA8)
brenda
Bijttebier, A.; Goesaert, H.; Delcour, J.
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brenda
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Thermofilum pendens
brenda
Jung, J.H.; Seo, D.H.; Holden, J.F.; Park, C.S.
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Pyrococcus sp. (I3RE04), Pyrococcus sp. ST04 (I3RE04)
brenda
Jeon, E.J.; Jung, J.H.; Seo, D.H.; Jung, D.H.; Holden, J.F.; Park, C.S.
Bioinformatic and biochemical analysis of a novel maltose-forming alpha-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1
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Thermococcus sp. (I3ZTN9), Thermococcus sp. CL1 (I3ZTN9)
brenda
Jun, S.Y.; Kim, J.S.; Choi, K.H.; Cha, J.; Ha, N.C.
Structure of a novel alpha-amylase AmyB from Thermotoga neapolitana that produces maltose from the nonreducing end of polysaccharides
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Thermotoga neapolitana (B5ARZ9)
brenda
Park, K.H.; Jung, J.H.; Park, S.G.; Lee, M.E.; Holden, J.F.; Park, C.S.; Woo, E.J.
Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04
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Pyrococcus sp. (I3RE04), Pyrococcus sp. ST04 (I3RE04)
brenda
Miao, M.; Xiong, S.; Ye, F.; Jiang, B.; Cui, S.W.; Zhang, T.
Development of maize starch with a slow digestion property using maltogenic alpha-amylase
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Geobacillus stearothermophilus
brenda
Derde, L.J.; Gomand, S.V.; Courtin, C.M.; Delcour, J.A.
Characterisation of three starch degrading enzymes: thermostable beta-amylase, maltotetraogenic and maltogenic alpha-amylases
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Geobacillus stearothermophilus
brenda
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Combined impact of Bacillus stearothermophilus maltogenic alpha-amylase and surfactants on starch pasting and gelation properties
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Geobacillus stearothermophilus
brenda
Li, X.; Li, D.; Tian, H.; Park, K.
Reducing retrogradation of gelatinized rice starch and rice meal under low temperature storage by addition of extremely thermostable maltogenic amylase during their cooking
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Thermofilum pendens
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brenda
Khemakhem, B.; Fendri, I.; Dahech, I.; Belghuith, K.; Kammoun, R.; Mejdoub, H.
Purification and characterization of a maltogenic amylase from Fenugreek (Trigonella foenum graecum) seeds using the Box Benkhen Design (BBD)
Ind. Crops Prod.
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Trigonella foenum-graecum
brenda
Nasrollahi, S.; Golalizadeh, L.; Sajedi, R.H.; Taghdir, M.; Asghari, S.M.; Rassa, M.
Substrate preference of a Geobacillus maltogenic amylase: a kinetic and thermodynamic analysis
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Geobacillus sp. (E0X988)
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Jung, T.Y.; Li, D.; Park, J.T.; Yoon, S.M.; Tran, P.L.; Oh, B.H.; Janecek, ?.; Park, S.G.; Woo, E.J.; Park, K.H.
Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus
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Staphylothermus marinus (A3DM60), Staphylothermus marinus DSM 3639 (A3DM60)
brenda
Ben Mabrouk, S.; Ayadi, D.Z.; Ben Hlima, H.; Bejar, S.
Thermostability improvement of maltogenic amylase MAUS149 by error prone PCR
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Bacillus sp. (in: Bacteria) (A7DWA8), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) US149 (A7DWA8)
brenda
Ben Mabrouk, S.; Ayadi-Zouari, D.; Ben Hlima, H.; Bejar, S.
Changes in the catalytic properties and substrate specificity of Bacillus sp. US149 maltogenic amylase by mutagenesis of residue 46
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40
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Bacillus sp. (in: Bacteria) (A7DWA8), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) US149 (A7DWA8)
brenda
Samant, S.; Gupta, G.; Karthikeyan, S.; Haq, S.F.; Nair, A.; Sambasivam, G.; Sukumaran, S.
Effect of codon-optimized E. coli signal peptides on recombinant Bacillus stearothermophilus maltogenic amylase periplasmic localization, yield and activity
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Geobacillus stearothermophilus
brenda
Mehta, D.; Satyanarayana, T.
Dimerization mediates thermo-adaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovorans
PLoS ONE
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Geobacillus thermoleovorans (G8N704)
brenda
Abdul Manas, N.H.; Pachelles, S.; Mahadi, N.M.; Illias, R.M.
The characterisation of an alkali-stable maltogenic amylase from Bacillus lehensis G1 and improved malto-oligosaccharide production by hydrolysis suppression
PLoS ONE
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Alkalihalobacillus lehensis (X5CPN2), Alkalihalobacillus lehensis G1 (X5CPN2)
brenda
Herale, R.; Sukumaran, U.; Kadeppagari, R.
Evidence for the improvement of thermostability of the maltogenic alpha-amylase of Aspergillus niger by negative pressure
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Aspergillus niger
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brenda
Rahmati, P.; Sajedi, R.H.; Zamani, P.; Rahmani, H.; Khajeh, K.
Allosteric properties of Geobacillus maltogenic amylase
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Geobacillus sp. Gh6 (E0X988)
brenda
Straksys, A.; Kochane, T.; Budriene, S.
Catalytic properties of maltogenic alpha-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles
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Geobacillus stearothermophilus (P19531)
brenda
Guo, L.; Tao, H.; Cui, B.; Janaswamy, S.
The effects of sequential enzyme modifications on structural and physicochemical properties of sweet potato starch granules
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Geobacillus stearothermophilus
brenda
Sulong, M.; Leow, T.; Rahman, R.; Basri, M.; Salleh, A.
Characteristics of recombinant maltogenic amylase from Geobacillus sp. SK70
Indian J. Biotechnol.
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91-99
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Geobacillus sp. SK70
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brenda
Li, X.; Wang, Y.; Park, J.T.; Gu, L.; Li, D.
An extremely thermostable maltogenic amylase from Staphylothermus marinus Bacillus expression of the gene and its application in genistin glycosylation
Int. J. Biol. Macromol.
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2018
Staphylothermus marinus (A3DM60), Staphylothermus marinus ATCC 43588 (A3DM60)
brenda
Mehta, D.; Satyanarayana, T.
Structural elements of thermostability in the maltogenic amylase of Geobacillus thermoleovorans
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Geobacillus thermoleovorans (I6RE37), Geobacillus thermoleovorans
brenda
Sun, Y.; Duan, X.; Wang, L.; Wu, J.
Enhanced maltose production through mutagenesis of acceptor binding subsite +2 in Bacillus stearothermophilus maltogenic amylase
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Geobacillus stearothermophilus (P19531)
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Maciulyte, S.; Kochane, T.; Budriene, S.
Microencapsulation of maltogenic alpha-amylase in poly(urethane-urea) shell inverse emulsion method
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Geobacillus stearothermophilus (P19531), Geobacillus stearothermophilus
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Manas, N.H.; Bakar, F.D.; Illias, R.M.
Computational docking, molecular dynamics simulation and subsite structure analysis of a maltogenic amylase from Bacillus lehensis G1 provide insights into substrate and product specificity
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Alkalihalobacillus lehensis (X5CPN2), Alkalihalobacillus lehensis G1 (X5CPN2)
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