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2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranoside
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside-6-phosphate + H2O
2-nitrophenol + D-galactopyranoside-6-phosphate
-
-
-
?
2-nitrophenyl beta-D-galactoside
2-nitrophenol + D-galactose
-
-
-
r
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranoside
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucose
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylopyranose
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinose
-
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-galactopyranoside is 7.6% compared to catalytic catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
4-nitrophenyl beta-D-galactoside
4-nitrophenol + beta-D-galactose
CelB has a beta-galactosidase activity of 61% of the beta-glucosidase activity
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
at 80°C 61% of the activity with 4-nitrophenyl beta-D-glucoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside
4-nitrophenol + beta-D-glucose
CelB has a beta-galactosidase activity of 61% of the beta-glucosidase activity
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannose
catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-mannopyranoside is 0.7% compared to catalytic catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
cellobiose + H2O
2 beta-D-glucose
-
-
-
?
cellobiose + H2O
2 D-glucose
-
-
-
?
cellobiose + H2O
?
-
as active as 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
D-glucose + D-glucose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
D-glucose
gluco-oligosaccharides + H2O
-
study on the effect of pressure on the reaction equilibrium. Oligosaccharides are synthesized from glucose in an equilibrium reaction at pressures from 0.1 to 500 MPa. The enzyme remains active at 500 MPa. The equilibrium of the reaction is influenced by pressure and shifts towards the hydrolysis side, decreasing final oligosaccharide concentrations with increasing pressure. This pressure dependence of the final product concentration and the equilibrium constant can be described with a positive reaction volume of 2.4 mol/cm3
-
?
daidzin + H2O
beta-D-glucose + daidzein
-
-
-
?
diosmin + H2O
diosmetin + rutinose
-
-
-
?
genistin + H2O
beta-D-glucose + genistein
-
-
-
?
ginsenoside Rb1 + 4 H2O
protopanaxadiol aglycone + 4 D-glucopyranose
-
-
-
?
ginsenoside Rb2 + 4 H2O
protopanaxadiol aglycone + 3 D-glucopyranose + L-arabinopyranose
-
-
-
?
ginsenoside Rc + 4 H2O
protopanaxadiol aglycone + 3 D-glucopyranose + L-arabinopyranose
-
-
-
?
ginsenoside Rc + H2O
(3beta,12beta)-dammar-24-ene-3,12,20-triol + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rd + 3 H2O
protopanaxadiol aglycone + 3 D-glucopyranose
-
-
-
?
glycitin + H2O
beta-D-glucose + glycitein
i.e. glycitein 7-O-beta-glucoside
-
-
?
hesperidin + H2O
hesperetin + rutinose
-
-
-
?
isoquercitrin + H2O
quercetin + beta-D-glucose
i.e. quercetin 3-O-beta-D-glucoside
-
-
?
lactose + H2O
D-glucose + D-galactose
lactose + N,N'-diacetylchitobiose
Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc + H2O
-
-
-
?
mannooligosaccharide + H2O
?
hydrolysis of mannose from the reducing end
-
-
?
methyl beta-D-galactoside
methanol + D-galactose
-
-
-
r
N-acetyl-D-glucosamine + lactose
4-O-beta-D-galactopyranosyl-N-acetyl-D-glucosamine + D-glucose
-
transgalactosylation reaction
-
?
naringin + H2O
naringenin + rutinose
-
-
-
?
narirutin + H2O
naringenin + neohesperidose
-
-
-
?
neohesperidin + H2O
hesperetin + neohesperidose
-
-
-
?
neoponcirin + H2O
isosakuranetin + rutinose
-
-
-
?
pentyl beta-D-glucopyranoside + H2O
pentanol + beta-D-glucopyranose
-
-
-
?
poncirin + H2O
isosakuranetin + neohesperidose
-
-
-
?
quercitrin + H2O
quercetin + alpha-L-rhamnose
i.e. quercetin 3-O-alpha-L-rhamnoside
-
-
?
rutin + H2O
quercetin + rutinose
-
-
-
?
additional information
?
-
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
37% of the activity compared to 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
hydrolysed at 34% compared to activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
114% of the activity compared to 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
37% of the activity compared to 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
hydrolysed at 9.2% compared to activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
lactose + H2O
D-glucose + D-galactose
-
-
-
-
?
lactose + H2O
D-glucose + D-galactose
-
-
-
?
lactose + H2O
D-glucose + D-galactose
-
-
-
r
lactose + H2O
D-glucose + D-galactose
-
-
-
?
lactose + H2O
D-glucose + D-galactose
-
lactose is hydrolyzed into glucose and galactose, and then tri-, tetra-, and pentasaccharides are synthesized. The conversion rate for lactose increases with temperature, directly resulting in an increase in both the rate of hydrolysis and the rate of oligosaccharide synthesis. Because the increase in production rate is faster for oligosaccharide synthesis than for hydrolysis, relatively more oligosaccharides are produced at higher temperatures. At 50°C the optimum in oligosaccharide concentration, of which the occurrence is typical for a kinetically controlled reaction, is not yet reached after 250 h. At 95°C this optimum is reached within 4 h
-
r
lactose + H2O
D-glucose + D-galactose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
additional information
?
-
the enzyme also shows transglucosylation activity
-
-
?
additional information
?
-
the enzyme shows also beta-rutinosidase activity with rutin (hydrolysis of rutin to quercetin and rutinose)
-
-
?
additional information
?
-
the enzyme shows transglycosylation and transgalactosylation activities toward cellobiose, lactose and mannooligosaccharides that could produce galactooligosaccharides and maltooligosaccharides. It can not hydrolyze alpha-form substrates and bulk polymers like mannan and starch
-
-
?
additional information
?
-
the transferase activity of the enzyme can be improved significantly by addition of the ionic liquid 1,3-dimethylimidazoliummethylsulfate. The relative enhancement of the selectivity of the enzyme for glycosyl transfer to the acceptor nucleophile compared with water by the cosolvent is strongly dependent on the structure of the acceptor, suggesting that interactions of the acceptor with solvent molecules, water or ionic liquid, make a major contribution to the observed transgalactosylation specificity of the enzyme
-
-
?
additional information
?
-
the enzyme catalyzes the conversion of lactose to hexyl-beta-galactoside in hexanol (transgalactosylation reaction)
-
-
?
additional information
?
-
the transfer of the galactosyl group from lactose to acceptors such as lactose or D-glucose rather than water is significant and depends on the initial lactose concentration as well as the time-dependent substrate/product ratio during batchwise lactose conversion
-
-
?
additional information
?
-
enzyme additionally catalyzes transglycosylation reactions, making new beta(1->3) and beta(1->6) glycosidic bonds by intermolecular as well as intramolecular transfer reactions. The intramolecular galactosyl transfer of CelB yields beta-D-Galp-(1->6)-D-glucose and beta-D-Galp-(1->3)-D-glucose in a molar ratio of about 1 : 2. Galactosyl transfer from CelB to D-glucose occurs with partitioning ratios, kNu /kwater, which are 170 times those for the reactions of the galactosylated enzyme with 2-propanol. Therefore, the binding interactions with nucleophiles contribute chiefly to formation of new beta-glycosides during lactose conversion. Likewise, noncovalent interactions with the glucose leaving group govern the catalytic efficiencies for the hydrolysis of lactose
-
-
?
additional information
?
-
enzyme catalyzes both hydrolysis and transglycosylation of glycosidc substrates. In hexanol/water two-phase systems, hydrolysis is by far the dominating reaction even though the total activity increases. In hexanol containing various amounts of water, the selectivity for the alcohol increases with increasing water activity. This counteracts the effect of higher water concentration and the transglycosylation/hydrolysis ratio increases with increasing water activity
-
-
?
additional information
?
-
enzyme converts ginsenosides Rb1, Rb2, Rc, and Rd to protopanaxadiol aglycone via compound K
-
-
?
additional information
?
-
enzyme is able to catalyze formation of lacto-N-neotetraose, i.e. Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc, from lactose and N,N'-diacetylchitobiose and of N-acetyllactosamine, i.e Gal-beta(1,4)-GlcNAc from N-acetylglucosamine and lactose. When compared with beta-glycosidase BglT from Thermus thermophilus, and beta-galactosidase BgaD-D from Bacillus circulans, BgaD is the most potent transgalactosidase, but both BglT and CelB can catalyze formation of LNnT and LacNAc, with BglT giving higher yields than CelB
-
-
?
additional information
?
-
enzyme shows transglucosylation activity with glucosyl donors 2-nitrophenyl beta-D-glucoside and cellobiose. Transglucosylation products are 1-O-beta-D-glucopyranosyl-rac-glycerol (79%) and 2-O-beta-D-glucopyranosyl-sn-glycerol (21%)
-
-
?
additional information
?
-
-
the enzyme also contains alpha-L-arabinofuranosidase activity
-
-
?
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0.12 - 42
2-nitrophenyl beta-D-galactopyranoside
16 - 38
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
5.3
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
0.1 - 59
2-nitrophenyl beta-D-glucopyranoside
0.7 - 22
4-nitrophenyl beta-D-galactopyranoside
1.3 - 7.2
4-nitrophenyl beta-D-galactoside
0.02 - 13.9
4-nitrophenyl beta-D-glucopyranoside
2.6 - 49
4-nitrophenyl beta-D-glucoside
0.03 - 1.5
4-nitrophenyl beta-D-mannopyranoside
0.42
daidzin
pH 6.0, 95°C
0.5
genistin
pH 6.0, 95°C
0.33
glycitin
pH 6.0, 95°C
1.6
hesperidin
pH 5.5, 95°C
0.17
isoquercitrin
pH 5.0, 95°C
861
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
1.7
naringin
pH 5.5, 95°C
3.7
narirutin
pH 5.5, 95°C
4.6
neohesperidin
pH 5.5, 95°C
46
pentyl beta-D-glucopyranoside
pH 5.0, 80°C, 6% water, 94% hexanol
3.095
quercitrin
pH 5.0, 95°C
additional information
additional information
mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
-
0.12
2-nitrophenyl beta-D-galactopyranoside
pH 5.0, 100°C
0.89
2-nitrophenyl beta-D-galactopyranoside
mutant F426Y, pH 5.0, 90°C
2.3
2-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.0, 90°C
2.57
2-nitrophenyl beta-D-galactopyranoside
pH 5.4, 75°C
4.8
2-nitrophenyl beta-D-galactopyranoside
mutant M424K, pH 5.0, 90°C
5.3
2-nitrophenyl beta-D-galactopyranoside
pH 5.5, 80°C
40
2-nitrophenyl beta-D-galactopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
42
2-nitrophenyl beta-D-galactopyranoside
mutant E417S, pH 5.0, 90°C
16
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S/M424K/F426Y, pH 5.0, 90°C
22
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S, pH 5.0, 90°C
31
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
wild-type, pH 5.0, 90°C
38
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant F426Y, pH 5.0, 90°C
0.1
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.22
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
0.25
2-nitrophenyl beta-D-glucopyranoside
pH 5.4, 75°C
0.28
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.0, 90°C
0.28
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C
0.3
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.51
2-nitrophenyl beta-D-glucopyranoside
mutant M424K, pH 5.0, 90°C
0.57
2-nitrophenyl beta-D-glucopyranoside
mutant F426Y, pH 5.0, 90°C
1.3
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 5.0, 65°C
1.49
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 6.5, 65°C, presence of 2 M formate
2.1
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 4.0, 65°C
4.3
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 3.0, 65°C
29
2-nitrophenyl beta-D-glucopyranoside
mutant E417S, pH 5.0, 90°C
59
2-nitrophenyl beta-D-glucopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
0.7
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 20°C
1.11
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 30°C
1.2
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 20°C
1.3
4-nitrophenyl beta-D-galactopyranoside
mutant T371A, pH 4.8, 20°C
1.31
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 40°C
1.97
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 65°C
2.05
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 50°C
2.09
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 60°C
2.6
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 70°C
2.8
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 75°C
3.4
4-nitrophenyl beta-D-galactopyranoside
mutant M424V, pH 4.8, 20°C
4.1
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 85°C
4.5
4-nitrophenyl beta-D-galactopyranoside
mutant A419T, pH 4.8, 20°C
5
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, wild-type enzyme
5
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 90°C
8.5
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 90°C
15.7
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme N206D
21.7
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
22
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
1.3
4-nitrophenyl beta-D-galactoside
pH 5.0, 90°C
4.6
4-nitrophenyl beta-D-galactoside
pH 5.0, 70°C
7.2
4-nitrophenyl beta-D-galactoside
pH 5.0, 50°C
0.02
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.05
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.09
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 100°C
0.15
4-nitrophenyl beta-D-glucopyranoside
-
pH 5, 80°C
0.19
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, wild-type enzyme
0.37
4-nitrophenyl beta-D-glucopyranoside
pH 5.4, 75°C
0.39
4-nitrophenyl beta-D-glucopyranoside
90°C, pH not specified in the publication, enzyme from Pyrococcus furiosus
0.39
4-nitrophenyl beta-D-glucopyranoside
pH 6.5, temperature not specified in the publication, recombinant enzyme
0.41
4-nitrophenyl beta-D-glucopyranoside
90°C, pH not specified in the publication, enzyme expressed in Escherichia coli
0.41
4-nitrophenyl beta-D-glucopyranoside
pH 6.5, temperature not specified in the publication, enzyme purified from Pyrococcus furiosus
0.42
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 4.8, 90°C
0.53
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 4.8, 20°C
0.57
4-nitrophenyl beta-D-glucopyranoside
mutant T371A, pH 4.8, 20°C
0.8
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 70°C
0.92
4-nitrophenyl beta-D-glucopyranoside
mutant M424V, pH 4.8, 20°C
1.1
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 20°C
1.3
4-nitrophenyl beta-D-glucopyranoside
mutant A419T, pH 4.8, 20°C
1.4
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 90°C
4.6
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme N206D
13.8
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
13.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
2.6
4-nitrophenyl beta-D-glucoside
pH 5.0, 90°C
9.1
4-nitrophenyl beta-D-glucoside
pH 5.0, 70°C
20
4-nitrophenyl beta-D-glucoside
pH 5.0, 50°C
21
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme F426Y
27
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K/F426Y
39
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K
49
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, wild-type enzyme
0.03
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.05
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.09
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 100°C
0.1
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
0.15
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
0.63
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme N206D
0.64
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.3
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, wild-type enzyme
1.5
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
0.04
cellobiose
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.07
cellobiose
pH 5.0, 100°C
0.38
cellobiose
pH 5.0, 95°C, mutant enzyme Q150W
2 - 3
cellobiose
wild-type, pH 4.8, 20°C
3.2
cellobiose
pH 5.0, 70°C
11
cellobiose
mutant T371A, pH 4.8, 20°C
14
cellobiose
wild-type, pH 4.8, 90°C
16
cellobiose
mutant M424V, pH 4.8, 20°C
20
cellobiose
-
pH 5, 80°C
20
cellobiose
mutant N4515S, pH 4.8, 20°C
25
cellobiose
mutant A419T, pH 4.8, 20°C
38
cellobiose
mutant N4515S, pH 4.8, 90°C
0.01
lactose
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.03
lactose
pH 5.0, 95°C, mutant enzyme Q150W
0.04
lactose
pH 5.0, 100°C
49
lactose
-
pH 5.5, 70°C, enzyme immobilized on Eupergit C
52
lactose
mutant T371A, pH 4.8, 20°C
52
lactose
wild-type, pH 4.8, 20°C
59.8
lactose
pH 5.0, 70°C
61
lactose
-
pH 5.5, 70°C, soluble enzyme
62
lactose
-
pH 5.5, 70°C, enzyme immobilized on chitosan
83
lactose
mutant A419T, pH 4.8, 20°C
95
lactose
mutant N4515S, pH 4.8, 20°C
97
lactose
mutant M424V, pH 4.8, 20°C
120
lactose
wild-type, pH 4.8, 90°C
186
lactose
release of D-glucose, pH 7.5, 80°C
202
lactose
-
pH 5.5, 70°C, enzyme immobilized on controlled pore glass
220
lactose
mutant N4515S, pH 4.8, 90°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.23 - 9600
2-nitrophenyl beta-D-galactopyranoside
26 - 171
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
10000
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
0.22 - 3300
2-nitrophenyl beta-D-glucopyranoside
4.2 - 4863
4-nitrophenyl beta-D-galactopyranoside
0.05 - 2600
4-nitrophenyl beta-D-glucopyranoside
0.8 - 7.1
4-nitrophenyl beta-D-glucoside
0.11 - 65.9
4-nitrophenyl beta-D-mannopyranoside
1880
daidzin
pH 6.0, 95°C
6050
genistin
pH 6.0, 95°C
610
glycitin
pH 6.0, 95°C
68.4
hesperidin
pH 5.5, 95°C
53.3
isoquercitrin
pH 5.0, 95°C
8.3
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
27.7
naringin
pH 5.5, 95°C
74.1
narirutin
pH 5.5, 95°C
84.8
neohesperidin
pH 5.5, 95°C
0.22
quercitrin
pH 5.0, 95°C
additional information
additional information
mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
-
0.23
2-nitrophenyl beta-D-galactopyranoside
pH 5.0, 100°C
20 - 50
2-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.0, 90°C
175
2-nitrophenyl beta-D-galactopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
892
2-nitrophenyl beta-D-galactopyranoside
mutant F426Y, pH 5.0, 90°C
1060
2-nitrophenyl beta-D-galactopyranoside
mutant E417S, pH 5.0, 90°C
1880
2-nitrophenyl beta-D-galactopyranoside
mutant M424K, pH 5.0, 90°C
9600
2-nitrophenyl beta-D-galactopyranoside
pH 5.4, 75°C
26
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant F426Y, pH 5.0, 90°C
49
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
wild-type, pH 5.0, 90°C
69
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S/M424K/F426Y, pH 5.0, 90°C
171
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S, pH 5.0, 90°C
0.22
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.45
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 5.0, 65°C
0.67
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
3.9
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 6.5, 65°C, presence of 2 M formate
6.7
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 4.0, 65°C
47.6
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 3.0, 65°C
772
2-nitrophenyl beta-D-glucopyranoside
mutant M424K, pH 5.0, 90°C
777
2-nitrophenyl beta-D-glucopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
840
2-nitrophenyl beta-D-glucopyranoside
mutant F426Y, pH 5.0, 90°C
860
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.0, 90°C
1189
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
1797
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C
3300
2-nitrophenyl beta-D-glucopyranoside
pH 5.4, 75°C
3300
2-nitrophenyl beta-D-glucopyranoside
mutant E417S, pH 5.0, 90°C
4.2
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 20°C
9.1
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 20°C
11
4-nitrophenyl beta-D-galactopyranoside
mutant T371A, pH 4.8, 20°C
12
4-nitrophenyl beta-D-galactopyranoside
mutant M424V, pH 4.8, 20°C
14
4-nitrophenyl beta-D-galactopyranoside
mutant A419T, pH 4.8, 20°C
29.2
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
69.2
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
90
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 30°C
180
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme N206D
236
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 40°C
298
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 70°C
580
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 50°C
1000
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 90°C
1222
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 60°C
1486
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 65°C
2400
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 90°C
2827
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, wild-type enzyme
2907
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 75°C
4863
4-nitrophenyl beta-D-galactopyranoside
pH 5.4, 85°C
0.05
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.13
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.26
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 100°C
13
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 4.8, 20°C
26
4-nitrophenyl beta-D-glucopyranoside
mutant T371A, pH 4.8, 20°C
40
4-nitrophenyl beta-D-glucopyranoside
mutant A419T, pH 4.8, 20°C
40
4-nitrophenyl beta-D-glucopyranoside
mutant M424V, pH 4.8, 20°C
47
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 20°C
116
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme N206D
172
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
206
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 70°C
207
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
1140
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, wild-type enzyme
1400
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 90°C
1600
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 4.8, 90°C
2600
4-nitrophenyl beta-D-glucopyranoside
pH 5.4, 75°C
0.8
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K/F426Y
0.9
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme F426Y
5
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K
7.1
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, wild-type enzyme
0.11
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.13
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.3
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 100°C
0.85
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.02
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.22
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.9
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.97
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme N206D
65.9
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, wild-type enzyme
0.1
cellobiose
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.16
cellobiose
pH 5.0, 100°C
0.74
cellobiose
pH 5.0, 95°C, mutant enzyme Q150W
15
cellobiose
mutant T371A, pH 4.8, 20°C
16
cellobiose
wild-type, pH 4.8, 20°C
18
cellobiose
mutant M424V, pH 4.8, 20°C
19
cellobiose
mutant A419T, pH 4.8, 20°C
20
cellobiose
mutant N4515S, pH 4.8, 20°C
37.6
cellobiose
pH 5.0, 70°C
240
cellobiose
mutant N4515S, pH 4.8, 90°C
454
cellobiose
-
pH 5, 80°C
670
cellobiose
wild-type, pH 4.8, 90°C
0.03
lactose
pH 5.0, 95°C, mutant enzyme Q150W
0.03
lactose
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.08
lactose
pH 5.0, 100°C
13
lactose
wild-type, pH 4.8, 20°C
15
lactose
mutant A419T, pH 4.8, 20°C
17
lactose
mutant T371A, pH 4.8, 20°C
21
lactose
mutant M424V, pH 4.8, 20°C
21
lactose
mutant N4515S, pH 4.8, 20°C
530
lactose
mutant N4515S, pH 4.8, 90°C
1300
lactose
wild-type, pH 4.8, 90°C
3800
lactose
release of D-glucose, pH 7.5, 80°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.89 - 1000
2-nitrophenyl beta-D-galactopyranoside
0.7 - 7.7
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
1900
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
0.3 - 6480
2-nitrophenyl beta-D-glucopyranoside
1.3 - 561
4-nitrophenyl beta-D-galactopyranoside
2.44 - 7337
4-nitrophenyl beta-D-glucopyranoside
1.3 - 49.8
4-nitrophenyl beta-D-mannopyranoside
42.1
hesperidin
pH 5.5, 95°C
0.01
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
16.5
naringin
pH 5.5, 95°C
19.8
narirutin
pH 5.5, 95°C
18.5
neohesperidin
pH 5.5, 95°C
additional information
additional information
mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
-
1.89
2-nitrophenyl beta-D-galactopyranoside
pH 5.0, 100°C
4.4
2-nitrophenyl beta-D-galactopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
25.3
2-nitrophenyl beta-D-galactopyranoside
mutant E417S, pH 5.0, 90°C
396
2-nitrophenyl beta-D-galactopyranoside
mutant M424K, pH 5.0, 90°C
899
2-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.0, 90°C
1000
2-nitrophenyl beta-D-galactopyranoside
mutant F426Y, pH 5.0, 90°C
0.7
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant F426Y, pH 5.0, 90°C
1.6
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
wild-type, pH 5.0, 90°C
4.2
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S/M424K/F426Y, pH 5.0, 90°C
7.7
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S, pH 5.0, 90°C
0.3
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 5.0, 65°C
2.17
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
2.26
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
2.6
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 6.5, 65°C, presence of 2 M formate
3.1
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 4.0, 65°C
10.9
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 3.0, 65°C
13
2-nitrophenyl beta-D-glucopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
113
2-nitrophenyl beta-D-glucopyranoside
mutant E417S, pH 5.0, 90°C
1484
2-nitrophenyl beta-D-glucopyranoside
mutant F426Y, pH 5.0, 90°C
1510
2-nitrophenyl beta-D-glucopyranoside
mutant M424K, pH 5.0, 90°C
4048
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.0, 90°C
5350
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
6480
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C
1.3
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
3.1
4-nitrophenyl beta-D-galactopyranoside
mutant A419T, pH 4.8, 20°C
3.2
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
3.4
4-nitrophenyl beta-D-galactopyranoside
mutant M424V, pH 4.8, 20°C
3.5
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 20°C
8.2
4-nitrophenyl beta-D-galactopyranoside
mutant T371A, pH 4.8, 20°C
11.5
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme N206D
13
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 20°C
115
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 70°C
120
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 90°C
480
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 90°C
561
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, wild-type enzyme
2.44
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
2.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 100°C
2.95
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
12.3
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
14.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
24.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme N206D
25
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 4.8, 20°C
31
4-nitrophenyl beta-D-glucopyranoside
mutant A419T, pH 4.8, 20°C
43
4-nitrophenyl beta-D-glucopyranoside
mutant M424V, pH 4.8, 20°C
43
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 20°C
45
4-nitrophenyl beta-D-glucopyranoside
mutant T371A, pH 4.8, 20°C
258
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 70°C
1000
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 90°C
3900
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 4.8, 90°C
7337
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, wild-type enzyme
1.3
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.9
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
2.83
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
3.02
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 100°C
3.1
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme N206D
3.63
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
5.7
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
10.2
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
49.8
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, wild-type enzyme
0.69
cellobiose
wild-type, pH 4.8, 20°C
0.75
cellobiose
mutant A419T, pH 4.8, 20°C
1
cellobiose
mutant N4515S, pH 4.8, 20°C
1.1
cellobiose
mutant M424V, pH 4.8, 20°C
1.4
cellobiose
mutant T371A, pH 4.8, 20°C
1.92
cellobiose
pH 5.0, 95°C, mutant enzyme Q150W
2.28
cellobiose
pH 5.0, 100°C
2.71
cellobiose
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
11.8
cellobiose
pH 5.0, 70°C
1000
cellobiose
mutant N4515S, pH 4.8, 90°C
2400
cellobiose
wild-type, pH 4.8, 90°C
0.18
lactose
mutant A419T, pH 4.8, 20°C
0.22
lactose
mutant M424V, pH 4.8, 20°C
0.22
lactose
mutant N4515S, pH 4.8, 20°C
0.25
lactose
wild-type, pH 4.8, 20°C
0.33
lactose
mutant T371A, pH 4.8, 20°C
1.36
lactose
pH 5.0, 95°C, mutant enzyme Q150W
1.82
lactose
pH 5.0, 100°C
2.21
lactose
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
2.4
lactose
mutant N4515S, pH 4.8, 90°C
4.78
lactose
pH 5.0, 70°C
11
lactose
wild-type, pH 4.8, 90°C
20.4
lactose
release of D-glucose, pH 7.5, 80°C
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0.011
substrate: rutin, pH 5.5, 95°C
0.081
substrate: neoponcirin, pH 5.5, 95°C
0.085
substrate: diosmin, pH 5.5, 95°C
0.091
substrate: poncirin, pH 5.5, 95°C
0.102
substrate naringin, pH 5.5, 95°C
0.103
substrate: neohesperidin, pH 5.5, 95°C
0.153
substrate: narirutin, pH 5.5, 95°C
0.172
substrate: hesperidin, pH 5.5, 95°C
0.23
substrate: quercitrin, pH 5.0, 95°C
0.28
mutant E372A, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
0.55
substrate ginsenoside Rb2, pH 5.5, 95°C
0.83
pH 5.0, 90°C, addition of aerosol dioctyl sulfosuccinate
1049
wild-type, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
13.04
pH 5.0, 90°C, lyophilized enzyme
15
substrate 4-nitrophenyl alpha-L-arabinopyranoside, pH 5.5, 95°C
180
substrate: daidzin, pH 6.0, 95°C
2.75
pH 5.0, 90°C, enzyme immobilized on XAD-4
220
substrate: isoquercitrin, pH 5.0, 95°C
291
wild-type, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
3.18
pH 5.0, 90°C, enzyme immobilized on XAD-16
320
wild-type, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
330
substrate: genistin, pH 6.0, 95°C
4.7
mutant E372A, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
4.77
pH 5.0, 90°C, enzyme immobilized on Celite
5.5
substrate ginsenoside Rd, pH 5.5, 95°C
529
substrate 2-nitrophenyl beta-D-galactopyranoside, pH 5.5, 95°C
534
wild-type, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
561
substrate 4-nitrophenyl beta-D-galactopyranoside, pH 5.5, 95°C
66
wild-type, substrate cellobiose, pH 3.0, 65°C
8.3
mutant E372A, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
828
substrate 2-nitrophenyl beta-D-glucopyranoside, pH 5.5, 95°C
885
recombinant protein, 90°C, pH 5.0
0.08
mutant E372A, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
0.08
substrate ginsenoside Rc, pH 5.5, 95°C
4.5
substrate 4-nitrophenyl alpha-L-arabinofuranoside, pH 5.5, 95°C
4.5
substrate ginsenoside Rb1, pH 5.5, 95°C
75
substrate: glycitin, pH 6.0, 95°C
75
wild-type, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
912
substrate: 4-nitrophenyl-beta-D-glucopyranoside, pH 6.0, 95°C
912
substrate 4-nitrophenyl beta-D-glucopyranoside, pH 5.5, 95°C
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A419T
159% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 109% with 4-nitrophenyl beta-D-galactoside, 53% residual activity after 1 h at 106°C
E372D
200-fold reduction in specific activity
E372Q
1000-fold reduction in specific activity
E386G
mutation in nucleophile residue E387, mutation completely abolishes activity under statndard conditions. The addition of 2 M sodium formate as an external nucleophile leads to the recovery of 8.40% activity with accumulation of oligosaccharides. At pH 3.0 and low concentrations of sodium formate buffer, the hyperthermophilic glycosynthase shows kcat values similar to those of the wild-type and 17fold higher than those observed at the usual reactivation conditions in 2 M sodium formate at pH 6.5
E417S
mutation in phosphate binding site, 5fold increase of the efficiency of hydrolyzing o-nitrophenol-beta-D-galactopyranoside-6-phosphate. Activity on nonphosphorylated sugars is largely reduced
E417S/M424K/F426Y
mutations in phosphate binding site, 3fold increase of the efficiency of hydrolyzing 2-nitrophenyl beta-D-galactopyranoside-6-phosphate. Activity on nonphosphorylated sugars is largely reduced
I161V
110% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 37% with 4-nitrophenyl beta-D-galactoside, 84% residual activity after 1 h at 106°C
I67T
110% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 97% with 4-nitrophenyl beta-D-galactoside, 100% residual activity after 1 h at 106°C
K285R
155% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 103% with 4-nitrophenyl beta-D-galactoside, 58% residual activity after 1 h at 106°C
K70R
175% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 147% with 4-nitrophenyl beta-D-galactoside, 1% residual activity after 1 h at 106°C
M424K/F426Y
mutant has lower activity than the wild-type enzyme, but provides a higher ratio of transglucosylation product to hydrolysis products compared to wild-type enzyme
M424V
199% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 140% with 4-nitrophenyl beta-D-galactoside, 24% residual activity after 1 h at 106°C
N206N
about 300fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, about 50fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside
N415S
259% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 64% with 4-nitrophenyl beta-D-galactoside. 7.5fold increase in the ratio of 4-nitrophenyl beta-D-glucopyranoside/p-nitrophenyl beta-D-galactopyranoside hydrolysis, no decrease in thermostability
Q150W
the mutant enzyme has more affinity (Km) towards each substrate but shows lower turnover number (kcat) compared to the wild-type enzyme
Q77R/Q150W
the mutant enzyme has more affinity (Km) towards each substrate but shows lower turnover number (kcat) compared to the wild-type enzyme
R77Q
2000fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, 175fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
R77Q/N206D
about 600fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, about 430fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
T371A
148% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 149% with 4-nitrophenyl beta-D-galactoside, 14% residual activity after 1 h at 106°C
V211A
260% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 151% with 4-nitrophenyl beta-D-galactoside, 1% residual activity after 1 h at 106°C
F426Y
mutant has lower activity than the wild-type enzyme, but provides a higher ratio of transglucosylation product to hydrolysis products compared to wild-type enzyme, 2.6fold increase. The mutant enzyme has higher selectivity over the wide range of temperatures tested
F426Y
mutation in phosphate binding site, results in an increased affinity for galactosides. Activity on nonphosphorylated sugars is largely reduced
M424K
mutant has lower activity than the wild-type enzyme, but provides a higher ratio of transglucosylation product to hydrolysis products compared to wild-type enzyme
M424K
mutation in phosphate binding site, shifting pH optimum from 5.0 to 6.0. Activity on nonphosphorylated sugars is largely reduced
additional information
generation of functional glycoside hydrolase hybrids by shuffling of the genes coding for Pyrococcus furiosus CelB and Sulfolobus solfataricus LacS. Generating of thermostable hybrid beta-glycosidases and isolating high-performance variants
additional information
a mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal. The lack of the C-terminal region does not affect the activity of the enzyme, but disrupts its oligomeric state and hyperthermostability
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degradation
encapsulation of CelB into silica microcapsules for degradation of biomass. The encapsulated enzyme is active at 80-100°C, but diffusion of cellobiose into the silica microcapsules is a rate-limiting step
pharmacology
the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications
additional information
the enzyme converts flavanone glycoside to flavanone aglycone via a one-step reaction. It may be useful in the production of the flavanone aglycones naringenin and hesperetin from flavanone glycosides in citrus extracts
food industry
the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications
food industry
the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C
food industry
-
the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C
synthesis
a continuous stirred-tank reactor charged with the enzyme and operated at steady-state conditions could be a useful reaction system for the production of galacto-oligosaccharides in which composition is narrower and more easily programmable, in terms of the individual components contained, as compared to the batchwise reaction
synthesis
optimization of hexyl-beta-glycoside synthesis from lactose in hexanol at low water activity and high temperature. Compared to other beta-glycosidases in lactose conversion into alkyl glycoside, the enzyme shows high activity in a hexanol one-phase system and synthesized high yields of both hexyl-beta-galactoside and hexyl-beta-glucoside. The enzyme synthesizes yields of 63% galactoside (58.6mM) and 28% glucoside (26.1 mM)
synthesis
-
the immobilized enzyme is useful for the production of galactooligosaccharides by using a packed-bed enzyme reactor operated at 70°C
synthesis
beta-glycosidase converts ginsenosides Rb1, Rb2, Rc, and Rd to protopanaxadiol aglycone via compound K. With increases in the enzyme activity, the productivities increase. The substrate concentration is optimal at ginsenoside Rd or 10% (w/v) ginseng root extract. 4 mM of ginsenoside Rd is converted to 3.3 mM compound K with a yield of 82.5% (mol/mol) and a productivity of 2010 mg per l and h at 1 h and is hydrolyzed completely to the aglycone with 364 mg per l and h after 5 h
synthesis
continuous enzymatic process for the production of the prebiotic disaccharide lactulose through transgalactosylation by CelB. CelB is immobilized onto anion-exchange resin Amberlite IRA-93 or onto Eupergit C with immobilization yields of 72% and 83%, respectively, giving specific activities of 920 nkat/g dry carrier and 1500 nkat/g dry carrier at 75°C with 4-nitrophenyl-beta-D-galactopyranoside as substrate. Maximum lactulose yields of 43% related to the initial lactose concentration are reached. The corresponding productivities are 52 g lactulose per l and h using Amberlite IRA-93 and 15 g lactulose per l and h unsing Eupergit C, respectively. While both carrier-bound CelB preparations are 100% stable for at least 14 days, the half-life of the free CelB in the enzyme membrane reactor is only about 1.5 days
synthesis
development of a microstructured immobilized enzyme reactor for production of beta-glucosylglycerol, transglycosylation reaction, under conditions of continuous flow at 70°C. CelB is covalently attached onto coated microchannel walls to give an effective enzyme activity of 30 U per total reactor working volume of 25 ml. Glycerol causes a concentration-dependent decrease in the conversion of the glucosyl donors 2-nitrophenyl beta-D-glucoside and cellobiose via hydrolysis and strongly suppresses participation of the substrate in the reaction as glucosyl acceptor. The yields of beta-glucosylglycerol are about 80% and 60% based on 2-nitrophenyl beta-D-glucoside and cellobiose converted, respectively, and maintain up to near exhaustion of substrate, giving about 120 mM (30 g/l) of beta-glucosylglycerol from the reaction of cellobiose and 1 M glycerol. The structure of the transglucosylation products is 1-O-beta-D-glucopyranosyl-rac-glycerol (79%) and 2-O-beta-D-glucopyranosyl-sn-glycerol (21%)
synthesis
expression of CleB gene in Escherichia coli gives approx 100000 U of enzyme activity/l of culture medium after 8 h of growth
synthesis
expression of enzyme using a baculovirus expression vector system in silkworm, Bombyx mori and purification to about 81% homogeneity in a single heat-treatment step. The expressed beta-glucosidase accounts for more than 10% of silkworm total haemolymph proteins. The expression level reaches 10199.5 U per ml hemolymph and 19797.4 U per silkworm larva, and the specific activity of the one-step purified crude enzyme is 885 U per mg
synthesis
hydrolysis of lactose in UHT skim milk at 70°C using CelB covalently attached onto Eupergit C in yields of 80%, and in a packed-bed immobilized enzyme reactor. The packed-bed reactor is about 10fold more stable and gives about the same productivity at 80% substrate conversion as the hollow-fiber reactor at 60% substrate conversion. The marked difference in the stability of free and immobilized CelB seems to reflect mainly binding of the soluble enzyme to the membrane surface of the hollow-fiber module. Microbial contamination of the reactors did not occur during reaction times of up to 39 d
synthesis
improvement of the stability of recombinant CelB by entrapment into Escherichia coli cells under conditions promoting strong inactivation. Glutardialdehyde-mediated protein cross-linking or rigidification of the cell membrane by adding magnesium ions is required to prevent release of CelB from within the cell into the bulk solution. In the presence of 1M glucose or when applying recirculation rates of 2.6per min, the entrapped enzyme is around 2fold more stable at 80°C than free CelB. The significance of the stabilisation is attenuated by the decrease in CelB initial activity which wis due to cross-linking and glutardialdehyde concentration-dependent
synthesis
use of CelB for oligosaccharide production from lactose in a kinetically controlled reaction. At reaction temperatures of 80°C and higher, the inactivation rate of the enzyme in the presence of sugars is increased by a factor of 2, caused by the occurrence of Maillard reactions between the sugar and the enzyme
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Comparative structural analysis and substrate specificity engineering of the hyperthermostable beta-glucosidase CelB from Pyrococcus furiosus
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39
4963-4970
2000
Pyrococcus furiosus (Q51723)
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Substrate specificity engineering of beta-mannosidase and beta-glucosidase from Pyrococcus by exchange of unique active site residues
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Pyrococcus furiosus (Q51723)
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4
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60
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28
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20
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20
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Pyrococcus furiosus (Q51723)
-
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29
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Pyrococcus furiosus (Q51723)
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Hydrolysis of flavanone glycosides by beta-glucosidase from Pyrococcus furiosus and its application to the production of flavanone aglycones from citrus extracts.
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61
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Pyrococcus furiosus (Q51723)
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Monomer structure of a hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form
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70
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Pyrococcus furiosus (Q51723)
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Structure of hyperthermophilic beta-glucosidase from Pyrococcus furiosus
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67
1473-1479
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Pyrococcus furiosus (Q51723)
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Splechtna, B.; Petzelbauer, I.; Kuhn, B.; Kulbe, K.D.; Nidetzky, B.
Hydrolysis of lactose by beta-glycosidase CelB from hyperthermophilic archaeon Pyrococcus furiosus: comparison of hollow-fiber membrane and packed-bed immobilized enzyme reactors for continuous processing of ultrahigh temperature-treated skim milk
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98-100
473-88
2002
Pyrococcus furiosus (Q51723)
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89
1019-1028
2011
Pyrococcus furiosus (Q51723)
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Lebbink, J.H.; Kaper, T.; Bron, P.; van der Oost, J.; de Vos, W.M.
Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution
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39
3656-3665
2000
Pyrococcus furiosus (Q51723)
brenda
Perugino, G.; Trincone, A.; Giordano, A.; van der Oost, J.; Kaper, T.; Rossi, M.; Moracci, M.
Activity of hyperthermophilic glycosynthases is significantly enhanced at acidic pH
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42
8484-8493
2003
Pyrococcus furiosus (Q51723)
brenda
Schwarz, A.; Thomsen, M.S.; Nidetzky, B.
Enzymatic synthesis of beta-glucosylglycerol using a continuous-flow microreactor containing thermostable beta-glycoside hydrolase CelB immobilized on coated microchannel walls
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103
865-872
2009
Pyrococcus furiosus (Q51723)
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Maillard reactions and increased enzyme inactivation during oligosaccharide synthesis by a hyperthermophilic glycosidase
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81
546-552
2003
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
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Encapsulation of hyperthermophilic beta-glucosidase from Pyrococcus furiosus into silica microcapsules
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43
1272-1274
2014
Pyrococcus furiosus (Q51723)
-
brenda
Powers, S.L.; Robinson, C.R.; Robinson, A.S.
Denaturation of an extremely stable hyperthermophilic protein occurs via a dimeric intermediate
Extremophiles
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2007
Pyrococcus furiosus (Q51723)
brenda
Voorhorst, W.G.B.; Gueguen, Y.; Geerling, A.C.M.; Schut, G.; Dahlke, I.; Thomm, M.; van der Oost, J.; de Vos, W.M.
Transcriptional regulation in the hyperthermophilic archaeon Pyrococcus furiosus: coordinated expression of divergently oriented genes in response to beta-linked glucose polymers
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Pyrococcus furiosus (Q51723)
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Kamrat, T.; Nidetzky, B.
Entrapment in E. coli improves the operational stability of recombinant beta-glycosidase CelB from Pyrococcus furiosus and facilitates biocatalyst recovery
J. Biotechnol.
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2007
Pyrococcus furiosus (Q51723)
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Mayer, J.; Kranz, B.; Fischer, L.
Continuous production of lactulose by immobilized thermostable beta-glycosidase from Pyrococcus furiosus
J. Biotechnol.
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Pyrococcus furiosus (Q51723)
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Bruins, M.E.; Janssen, A.E.M.; Boom, R.M.
Equilibrium shifts in enzyme reactions at high pressure
J. Mol. Catal. B
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Pyrococcus furiosus (Q51723)
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brenda
Zeuner, B.; Nyffenegger, C.; Mikkelsen, J.D.; Meyer, A.S.
Thermostable beta-galactosidases for the synthesis of human milk oligosaccharides
N. Biotechnol.
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2016
Pyrococcus furiosus (Q51723)
brenda
Lin, X.A.; Zhang, W.; Chen, Y.; Yao, B.; Zhang, Z.F.
Overexpression of celB gene coding for beta-glucosidase from Pyrococcus furiosus using a baculovirus expression vector system in silkworm, Bombyx mori
Z. Naturforsch. C
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2006
Pyrococcus furiosus (Q51723)
brenda
Choi, J.H.; Shin, K.C.; Oh, D.K.
An L213A variant of beta-glycosidase from Sulfolobus solfataricus with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to compound K
PLoS ONE
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2018
Pyrococcus furiosus
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