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EC Tree
IUBMB Comments Some enzymes in this group hydrolyse alpha-L-arabinosides; some animal enzymes also hydrolyse beta-D-fucosides and beta-D-glucosides; cf. EC 3.2.1.108 lactase.
The taxonomic range for the selected organisms is: Lactobacillus delbrueckii The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-galactosidase, beta-gal, beta-d-galactosidase, senescence-associated beta-galactosidase, endo-beta-galactosidase, bglap, sa-beta-gal, acid beta-galactosidase, beta galactosidase, betagal,
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Acid beta-galactosidase
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-
-
-
beta-D-galactoside galactohydrolase
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-
-
-
beta-D-glactanase
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-
-
-
beta-D-lactosidase
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-
-
-
Exo-(1-->4)-beta-D-galactanase
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-
-
-
exo-beta-(1->3)-D-galactanase
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-
-
-
galactosidase, beta
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-
-
-
lactosylceramidase II
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-
-
-
p-nitrophenyl beta-galactosidase
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-
-
-
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hydrolysis of O-glycosyl bond
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-
-
-
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beta-D-galactoside galactohydrolase
Some enzymes in this group hydrolyse alpha-L-arabinosides; some animal enzymes also hydrolyse beta-D-fucosides and beta-D-glucosides; cf. EC 3.2.1.108 lactase.
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2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
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-
-
?
lactose + H2O
D-galactose + D-glucose
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-
-
?
lactose + H2O
D-glucose + D-galactose
o-nitrophenyl-beta-D-galactoside + H2O
o-nitrophenol + beta-D-galactose
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-
-
-
?
lactose + H2O
D-glucose + D-galactose
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-
-
-
?
lactose + H2O
D-glucose + D-galactose
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the enzyme is involved in lactose fermentation in the colon playing a central role in lactose intolerance in humans
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-
?
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lactose + H2O
D-galactose + D-glucose
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-
-
?
lactose + H2O
D-glucose + D-galactose
-
the enzyme is involved in lactose fermentation in the colon playing a central role in lactose intolerance in humans
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-
?
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Co2+
the enzyme requires 1 mM Co2+ for optimal activity and thermostability
Mg2+
the enzyme requires 1 mM Mn2+ for optimal activity and thermostability
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Cu2+
1 mM Cu2+ inhibits the activity more than 13fold
EDTA
35% residual activity at 10 mM
additional information
not significantly inhibited by Fe2+, Ca2+, Mg2+, Zn2+, Ba2+, and Ni2+
-
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0.16 - 0.17
2-nitrophenyl-beta-D-galactopyranoside
0.365 - 0.479
o-nitrophenyl-beta-D-galactoside
0.16
2-nitrophenyl-beta-D-galactopyranoside
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
0.17
2-nitrophenyl-beta-D-galactopyranoside
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
0.94
lactose
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
0.98
lactose
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
0.365
o-nitrophenyl-beta-D-galactoside
-
wild-type enzyme, at 11-45°C
0.371
o-nitrophenyl-beta-D-galactoside
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mutant enzyme L317F, 11-45°C
0.479
o-nitrophenyl-beta-D-galactoside
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mutant enzyme P429S, at 11-45°C
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47.2 - 49.2
2-nitrophenyl-beta-D-galactopyranoside
47.2
2-nitrophenyl-beta-D-galactopyranoside
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
49.2
2-nitrophenyl-beta-D-galactopyranoside
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
45.7
lactose
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
46.3
lactose
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
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289.4 - 295
2-nitrophenyl-beta-D-galactopyranoside
289.4
2-nitrophenyl-beta-D-galactopyranoside
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
295
2-nitrophenyl-beta-D-galactopyranoside
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
46.6
lactose
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
47
lactose
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
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additional information
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-
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strain ATCC 11842, subspecies Lactobacillus delbrueckii bulgaricus
UniProt
brenda
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110000
4 * 110000, SDS-PAGE
110000
-
2 * 110000, wild-type enzyme and mutant enzymes L317D and P429S, SDS-PAGE
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homotetramer
4 * 110000, SDS-PAGE
dimer
-
2 * 110000, wild-type enzyme and mutant enzymes L317D and P429S, SDS-PAGE
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E491A
the mutant shows wild type optimal temperature, but displays an optimal pH at 6.5-7.0
L317F
-
maximal velocity deviates from that of wild-type enzyme only at lower temperatures, in 2 mM Mg2+. This temperature-dependent effect can be suppressed by increasing the Mg2+ concentration
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5.5
the wild type protein retains about 90% of its activity after 32 h at pH 5.5. At pH 5.0 and 6.0 the enzyme conserves more than 50% of its initial activity after 32 h of incubation, at pH 4.5, 6.5, 7.0 and 7.5 the enzyme half-lives are 24, 28, 20 and 18 h respectively
706705
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40 - 65
the wild-type beta-galactosidase is fully stable at 40°C and 45°C for 16 h, respectively. At temperatures of 50, 55, 60 and 65°C wild type enzyme half-lives are 6, 3, 1.5 and 0.4 h respectively. Above 65°C occurs rapid inactivation with or without divalent ions
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ammonium sulfate precipitation and fast-performance liquid chromatography using an anion-exchange column equilibrated with 100 mM sodium acetate buffer (pH 5.5)
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expressed in Escherichia coli MRS32 cells
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food industry
the enzyme is used for hydrolysis of lactose extracted from whey or milk
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Adams, R.M.; Yoast, S.; Mainzer, S.E.; Moon, K.; Palombella, A.L.; Estell, D.A.; Power, S.D.; Schmidt, B.F.
Characterization of two cold-sensitive mutants of the beta-galactosidase from Lactobacillus delbruckii subsp. Bulgaricus
J. Biol. Chem.
8
5666-5672
1994
Lactobacillus delbrueckii
brenda
Honda, H.; Kataoka, F.; Nagaoka, S.; Kawai, Y.; Kitazawa, H.; Itoh, H.; Kimura, K.; Taketomo, N.; Yamazaki, Y.; Tateno, Y.; Saito, T.
beta-Galactosidase, phospho-beta-galactosidase and phospho-beta-glucosidase activities in Lactobacilli strains isolated from human faeces
Lett. Appl. Microbiol.
45
461-466
2007
Lactobacillus acidophilus, Lactiplantibacillus plantarum, Lacticaseibacillus casei, Limosilactobacillus fermentum, Lactobacillus crispatus, Lactobacillus delbrueckii, Lactobacillus delbrueckii subsp. lactis, Lactobacillus johnsonii, Limosilactobacillus reuteri, Ligilactobacillus salivarius, Lactobacillus amylovorus, Limosilactobacillus mucosae, no activity in Lactobacillus gasseri, Limosilactobacillus oris, Limosilactobacillus vaginalis, Limosilactobacillus vaginalis MEP181R91, Limosilactobacillus reuteri MEP181R88
brenda
Rhimi, M.; Aghajari, N.; Jaouadi, B.; Juy, M.; Boudebbouze, S.; Maguin, E.; Haser, R.; Bejar, S.
Exploring the acidotolerance of beta-galactosidase from Lactobacillus delbrueckii subsp. bulgaricus: an attractive enzyme for lactose bioconversion
Res. Microbiol.
160
775-784
2009
Lactobacillus delbrueckii (Q1G9Z4)
brenda