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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:
9031-11-2
Enzyme Commission number:
3.2.1.23 (BRENDA, IUBMB)
MDL number:
MFCD01092684
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

100

form

buffered aqueous solution

specific activity

≥6 units/mg protein

packaging

vial of 0.06 unit

UniProt accession no.

P16278

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Qayyum Husain
Critical reviews in biotechnology, 30(1), 41-62 (2010-02-11)
Beta galactosidases have been obtained from microorganisms such as fungi, bacteria and yeasts; plants, animals cells, and from recombinant sources. The enzyme has two main applications; the removal of lactose from milk products for lactose intolerant people and the production
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