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Information on EC 3.2.1.23 - beta-galactosidase and Organism(s) Aspergillus niger and UniProt Accession P29853

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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.
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This record set is specific for:
Aspergillus niger
UNIPROT: P29853
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The taxonomic range for the selected organisms is: Aspergillus niger
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
lactase phlorizin hydrolase
-
Acid beta-galactosidase
-
-
-
-
beta-D-galactoside galactohydrolase
-
-
-
-
beta-D-glactanase
-
-
-
-
beta-D-lactosidase
-
-
-
-
beta-galactosidase
-
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
-
-
-
-
Oryzatym
-
-
-
-
p-nitrophenyl beta-galactosidase
-
-
-
-
S 2107
-
-
-
-
SR12 protein
-
-
-
-
Sumiklat
-
-
-
-
Trilactase
-
-
-
-
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-galactopyranose
show the reaction diagram
6% activity compared to 4-nitrophenyl alpha-D-galactopyranoside
-
-
?
4-nitrophenyl alpha-D-galactopyranoside + H2O
4-nitrophenol + alpha-D-galactopyranose
show the reaction diagram
100% activity
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
show the reaction diagram
42% activity compared to 4-nitrophenyl alpha-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
show the reaction diagram
3% activity compared to 4-nitrophenyl alpha-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
show the reaction diagram
81% activity compared to 4-nitrophenyl alpha-D-galactopyranoside
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside + H2O
5-bromo-4-chloroindol + beta-D-galactose
show the reaction diagram
-
-
-
?
lactose + H2O
D-galactose + D-glucose
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-beta-D-galactoside + H2O
o-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-galactoside + H2O
p-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
pectic galactan + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activation of the recombinant hybrid enzyme
Mn2+
-
activates the recombinant hybrid enzyme
Ni2+
-
activates the recombinant hybrid enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zn2+
-
slightly inhibits the recombinant hybrid enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.21 - 3.76
2-nitrophenyl beta-D-galactopyranoside
0.8
2-nitrophenyl-beta-D-galactopyranoside
-
pH 6.5, 40°C, recombinant hybrid enzyme
8.7 - 125
lactose
1.17 - 2.38
o-nitrophenyl-beta-D-galactoside
additional information
additional information
-
kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76 - 6.46
D-galactose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3
crude enzyme, in 200 mM potassium phosphate buffer, pH 6.8, for 15 min at 37°C
69.3
after 53.3fold purification, in 200 mM potassium phosphate buffer, pH 6.8, for 15 min at 37°C
23.1
-
enzyme form 1
77.5
-
enzyme form 2
82.4
-
enzyme form 3
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
enzyme form 1, 2 and 3, hydrolysis of lactose
3 - 3.5
-
immobilized enzyme
3.2
-
enzyme form 3, hydrolysis of o-nitrophenyl-beta-D-galactoside
3.5 - 4
-
soluble enzyme
4 - 4.5
4.5
mutant S259F/P261T/L262S/G263S
6.5
-
recombinant mutant hybrid enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
recombinant mutant hybrid enzyme
55 - 60
-
soluble enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
glycosylated enzyme, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM 22593
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
kinetics of growth and secretion
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BGAL_ASPNG
1006
0
109161
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
123000
glycosylated enzyme, gel filtration
129000
1 * 129000, glycosylated enzyme, SDS-PAGE
124000
-
enzyme form 1, gel filtration
150000
-
enzyme form 2, gel filtration
173000
-
enzyme form 3, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 129000, glycosylated enzyme, SDS-PAGE
additional information
-
tertiary structure of the recombinant hybrid enzyme, protein structure homology-modelling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S259F/P261T/L262S/G263S
mutant shows slightly reduced affinity for substrate (Km: 3.76 mM), 8.5fold reduction in inhibition by galactose, maximal activity lower than wild-type, pH stability lower than wild-type
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, Kluyveromyces lactis 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
4 - 8
a sharp drop of activity occurs above pH 4.0, about 35% residual activity at pH 4.5-5.5, about 10% residual activity at pH 6.5, no activity is detected at pH 8.0 and above
701882
2.5 - 8
-
stable
171190
3 - 5
-
30°C, 20 h, stable
171339
3 - 8
-
stable
171280
4.4 - 8
-
30 min, pH 4.4: soluble and immobilized enzymes, stable, pH 8.0: immobilized enzymes are stable, soluble enzyme loses 29% of its activity
171279
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 80
a sharp drop of activity occurs above 60°C, no activity is detected at 80°C
25
-
30 min, soluble and immobilized enzymes, stable
30
-
30 min, recombinant hybrid enzyme, stable
40
-
15 min, recombinant hybrid enzyme, stable
50
-
15 min, recombinant hybrid enzyme, loss of 40% activity
additional information
-
thermostability of soluble and immobilized enzymes at enzyme concentration 0.1-15 mg/ml
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the purified enzyme retains 68% residual activity after in vitro exposure to simulated gastric conditions (pepsin at pH 2.0) for 2 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, immobilized enzymes, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, Sephacryl S200 gel filtration, phenyl-agarose column chromatography, and PBE 94 chromatofocusing column chromatography
3 enzyme forms
-
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris as a His-tagged fusion protein
expression of wild-type and recombinant hybrid mutant enzymes in Escherichia coli strain DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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.; Malhotra, O.M.
beta-Galactosidase
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
4
409-430
1960
Klebsiella aerogenes, Aspergillus flavus, Aspergillus niger, Aspergillus oryzae, Bos taurus, Canis lupus familiaris, Capra hircus, Coffea sp., Oryctolagus cuniculus, Escherichia coli, Felis catus, Helix pomatia, Ovis aries, Homo sapiens, Medicago sativa, Malus sp., Neurospora sp., Prunus dulcis, Prunus armeniaca, Prunus persica, Saccharomyces fragilis, Shigella sonnei, Escherichia coli K 12, Escherichia coli ML 308, Escherichia coli ML 309
-
Manually annotated by BRENDA team
Sarto, V.; Marzetti, A.; Focher, B.
beta-D-Galactosidases immobilized on soluble matrices: kinetic and stability
Enzyme Microb. Technol.
7
515-520
1985
Aspergillus niger, Aspergillus oryzae, Saccharomyces fragilis
-
Manually annotated by BRENDA team
Baret, J.L.
Large-scale production and application of immobilized lactase
Methods Enzymol.
136
411-423
1987
Aspergillus niger, Aspergillus oryzae
-
Manually annotated by BRENDA team
Widmer, F.; Leuba, J.L.
beta-Galactosidase from Aspergillus niger. Separation and characterization of three multiple forms
Eur. J. Biochem.
100
559-567
1979
Aspergillus niger
Manually annotated by BRENDA team
Watanabe, Y.; Kibesaki, Y.; Takenishi, S.; Sakai, K.; Tsujisaka, Y.
Purification and properties of beta-galactosidase from Penicillium citrinum
Agric. Biol. Chem.
43
943-950
1979
Aspergillus awamori, Aspergillus cellulosae, Aspergillus niger, Aspergillus oryzae, Fusarium oxysporum, Geotrichum candidum, Mucor javanicus, Mucor mucedo, Neurospora crassa, Penicillium chrysogenum, Penicillium citrinum, Penicillium cyclopium, Penicillium glabrum, Penicillium glaucum, Ascospirella lutea, Penicillium roqueforti, Penicillium toxidarium, Rhizopus acidus, Rhizopus arrhizus, Rhizopus microsporus var. chinensis, Rhizopus formosciensis, Rhizopus stolonifer, Rhizopus niveus, Trichoderma viride
-
Manually annotated by BRENDA team
Manzanares, P.; de Graaff, L.H.; Visser, J.
Characterization of galactosidases from Aspergillus niger: purification of a novel alpha-galactosidase activity
Enzyme Microb. Technol.
22
383-390
1998
Aspergillus niger
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
O'Connell, S.; Walsh, G.
A novel acid-stable, acid-active beta-galactosidase potentially suited to the alleviation of lactose intolerance
Appl. Microbiol. Biotechnol.
86
517-524
2010
Aspergillus niger (P29853), Aspergillus niger
Manually annotated by BRENDA team
Hu, X.; Robin, S.; OConnell, S.; Walsh, G.; Wall, J.G.
Engineering of a fungal beta-galactosidase to remove product inhibition by galactose
Appl. Microbiol. Biotechnol.
87
1773-1782
2010
Aspergillus niger (B6HYI9), Aspergillus niger
Manually annotated by BRENDA team