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0.012
recombinant isozyme BGal1 in Escherichia coli, substrate 4-nitrophenyl-beta-D-galactopyranoside
0.025
-
crude homogenate, at pH 4.8, 60°C
0.04
recombinant isozyme BGal2 in Escherichia coli, substrate 2-nitrophenyl-beta-D-galactopyranoside
0.058
recombinant isozyme BGal1 in Escherichia coli, substrate 2-nitrophenyl-beta-D-galactopyranoside
0.083
recombinant isozyme BGal2 in Escherichia coli, substrate 4-nitrophenyl-beta-D-galactopyranoside
0.085
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crude extract, at 37°C
0.19
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wild type enzyme, using 20 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
0.22
-
mutant enzyme R109K, using 2.65 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
0.27
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after 11.1fold purification, at pH 4.8, 60°C
0.3346
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40% of nitrogen source for yeast is supplemented as urea
0.35
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cell extract, in 50 mM potassium phosphate buffer, pH 7.3, containing 100 mM NaCl and 100 mM beta-mercaptoethanol
0.47
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mutant enzyme R109K, using 20 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
0.5
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wild type enzyme, using 2.65 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
0.6
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mutant enzyme R109W, using 2.65 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
0.6597
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nitrogen source for yeast is ammonium sulfate
0.72
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partially purified enzyme, 37°C
0.9
Kerstingiella geocarpa
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0.96
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wild-type, pH 6.5, 40°C
1.148
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37°C, 3 min, pH 6.6, 20% of nitrogen source for yeast is supplemented as urea
1.3
crude enzyme, in 200 mM potassium phosphate buffer, pH 6.8, for 15 min at 37°C
1.52
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mutant enzyme R109V, using 2.65 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
1.79
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mutant enzyme R109W, using 20 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
1093
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His-tagged enzyme from crude extract, at 30°C in 0.1 M sodium phosphate, pH 7.0, 10 mM KCl, 1 mM MgSO4, 5 mM mercaptoethanol
11.6
Caldariella acidophila
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121
substrate: beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C
1410
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substrate lactose, pH 3.5, 40°C
152.3
pH 7.5, 80°C, activity of recombinant mutant enzyme F441Y, substrate: 2-nitrophenyl beta-D-galactopyranoside
16
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partially purified enzyme, 75°C
17.7
substrate: lactose, pH 4.5, 60°C
1709
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purified commercial preparation
191.6
-
purified enzyme from mutant strain H26-10-7
2.6
-
after 7fold purification, in 50 mM potassium phosphate buffer, pH 7.3, containing 100 mM NaCl and 100 mM beta-mercaptoethanol
2.62
-
mutant FMNP01Gal-2, pH 6.5, 40°C
2.68
substrate: 4-nitrophenyl alpha-D-glucopyranoside, pH 6.0, 60°C
20.33
-
purified isozyme BGT II
20.4
purified recombinant His-tagged enzyme
21.7
-
crude extract, at pH 6.0 and 80°C
212
-
after 9.8fold purification, at pH 6.0 and 80°C
243
-
38°C, pH 7, substrate: 2-nitrophenyl-beta-D-galactopyranoside
2444
-
mature enzyme after 2.7fold purification, at 30°C in 0.1 M sodium phosphate, pH 7.0, 10 mM KCl, 1 mM MgSO4, 5 mM mercaptoethanol
25.4
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38°C, pH 7, substrate: lactose
25.7
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 6.0, 60°C
25.76
-
beta-galactosidase V
27.2
substrate: 4-nitrophenyl beta-D-fucopyranoside, pH 6.0, 60°C
2969
-
His-tagged enzyme after 2.7fold purification, at 30°C in 0.1 M sodium phosphate, pH 7.0, 10 mM KCl, 1 mM MgSO4, 5 mM mercaptoethanol
299
substrate: 4-nitrophenyl beta-D-galactopyranoside, pH 4.5, 60°C
3 - 3.9
substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C
31.25
-
purified isozyme BGT I
33.25
-
beta-D-galactoside galactohydrolase pH 4.2
35.8
substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C
36.2
substrate: 4-nitrophenyl beta-D-galactopyranoside, pH 6.0, 60°C
39.79
-
beta-galactosidase I
4.15
substrate: 4-nitrophenyl beta-D-xylopyranoside, pH 6.0, 60°C
4.9
-
mutant enzyme R109V, using 20 mM 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 37°C
40.2
-
purified enzyme from wild-type strain H26
42
substrate: 2-nitrophenyl-beta D-galactoside, pH 7.2, 22°C, the enzyme also shows beta-fucosidase activity
464
-
purified enzyme, substrate: 2-nitrophenyl beta-D-galactopyranoside, pH 6.5, 25-40°C
592
purified native enzyme
69.3
after 53.3fold purification, in 200 mM potassium phosphate buffer, pH 6.8, for 15 min at 37°C
71
substrate: beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C
77.33
-
after 910fold purification, at 37°C
898
-
mature enzyme from crude extract, at 30°C in 0.1 M sodium phosphate, pH 7.0, 10 mM KCl, 1 mM MgSO4, 5 mM mercaptoethanol
90
Saccharomyces fragilis
-
-
95.49
-
beta-galactosidase II
95.69
-
beta-galactosidase III
97
-
pH 6.5, 30°C, substrate: 2-nitrophenyl beta-D-galactopyranoside
10.2
-
-
110.8
pH 6.0, 25°C
110.8
25°C, pH 6.5, substrate: 2-nitrophenyl beta-D-galactopyranoside
125.2
-
-
125.2
-
after 19.4-fold purification
168.6
-
purified enzyme
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substrate specificity of recombinant wild-type and mutant enzymes, overview
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activities of free and entrapped cross-linked enzyme, overview
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detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview
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assay methods
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a method that allows measurement of catalytic activity of a site in a preparation containing inactive protein wether homologous or foreign
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beta-galactosidase from strains 8677 and 35321 demonstrate that the relative activities of the enzyme for the different substrates differ between the strains, assay method optimizationusing different substrates, overview
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electrophoretic mobility and catalytic activity of individual molecules of enzyme are reproducible for each molecule but different for individual molecules. There is no relationship between the observed activities and electrophoretic motilities
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in vivo enzyme activity in different fibroblast lines, cells in different growth stages, overview
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in vivo activity of cultures from cheese whey
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detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview
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detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview
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30.3 mU/mg, hematopoetic stem cells
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8.75 mU/mg, neural presursor cells
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highest activity for hydrolysis of lactose is obtained with immobilization onto Duolite ES-762
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beta-galactosidase activity is barely detectable in supernatants of wild-type and oprB1-deficient strains, the supernatant of glucose-grown colR-deficient strain contains 4% of total beta-galactosidase activity of the cell suspension.
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Membrane permeability of colRoprB1 double mutant is similar to that of the wild-type regardless of the presence of phenol in the growth medium.
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The oprB1 single mutant also behaves like the wild type in membrane permeability test.
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The presence of phenol in the growth medium of colR mutant increases the proportion of extracellular beta-galactosidase activity up to 15%.
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To evaluate membrane permeability, measurement of the activity of an intracellular enzyme beta-galactosidase in nonpermeabilized cells is done. beta-galactosidase is assayed after the bacterial cell membrane is permeabilized with SDS and chloroform. beta-galactosidase activity of untreated cells is compared with that of permeabilized cells. As a source of beta-galactosidase, a plasmid pKTlacZS/C containing the tnpA promoter of the transposon Tn4652 upstream the lacZ gene is used. beta-galactosidase activity in permeabilized glucose-grown cells of all studied genetic backgrounds is about 80 Miller units.
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Up to 15% of total beta-galactosidase activity is detectable in colR-deficient cells grown on glucose minimal plates, and about 35% when cells are grown on glucose medium supplemented with 1 mM phenol. The membrane of colR-deficient strain is more permeable and the presence of phenol further increases the leakiness of the membrane of colR mutant.
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When cells are assayed without the prior chloroform and SDS treatment, differences between the strains become evident. Only 4% of total beta-galactosidase activity is measurable in nonpermeabilized wild-type cells regardless of the presence of phenol in the growth medium.
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