3.2.1.23: beta-galactosidase
This is an abbreviated version!
For detailed information about beta-galactosidase, go to the full flat file.
Word Map on EC 3.2.1.23
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3.2.1.23
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lacz
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adenovirus
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lysosomal
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lactose
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endothelial
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oligosaccharide
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artery
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phage
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adenovirus-mediated
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beta-glucosidase
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immunoassay
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retroviral
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beta-glucuronidase
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herpes
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lambda
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simplex
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luciferase
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cytomegalovirus
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neuraminidase
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viruses
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hydrolases
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bacteriophage
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glycosidases
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gm1
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liposome
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ganglioside
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p16ink4a
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alpha-galactosidase
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alpha-mannosidase
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osteogenic
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vaccinia
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adeno-associated
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replication-defective
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n-acetyl-beta-glucosaminidase
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runx2
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sialidase
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alpha-glucosidase
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sialic
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galactosylation
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plaque-forming
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osteoblast
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kluyveromyces
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telomerase
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analysis
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degradation
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diagnostics
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lysogens
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beta-hexosaminidase
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keratan
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vector-mediated
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biotechnology
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molecular biology
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synthesis
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environmental protection
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ganciclovir
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nutrition
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transglycosylation
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medicine
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industry
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nonviral
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food industry
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biofuel production
- 3.2.1.23
- lacz
- adenovirus
- lysosomal
- lactose
- endothelial
- oligosaccharide
- artery
- phage
-
adenovirus-mediated
- beta-glucosidase
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immunoassay
-
retroviral
- beta-glucuronidase
-
herpes
- lambda
- simplex
- luciferase
- cytomegalovirus
- neuraminidase
- viruses
- hydrolases
- bacteriophage
- glycosidases
- gm1
- liposome
- ganglioside
- p16ink4a
- alpha-galactosidase
- alpha-mannosidase
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osteogenic
- vaccinia
-
adeno-associated
-
replication-defective
- n-acetyl-beta-glucosaminidase
- runx2
- sialidase
- alpha-glucosidase
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sialic
-
galactosylation
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plaque-forming
-
osteoblast
- kluyveromyces
- telomerase
- analysis
- degradation
- diagnostics
-
lysogens
- beta-hexosaminidase
- keratan
-
vector-mediated
- biotechnology
- molecular biology
- synthesis
- environmental protection
- ganciclovir
- nutrition
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transglycosylation
- medicine
- industry
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nonviral
- food industry
- biofuel production
Reaction
Synonyms
Aabeta-gal, Acid beta-galactosidase, B-GAL, BbgI, BbgII, BbgIII, BbgIV, beta galactosidase, beta-D-galactohydrolase, beta-D-galactosidase, beta-D-galactoside galactohydrolase, beta-D-glactanase, beta-D-lactosidase, beta-gal, beta-Gal 1, beta-Gal 2, beta-Gal II, beta-galactosidase, beta-galactosidase I, beta-galactosidase II, beta-galactosidase III, beta-galactosidase IV, beta-galase, beta-lactosidase, betagal, betaGly4, betaGS, BGA, BgaB, BgaBM, bgaD, BgaH, BGAL, BGAL1, BGAL10, BGAL11, BGAL12, BGAL13, BGAL14, BGAL15, BGAL16, BGAL17, BGAL2, BGAL3, BGAL4, BGAL5, BGAL6, BGAL7, BGAL8, BGAL9, BgalA, BgAP, BgaS, BgaX, BGL1, BglAp, BGT I, BGT II, cold-active beta-galactosidase, CTP-beta-gal, driselase, EABase, endo-beta-galactosidase, Exo-(1-->4)-beta-D-galactanase, exo-beta-(1->3)-D-galactanase, Gal-2, Gal-5, GAL1, Gal2, Gal3, Gal4, GALA, galactanase, galactosidase, galactosidase, beta, GALB, gherkin lactase, H-BgaS, hcbetagal, Hlac_2868, Hydrolact, LacA, LACS, lactase, lactase phlorizin hydrolase, lactosylceramidase II, Lactozym, Lactozym 3000L, LPH, Maxilact, Maxilact-L/2000, MeBglD2, More, ONPGase, Oryzatym, p-nitrophenyl beta-galactosidase, PF1208, PRGH1, S 2107, SA-beta-GAL, SA-betagal, senescence-associated beta-galactosidase, SPD_0065 protein, SR12 protein, Ss beta-gal, SSO3019, SSU0587, Sumiklat, Trilactase, XC1214, XG-specific beta-galactosidase, YesZ, YH4502, ZD410
ECTree
3.2.1.23 beta-galactosidaseAdvanced search results
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results (Application
Application on EC 3.2.1.23 - beta-galactosidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biofuel production
the saccharification yield of rice straw using Trichoderma reesei cellulase is improved by the addition of MeBglD2. These results show that MeBglD2 can be used to improve plant biomass saccharification, because both substrates and products can activate its enzymatic activity
biotechnology
degradation
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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
diagnostics
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the enzyme is a reliable marker for the course of replicative cell senescence
environmental protection
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the presence of coliforms in polluted water is determined enzymatically in situ by directly monitoring the activity of B-GAL through the hydrolysis of the yellow chromogenic subtrate, chlorophenol red beta-D-galactopyranoside, which produces a red chlorophenol red product, assay evaluation, overview
food industry
industry
medicine
molecular biology
nutrition
synthesis
analysis
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enzyme can be used as a tool in the structural analysis of D-galactose-containing oligosaccharide chains, as well as for the synthesis of glycoconjugates
analysis
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the enzyme is a reliable marker for the course of replicative cell senescence
analysis
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comparison of commercially available kits to assess water quality and evaluation of their ability to detect Escherichia coli. Chromocult, MI agar, Readycult, and Colilert detect beta-glucuronidase production from respectively 79.9, 79.9, 81.1, and 51.4% of the 74 Escherichia coli strains tested. These four methods detect beta-galactosidase production from respectively 85.1, 73.8, 84.1, and 84.1% of the total coliform strains tested. The high level of false-negative results for Escherichia coli recognition obtained by all four methods suggests that they may not be appropriate for identification of presumptive Escherichia coli strains
analysis
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electrophoretic mobility and catalytic activity of individual molecules of enzyme are reproducible for each molecule but different for individual molecules. The observed ranges in electrophoretic motility are similar for different experimental protocols. There is no relationship between the observed activities and electrophoretic motilities
analysis
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precise and reliable detection of Escherichia coli strains for differentiation from biochemically and phylogenetically related bacteria. Method is based on polymerase chain reaction, in which four genes coding for lactose permease, cytochrome bd complex, beta-D-glucuronidase, and beta-D-galactosidase, serve as target DNA sequences
analysis
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enzyme functions both as a marker, promoting colony color development in the presence of a lactose analogue S-gal, and as a reporter enabling quantitative measurement by a simple colorimetric assay. The combination of BgaB expressed from promoters of varying strength with S-gal produces distinct black colonies in aerobic and anaerobic conditions at temperatures ranging from 37 to 60°C, being an advantage over the conventional beta-galactosidase (LacZ) and substrate X-gal. The system allows for construction and measurement of expression levels of a library in just 4 days
biotechnology
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the enzyme is suitable for obtaining fermentable sugars from whey wastes
biotechnology
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single enzyme molecule assays performed on the native enzyme as well as recombinant enzyme with and without His-tag reveal significant differences in the average combined turnover numbers indicating that in vivo and in vitro produced enzymes are not identical and the presence of a C-terminal His-tag may alter the activity of beta-galactosidase
food industry
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enzyme immobilization onto Amberlite MB-150 beads greatly stabilizes the enzyme preparation, with no loss of activity for 12 months at room temperature. Immobilized enzyme hydrolyzes 64.5% and 69.2% of lactose present in milk and milk whey, respectively, within 10 h at room temperature. Enzyme has a reusability of 10 batchwise uses, with almost no loss in activity
food industry
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immobilization of recombinant enzyme onto chitosan and use for hydrolyzation of lactose in milk in a packed bed reactor. Immobilized beta-galactosidase is stable at 4°C for six weeks, shows greater relative activity in presence of Ca2+, and hydrolyzes more than 80% of lactose in milk after 2 h of operation in the reactor
food industry
the enzyme is used for hydrolysis of lactose extracted from whey or milk
food industry
the recombinant thermostable beta-galactosidase may be suitable for the hydrolysis of lactose in milk processing
industry
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beta-galactosidases are important industrial enzymes used for the hydrolysis of lactose from milk and milk whey, preparation of the improved mutant strain H26-10-7, overview
industry
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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
industry
potentially an important industrial enzyme due to the broad specificity, catalytic efficiency and thermostability
industry
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assimilation of lactose as a by-product of dairy industry
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industry
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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
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medicine
design of CHO-K1 cells to produce feline beta-galactosidase for potential use in preclinical trials in a cat model of GM1 gangliosidosis
medicine
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enzyme may be suitable for the use as a digestive supplement for the alleviation of lactose intolerance
medicine
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investigation of the pattern and mechanism of distribution of beta-galactosidase in the adult GM1-galgliosidosis mouse brain upon hippocampla injection of an adeno-associated viral vector encoding beta-galactosidase. Distribution in brain is by diffusion, by axonal transport within the neurons from the site of production, and by cerebrospinal fluid flow in the perivascular space of Virchow-Robin. Evidence of axonal transport of vector-encoded mRNA
medicine
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transfection of beta-galactosidase gene to fibroblast cells in culture using liposomes. 24 h after transfection, treated cells show a higher specific enzyme activity than untreated cells. Cells maintained in culture for 7 days show values similar to those of untreated patients with GM1 gangliosidosis
medicine
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enzyme may be suitable for the use as a digestive supplement for the alleviation of lactose intolerance
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molecular biology
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senescence-associated beta-galactosidase activity is a widely used biomarker for assessing replicative sensescence in mammalian cells. Quantitative assay of senescence-associated beta-galactosidase activity in mammalian cell extracts. The assay is capable of detecting relatively subtle changes in activity and confirms that confluency and contact inhibition of growth can cause a small increase in the expression of this biomarker. The assay for measuring senescence-associated changes in beta-galactosidase is suitable for mechanistic studies of senescence regulation in which graduated changes in biomarker expression may be anticipated
molecular biology
expression of bgaH under the control of various halobacterial promoters of known strength leads to different specific beta-galactosidase activities in the lysates. Using Northern blot hybridization and semiquantitative RT-PCR, it is shown that the bgaH transcript level corresponds to the specific enzyme activity. Therefore, the bgaH gene of Haloferax alicantei is a useful tool for in vivo studies of gene expression in Halobacterium salinarum and possibly other halophilic Archaea
molecular biology
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expression of bgaH under the control of various halobacterial promoters of known strength leads to different specific beta-galactosidase activities in the lysates. Using Northern blot hybridization and semiquantitative RT-PCR, it is shown that the bgaH transcript level corresponds to the specific enzyme activity. Therefore, the bgaH gene of Haloferax alicantei is a useful tool for in vivo studies of gene expression in Halobacterium salinarum and possibly other halophilic Archaea
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nutrition
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hydrolysis of whey ultrafiltrate from continous production of ethanol with Kluyveromyces sp. yields a sweet syrup which can be used as sweetener
nutrition
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potential use of the enzyme in the hydrolysis of whey and of milk lactose
nutrition
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production of a sweetener for food industry by hydrolysis of lactose in permeate whey
nutrition
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enzyme potentially serves as an inexpensive beta-galactosidase in food industry
nutrition
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enzyme is a potential catalyst in whey-processing programmes
nutrition
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lactase entrapped in cellulose-triacetate fibers is originally used to produce low lactose milk
nutrition
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conversion of cheese whey into a sweet protein-rich syrup which can be used in baked goods and ice cream
nutrition
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large-scale production and application of immobilized enzyme in the production of sweetener by hydrolysis of lactose in wheys
nutrition
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large-scale production and application of immobilized enzyme in the production of sweetener by hydrolysis of lactose in wheys
nutrition
cold-adapted beta-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants
nutrition
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high thermostability and pH-stability and good hydrolytic capability make this enzyme potentially useful in dairy industry
nutrition
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it may be possible that the cold active beta-galactosidases from the isolated strains can be applied to the food industry, e.g. processing of milk and whey below 5°C
nutrition
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production of lactose-free milk for babies and people who are not able to produce or do not have enough beta-galactosidase activity
nutrition
recombinant Pseudoalteromonas sp. 22b beta-galactosidase could be applied at refrigeration temperatures for production of lactose-reduced dairy products
nutrition
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the cold-active acid beta-galactosidase can be applied to the food industries, removal of lactose from refrigerated milk for people who are lactose intolerant and conversion of the lactose to glucose and galactose, which are more fermentable sugars than lactose, in whey
nutrition
the enzyme has a potential application as a digestive supplement
nutrition
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the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
nutrition
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the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
nutrition
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the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
nutrition
wide acceptor specificity for transglycosylation reactions capable of the synthesis of important galactosyl compounds such as alkyl glycoside. The enzyme may be a novel tool for enzymatic synthesis with applications in the food, healthcare, and pharmaceutical industries
nutrition
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enzyme immobilization onto Amberlite MB-150 beads greatly stabilizes the enzyme preparation, with no loss of activity for 12 months at room temperature. Immobilized enzyme hydrolyzes 64.5% and 69.2% of lactose present in milk and milk whey, respectively, within 10 h at room temperature. Enzyme has a reusability of 10 batchwise uses, with almost no loss in activity
nutrition
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enzyme is suitable for both the hydrolysis of lactose and the production of galacto-oligosaccharides in milk processing
nutrition
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enzyme may be suitable for the use as a digestive supplement for the alleviation of lactose intolerance
nutrition
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immobilization of recombinant enzyme onto chitosan and use for hydrolyzation of lactose in milk in a packed bed reactor. Immobilized beta-galactosidase is stable at 4°C for six weeks, shows greater relative activity in presence of Ca2+, and hydrolyzes more than 80% of lactose in milk after 2 h of operation in the reactor
nutrition
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the in vitro digestibility of lactose and cellobiose is three times greater with the enzymes from suckling rats than with those from adult rats. Michaelis constant Km and maximum velocity Vmax values for cellobiose are 25 and 7 times lower, respectively, than those for lactose. Normal rats fed a 6% cellobiose diet show a greater cecal organic acid than those fed the control diet, but no differences are observed between those fed the control and 3% cellobiose diets
nutrition
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recombinant Pseudoalteromonas sp. 22b beta-galactosidase could be applied at refrigeration temperatures for production of lactose-reduced dairy products
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nutrition
Weizmannia coagulans RCS3
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high thermostability and pH-stability and good hydrolytic capability make this enzyme potentially useful in dairy industry
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nutrition
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enzyme may be suitable for the use as a digestive supplement for the alleviation of lactose intolerance
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nutrition
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the cold-active acid beta-galactosidase can be applied to the food industries, removal of lactose from refrigerated milk for people who are lactose intolerant and conversion of the lactose to glucose and galactose, which are more fermentable sugars than lactose, in whey
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nutrition
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the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
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nutrition
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enzyme potentially serves as an inexpensive beta-galactosidase in food industry
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nutrition
Priestia megaterium 2-37-4-1
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wide acceptor specificity for transglycosylation reactions capable of the synthesis of important galactosyl compounds such as alkyl glycoside. The enzyme may be a novel tool for enzymatic synthesis with applications in the food, healthcare, and pharmaceutical industries
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nutrition
Geobacillus stearothermophilus ATCC 8005
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enzyme is suitable for both the hydrolysis of lactose and the production of galacto-oligosaccharides in milk processing
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nutrition
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cold-adapted beta-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants
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synthesis
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simple and inexpensive method for synthesizing (2R)-glycerol-O-D-beta-galactopyranoside by utilization of the transgalalactosylating properties of beta-galactosidase and the chloroform solubility of a derivative of (2R)-glycerol-O-D-beta-galactopyranoside that is formed by the transfer of galactose onto isopropylidene glycerol
synthesis
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enzyme mutant E184A is a valuable catalyst for the synthesis of metabolically stable analogues of the important glycosidic linkages to the 3 and 4 positions of glucosides and galactosides
synthesis
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expression in Escherichia coli under control of araBD promoter. The addition of D-fucose causes an improvement in specific beta-galactosidase production, although beta-galactosidase is produced as an inclusion body. The addition of D-fucose after induction leads to an increase in the specific activity of beta-galactosidase inclusion bodies and causes a changes in the structure of beta-galactosidase inclusion bodies, with higher enzyme activity
synthesis
production of beta-galactosidase by expression of the genes encoding the large and the small subunit in Lactobacillus plantarum WCFS1. Cultivations yield about 23000 U of enzyme per l
synthesis
the enzyme catalyzes the production of the synthetic disaccharide lactulose (4-O-beta-D-galactopyranosyl-D-fructose) via a transgalactosylation using lactose as a galactose donor and fructose as an acceptor. Lactulose is used in treatment of hyperammonemia and as a gentle laxative. It is also applied to commercial infant formulas and various milk products because it specifically promotes the intestinal proliferation of Bifidobacterium, which creates an acid medium that inhibits the growth of undesirable bacteria
synthesis
the F441Y mutant enzyme has potential application in the industrial preparation of galactooligosaccharides
synthesis
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immobilization by covalent attachment onto Eupergit C with a binding efficiency of 95%. Immobilization increases both activity and stability at higher pH values and temperature but does not significantly change kinetic parameters for the substrate lactose. The immobilized enzyme shows a strong transgalactosylation reaction, resulting in the formation of galactooligosaccharides. The maximum yield of 34% galactooligosaccharides is obtained when the degree of lactose conversion is roughly 80%
synthesis
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fermentation parameters for the maximum production of cold active beta-galactosidase are pH 7.3, 82% (v/v) cheese whey, 3.84% tryptone. An overall 3.6fold increase in cold active beta-galactosidase production (34.37 U/ml) is achieved in optimized medium
synthesis
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immobilization and stabilization of beta-galactosidase on Duolite A568 using a combination of physical adsorption, incubation at pH 9.0 and cross-linking with glutaraldehyde leads to a 44% increase in enzymatic activity as compared with a two-step immobilization process (adsorption and cross-linking). The immobilized enzyme presents a good thermal stability at temperatures around 50°C, and very good pH stability in the range from 1.5 to 9.0
synthesis
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immobilization of enzyme on aminovinylsulfone. The enzyme is immobilized at moderate ion strength at pH values from 5.0 to 9.0 via ion exchange on aminovinylsulfone support. 50-80% of the initial activity and a stabilization factor of around 8-15 can be obtained
synthesis
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immobilization of enzyme on functionalized multi-walled carbon nanotubes. Acid functionalization using H2SO4/HNO3 is the most effivcient method. Enzyme maintains 51% of initial activity after 90 days at 4°C and more than 90% of initial activity up to the 4th recycle
synthesis
Optimal extracellular beta-galactosidase activity in recombinant Escherichia coli is observed when induction is initiated when the optical density at 600 nm reaches 40, when expression is induced at 37°C; and lactose is added at a constant feeding rate of 1.0 g/l/h. The extracellular activity reaches 220.0 U/ml, which represents 65.0% of the total beta-galactosidase activity expressed
synthesis
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synthesis of propyl-beta-galactoside using immobilized beta-galactosidase in glyoxyl-agarose. Reaction yield increases twofold with the glyoxyl-agarose derivative, and after ten sequential batches, the efficiency is 115% higher than obtained with the free enzyme. Enzyme immobilization favors product recovery, and avoids browning reactions. Propyl-beta-galactoside can be recovered with a purity above 99%
synthesis
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immobilization by covalent attachment onto Eupergit C with a binding efficiency of 95%. Immobilization increases both activity and stability at higher pH values and temperature but does not significantly change kinetic parameters for the substrate lactose. The immobilized enzyme shows a strong transgalactosylation reaction, resulting in the formation of galactooligosaccharides. The maximum yield of 34% galactooligosaccharides is obtained when the degree of lactose conversion is roughly 80%
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synthesis
Enterobacter ludwigii MCC 3423
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fermentation parameters for the maximum production of cold active beta-galactosidase are pH 7.3, 82% (v/v) cheese whey, 3.84% tryptone. An overall 3.6fold increase in cold active beta-galactosidase production (34.37 U/ml) is achieved in optimized medium
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synthesis
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the F441Y mutant enzyme has potential application in the industrial preparation of galactooligosaccharides
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synthesis
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production of beta-galactosidase by expression of the genes encoding the large and the small subunit in Lactobacillus plantarum WCFS1. Cultivations yield about 23000 U of enzyme per l
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synthesis
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the enzyme catalyzes the production of the synthetic disaccharide lactulose (4-O-beta-D-galactopyranosyl-D-fructose) via a transgalactosylation using lactose as a galactose donor and fructose as an acceptor. Lactulose is used in treatment of hyperammonemia and as a gentle laxative. It is also applied to commercial infant formulas and various milk products because it specifically promotes the intestinal proliferation of Bifidobacterium, which creates an acid medium that inhibits the growth of undesirable bacteria
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