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G0413

Sigma-Aldrich

β(1→4)-Galactosidase, positionally specific from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

form

buffered aqueous solution

specific activity

≥6 units/mg protein

packaging

vial of 0.06 unit

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

Gene Information

human ... GLB1(2720)

General description

β-Galactosidase is present in bacteria, fungi, yeast and animal organs. It is also found in fruits, such as apples, almonds and apricots. β-Galactosidase is a tetramer and is made up of four polypeptide chains consisting of amino acids that assemble to form five structural domains. The domains are jelly roll barrel, a central domain that serves as an active site and the remaining domains are composed of β-sandwich and fibronectin.

Application

β(1→4)-Galactosidase, positionally specific from Streptococcus pneumonia has been used:
  • as a position-specific enzyme to study its effects in the terminal galactosylation with protective efficacy of glycosphingolipid (GSPL) in mice.
  • for the digestion of radioactive oligosaccharides.
  • as a position-specific enzymeto study its effects on the virulence profile of avirulent Leishmania donovani clone (A-LD).

Biochem/physiol Actions

β-Galactosidase plays a role in hydrolyzing the D-galactosyl moieties in oligosaccharides, polymers and secondary metabolites. It is widely applicable in the dairy industry to remove lactose from milk and dairy products for the benefit of lactose-intolerant individuals. β-Galactosidase is also applicable in the food industry to improve the sweetness, flavor and solubility.

Unit Definition

One unit will hydrolyze 1 μmole of p-nitrophenyl β-D-galactopyranoside per min at pH 5.0 at 37 °C.

Physical form

Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Virulence attenuation of a UDP-galactose/N-acetylglucosamine beta1, 4 galactosyltransferase expressing Leishmania donovani promastigote
Bhaumik, SK , et al.
Glycoconjugate Journal, 25(5), 459-472 (2008)
Shaima Saqib et al.
3 Biotech, 7(1), 79-79 (2017-05-14)
The enzyme β-galactosidases have been isolated from various sources such as bacteria, fungi, yeast, vegetables, and recombinant sources. This enzyme holds importance due to its wide applications in food industries to manufacture lactose-hydrolyzed products for lactose-intolerant people and the formation
Sources of beta-galactosidase and its applications in food industry
Saqib S, et al.
3 Biotech, 7(1), 79-79 (2017)
S K Bhaumik et al.
Glycoconjugate journal, 25(5), 459-472 (2008-01-17)
Protozoan parasites of the genus Leishmania are the causative agent of leishmaniasis, a disease whose manifestations in humans range from mild cutaneous lesions to fatal visceral infections. Human visceral leishmaniasis is caused by Leishmania donovani. Long-term culture in vitro leads
TLR4 and NKT cell synergy in immunotherapy against visceral leishmaniasis
Karmakar S, et al.
PLoS Pathogens, 8(4), 79-79 (2012)

Articles

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

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