G3665
β-Galactosidase from Kluyveromyces lactis
≥2600 units/g
Sinónimos:
Lactozyme® 2600 L, Lactase
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Permítanos ayudarleNombre del producto
β-Galactosidase from Kluyveromyces lactis, ≥2600 units/g
form
liquid
specific activity
≥2600 units/g
concentration
≥2600 units/g
storage temp.
2-8°C
Quality Level
Categorías relacionadas
Application
β-galactosidases from different species, including Kluyveromyces lactis and Kluyveromyces fragilis, hydrolyze lactose.
Biochem/physiol Actions
β-galactosidase cleaves lactose into its monosaccharide components, glucose and galactose. It also catalyzes the transglycosylation of glucose into allolactose, the inducer of β-galactosidase, in a feedback loop.
General description
A β-galactosidase preparation produced by submerged fermentation of a selected strain of the yeast Kluyveromyces lactis.
Legal Information
A product of Novozyme Corp.
Lactozyme is a registered trademark of Novozymes Corp.
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Robert E Ward et al.
Molecular nutrition & food research, 51(11), 1398-1405 (2007-10-30)
This study was conducted to investigate the catabolism and fermentation of human milk oligosaccharides (HMO) by individual strains of bifidobacteria. Oligosaccharides were isolated from a pooled sample of human milk using solid-phase extraction, and then added to a growth medium
Arun Beniwal et al.
3 Biotech, 7(5), 349-349 (2017-09-29)
The dairy yeast
Justyna Skoczek et al.
Food chemistry, 294, 231-237 (2019-05-28)
A fully mechanized Arduino-controlled multi-pumping flow analysis system and procedure for the determination of β-galactosidase activity are proposed. The applied bioanalytical method is based on the determination of p-nitrophenol formed in the course of enzyme-catalyzed hydrolysis of p-nitrophenyl-galactopyranosides. The photometric
D H Juers et al.
Protein science : a publication of the Protein Society, 8(1), 122-136 (1999-04-21)
Beta-galactosidase (lacZ) from Escherichia coli is a 464 kDa homotetramer. Each subunit consists of five domains, the third being an alpha/beta barrel that contains most of the active site residues. A comparison is made between each of the domains and
Anca D Petrescu et al.
Protein expression and purification, 58(2), 184-193 (2008-01-08)
Acyl coenzyme A binding protein (ACBP) has been proposed to transport fatty acyl CoAs intracellularly, facilitating their metabolism. In this study, a new mouse recombinant ACBP was produced by insertion of a histidine (his) tag at the C-terminus to allow
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