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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)

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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Articles

Learn about O-linked glycan strategies, such as the actions of O-glycosidase, how to remove di and trisialylation sialic acid residues, β-linked galactose, and N-acetylglucosamine, as well as other O-glycan modifications.

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