G0413
β(1→4)-Galactosidase, positionally specific from Streptococcus pneumoniae
recombinant, expressed in E. coli, buffered aqueous solution
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1 VIAL
$482.000
$482.000
Fecha estimada de envío03 de mayo de 2025
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1 VIAL
$482.000
About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.32
$482.000
Fecha estimada de envío03 de mayo de 2025
Productos recomendados
recombinante
expressed in E. coli
Nivel de calidad
Formulario
buffered aqueous solution
actividad específica
≥6 units/mg protein
envase
vial of 0.06 unit
Nº de acceso UniProt
Condiciones de envío
wet ice
temp. de almacenamiento
2-8°C
Información sobre el gen
human ... GLB1(2720)
Descripción general
β-Galactosidase is present in bacteria, fungi, yeast and animal organs. It is also found in fruits, such as apples, almonds and apricots.[1] 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.[2]
Aplicación
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.[3]
- for the digestion of radioactive oligosaccharides.[4]
- as a position-specific enzymeto study its effects on the virulence profile of avirulent Leishmania donovani clone (A-LD).[5]
Acciones bioquímicas o fisiológicas
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.[1]
Definición de unidad
One unit will hydrolyze 1 μmole of p-nitrophenyl β-D-galactopyranoside per min at pH 5.0 at 37 °C.
Forma física
Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Los clientes también vieron
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
Artículos
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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