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Information on EC 3.2.1.23 - beta-galactosidase and Organism(s) Kluyveromyces lactis and UniProt Accession P00723

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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.
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This record set is specific for:
Kluyveromyces lactis
UNIPROT: P00723
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The taxonomic range for the selected organisms is: Kluyveromyces lactis
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid beta-galactosidase
-
-
-
-
beta-D-galactoside galactohydrolase
beta-D-glactanase
-
-
-
-
beta-D-lactosidase
-
-
-
-
beta-galase
-
-
-
-
beta-lactosidase
-
-
-
-
driselase
-
-
-
-
Exo-(1-->4)-beta-D-galactanase
-
-
-
-
exo-beta-(1->3)-D-galactanase
-
-
-
-
galactosidase, beta
-
-
-
-
Hydrolact
-
-
-
-
lactase
lactosylceramidase II
-
-
-
-
Lactozym
-
-
-
-
Maxilact
-
-
-
-
Maxilact-L/2000
-
-
Oryzatym
-
-
-
-
p-nitrophenyl beta-galactosidase
-
-
-
-
S 2107
-
-
-
-
SR12 protein
-
-
-
-
Sumiklat
-
-
-
-
Trilactase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
show the reaction diagram
the conserved residues E482, M522, Y523 and E551 are important in catalysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-11-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
lactose + H2O
beta-D-glucose + beta-D-galactose
show the reaction diagram
lactose + H2O
D-galactose + D-glucose
show the reaction diagram
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
lactose + hydroquinone
hydroquinone galactoside + D-glucose
show the reaction diagram
-
transgalactosylation
60.27% yield
-
?
o-nitrophenyl beta-D-galactopyranoside + H2O
o-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-beta-D-galactoside + H2O
o-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
structure-activity relationship as a function of the pH, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lactose + H2O
beta-D-glucose + beta-D-galactose
show the reaction diagram
-
the enzyme is involved in the lactose metabolism of the organism, overview
-
-
?
lactose + H2O
D-galactose + D-glucose
show the reaction diagram
-
-
-
?
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
1 mM, 8.1fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside, 4.7fold stimulation of activity with lactose
Fe2+
-
1 mM, 4.5fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside, 4.1fold stimulation of activity with lactose
Ni2+
-
activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme
Zn2+
-
slightly activates the wild-type Kluyveromyces lactis enzyme, but slightly inhibits the recombinant hybrid enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-dinitrophenyl 2-deoxy-2-fluoro-beta-D-galactopyranoside
-
-
Ba2+
-
1 mM, 56% inhibition of activity with o-nitrophenyl beta-D-galactopyranoside
Cu2+
-
1 mM, 97% inhibition of activity with o-nitrophenyl beta-D-galactopyranoside, 88% inhibition of activity with lactose
D-galactose
-
competitive inhibition
D-glucose
-
noncompetitive inhibition
galactose
-
acts as an inhibitor at low concentrations of galactose and lactose, but does not inhibit the activity of beta-galactosidase at high concentrations of galactose (above 50 mM) and lactose (above 100 mM)
imidazole
Mn2+
-
activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme
Ni2+
-
activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme
Zn2+
-
slightly activates the wild-type Kluyveromyces lactis enzyme, but slightly inhibits the recombinant hybrid enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-Lactoglobulin
-
beta-lactoglobulin interacts with beta-galactosidase and increases the catalytic activity due to interaction of both proteins probably through the lysine epsilon-amino groups of beta-lactoglobulin
-
additional information
-
lactose slightly induces the enzyme in vivo
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 1.5
2-nitrophenyl-beta-D-galactopyranoside
8.7 - 21
lactose
1.5
o-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 37°C
0.1 - 12.5
o-nitrophenyl-beta-D-galactoside
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 888
o-nitrophenyl-beta-D-galactoside
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45 - 90
D-galactose
758
D-glucose
-
at 25°C and pH 6.5, using 2-nitrophenyl-beta-D-galactopyranoside as substrate
additional information
additional information
-
detailed inhibition kinetics, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1709
-
purified commercial preparation
additional information
-
in vivo activity of cultures from cheese whey
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
recombinant mutant hybrid enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
wild-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
119000
-
gel filtration
19000
-
isoenzyme betaG19, gel filtration
41000
-
isoenzyme betaG41, gel filtration
550000
-
isoenzyme betaG550, gel filtration
630000
-
isoenzyme betaG630, gel filtration
additional information
-
according to its CD spectrum, beta-galactosidase is mainly a beta-type protein. The antiparallel beta-sheet appears as the amino type of regular conformation (25%)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 23-27% (w/v) polyethylene glycol 350, 0.1 M bis-Tris pH 7.5, 0.2 M sodium tartrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of a hybrid mutant enzyme exchanging domains from Kluyveromyces lactis and Aspergillus niger enzymes, addition of a secretory signal in the N-terminus of the recombinant protein, enzyme optimization for industrial productions by fusion with extracellular and more stable enzyme from Aspergillus niger, overview, kinetics of growth and secretion
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
stable
171190
additional information
-
proposal of two kinetic models to explain the behaviour of the enzymatic activity versus pH, implying the dissociation of one or two protons of the enzyme
664772
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
30 min, recombinant hybrid enzyme, stable, the wild-type enzyme loses 45% activity within 60 min
40
-
15 min, recombinant hybrid enzyme, stable, the wild-type enzyme loses 10% activity within 10 min
50
-
15 min, recombinant hybrid enzyme, loss of 40% activity, the wild-type enzyme loses 60% activity
additional information
-
thermal deactivation is fit to a kinetic model
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dissociation and partial unfolding of the dimeric enzyme under high hydrostatic pressure, more resistant in presence of polyols
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4 isoenzymes: betaG630, betaG550, betaG41 and betaG19
-
anti-FLAG M2 affinity gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae BJ3505 cells
expression in Escherichia coli as a soluble His-tagged recombinant enzyme
-
expression of wild-type and recombinant hybrid mutant enzymes in Escherichia coli strain DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
-
evaluation of different commercial soluble beta-galactosidases for removal of the residual lactose in crude galactooligosaccharides. Best enzyme tested is lactase NL, with a hydrolytic activity of 286 IU/mg and a half-life of 9 h at 35°C in the presence of 1 mM Mn2+. The best reaction conditions are 35°C, 50% initial carbohydrate concentration and 135 IU/g, leading to 70% reduction of lactose in raw galactooligosaccharides, with an increase of 48% in monosaccharides and of 30% in galactooligosaccharides
industry
-
the beta-galactosidase from Kluyveromyces lactis is a protein of outstanding biotechnological interest in the food industry and milk whey reutilization, optimization of extraction and downstream processing of the intracellular enzyme for reduction of costs in industrial production by genetic modification, overview
nutrition
-
lactase entrapped in cellulose-triacetate fibers is originally used to produce low lactose milk
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crueger, A.; Crueger, W.
Carbohydrates
Biotechnology (Kieslich, K. , ed. ) Verlag Chemie, Weinheim
6A
421-457
1984
Aspergillus niger, Aspergillus oryzae, Geobacillus stearothermophilus, Niallia circulans, Weizmannia coagulans, Saccharomyces cerevisiae, Caldariella acidophila, Kluyveromyces marxianus, Thermothelomyces heterothallicus, Curvularia inaequalis, Escherichia coli, Fusarium verticillioides, Trichocladium griseum, Thermomyces lanuginosus, Kluyveromyces lactis, Kluyveromyces sp., Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus sp. 'thermophilus', Leuconostoc citrovorum, Umbelopsis vinacea, Rhizomucor miehei, Rhizomucor pusillus, Penicillium multicolor, Sinorhizobium meliloti, Saccharomyces anamensis, Mycothermus thermophilus, Sporotrichum sp., Streptomyces coelicolor, Zygosaccharomyces lactis, Geobacillus stearothermophilus HRI
-
Manually annotated by BRENDA team
Wallenfels, K.; Weil, R.
beta-Galactosidase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
617-663
1972
Enterobacter cloacae, Aeromonas caviae, Priestia megaterium, Bacillus subtilis, Bos taurus, Streptococcus pneumoniae, Escherichia coli, Helix pomatia, Ovis aries, Homo sapiens, Kluyveromyces lactis, Lactococcus lactis, Paracolobactrum aerogenoides, Rattus norvegicus, Saccharomyces fragilis, Shigella dysenteriae, Hamamotoa singularis, Tritrichomonas suis, Escherichia coli ML 309, Escherichia coli ML 35
-
Manually annotated by BRENDA team
Athes, V.; Lange, R.; Combes, D.
Influence of polyols on the structural properties of Kluyveromyces lactis beta-galactosidase under high hydrostatic pressure
Eur. J. Biochem.
255
206-211
1998
Kluyveromyces lactis
Manually annotated by BRENDA team
Mbuyi-Kalala, A.; Schnek, A.G.; Leonis, J.
Separation and characterization of four enzyme forms of beta-galactosidase from Saccharomyces lactis
Eur. J. Biochem.
178
437-443
1988
Kluyveromyces lactis
Manually annotated by BRENDA team
Kim, C.S.; Ji, E.S.; Oh, D.K.
Expression and characterization of Kluyveromyces lactis beta-galactosidase in Escherichia coli
Biotechnol. Lett.
25
1769-1774
2003
Kluyveromyces lactis
Manually annotated by BRENDA team
Kim, C.S.; Ji, E.S.; Oh, D.K.
A new kinetic model of recombinant beta-galactosidase from Kluyveromyces lactis for both hydrolysis and transgalactosylation reactions
Biochem. Biophys. Res. Commun.
316
738-743
2004
Kluyveromyces lactis
Manually annotated by BRENDA team
Jurado, E.; Camacho, F.; Luzon, G.; Vicaria, J.M.
Kinetic models of activity for b-galactosidases: influence of pH, ionic concentration and temperature
Enzyme Microb. Technol.
34
33-40
2004
Kluyveromyces marxianus, Kluyveromyces lactis
-
Manually annotated by BRENDA team
Tello-Solis, S.R.; Jimenez-Guzman, J.; Sarabia-Leos, C.; Gomez-Ruiz, L.; Cruz-Guerrero, A.E.; Rodriguez-Serrano, G.M.; Garcia-Garibay, M.
Determination of the secondary structure of Kluyveromyces lactis beta-galactosidase by circular dichroism and its structure-activity relationship as a function of the pH
J. Agric. Food Chem.
53
10200-10204
2005
Kluyveromyces lactis
Manually annotated by BRENDA team
Walsh, R.; Martin, E.; Darvesh, S.
A versatile equation to describe reversible enzyme inhibition and activation kinetics: modeling beta-galactosidase and butyrylcholinesterase
Biochim. Biophys. Acta
1770
733-746
2007
Kluyveromyces lactis
Manually annotated by BRENDA team
Ornelas, A.P.; Silveira, W.B.; Sampaio, F.C.; Passos, F.M.
The activity of beta-galactosidase and lactose metabolism in Kluyveromyces lactis cultured in cheese whey as a function of growth rate
J. Appl. Microbiol.
104
1008-1013
2007
Kluyveromyces lactis
Manually annotated by BRENDA team
Rodriguez, A.P.; Leiro, R.F.; Trillo, M.C.; Cerdan, M.E.; Siso, M.I.; Becerra, M.
Secretion and properties of a hybrid Kluyveromyces lactis-Aspergillus niger beta-galactosidase
Microb. Cell Fact.
5
41
2006
Aspergillus niger, Kluyveromyces lactis, Kluyveromyces lactis MW 190-9B
Manually annotated by BRENDA team
Del Moral-Ramirez, E.; Dominguez-Ramirez, L.; Cruz-Guerrero, A.E.; Rodriguez-Serrano, G.M.; Garcia-Garibay, M.; Gomez-Ruiz, L.; Jimenez-Guzman, J.
Role of lysine epsilon-amino groups of beta-lactoglobulin on its activating effect of Kluyveromyces lactis beta-galactosidase
J. Agric. Food Chem.
56
5859-5863
2008
Kluyveromyces lactis
Manually annotated by BRENDA team
Pereira-Rodriguez, A.; Fernandez-Leiro, R.; Gonzalez Siso, M.I.; Cerdan, M.E.; Becerra, M.; Sanz-Aparicio, J.
Crystallization and preliminary X-ray crystallographic analysis of beta-galactosidase from Kluyveromyces lactis
Acta Crystallogr. Sect. F
66
297-300
2010
Kluyveromyces lactis (P00723), Kluyveromyces lactis
Manually annotated by BRENDA team
Park, A.R.; Oh, D.K.
Galacto-oligosaccharide production using microbial beta-galactosidase: current state and perspectives
Appl. Microbiol. Biotechnol.
85
1279-1286
2010
Alicyclobacillus acidocaldarius, Aspergillus aculeatus, Aspergillus oryzae, Geobacillus stearothermophilus, Niallia circulans, Priestia megaterium, Bifidobacterium adolescentis, Bifidobacterium bifidum, Bifidobacterium longum subsp. infantis, Caldicellulosiruptor saccharolyticus, Kluyveromyces marxianus, Papiliotrema laurentii, Streptococcus pneumoniae, Pantoea agglomerans, Kluyveromyces lactis, Lactobacillus acidophilus, Limosilactobacillus reuteri, Saccharopolyspora rectivirgula, Hamamotoa singularis, Sterigmatomyces elviae, Saccharolobus solfataricus, Thermotoga maritima, Thermus aquaticus, Thermus sp., Arthrobacter psychrolactophilus
Manually annotated by BRENDA team
Kim, G.E.; Lee, J.H.; Jung, S.H.; Seo, E.S.; Jin, S.D.; Kim, G.J.; Cha, J.; Kim, E.J.; Park, K.D.; Kim, D.
Enzymatic synthesis and characterization of hydroquinone galactoside using Kluyveromyces lactis lactase
J. Agric. Food Chem.
58
9492-9497
2010
Aspergillus oryzae, Niallia circulans, Kluyveromyces lactis, Thermus sp.
Manually annotated by BRENDA team
Jochems, P.; Mueller, T.; Satyawali, Y.; Diels, L.; Dejonghe, W.; Hanefeld, U.
Active site titration of immobilized beta-galactosidase for the determination of active enzymes
Biochem. Eng. J.
93
137-141
2014
Kluyveromyces lactis
-
Manually annotated by BRENDA team
Santibanez, L.; Fernandez-Arrojo, L.; Guerrero, C.; Plou, F.; Illanes, A.
Removal of lactose in crude galacto-oligosaccharides by beta-galactosidase from Kluyveromyces lactis
J. Mol. Catal. B
133
85-91
2016
Kluyveromyces lactis
-
Manually annotated by BRENDA team