G3665
β-Galactosidase from Kluyveromyces lactis
≥2600 units/g
Synonym(s):
Lactozyme® 2600 L, Lactase
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About This Item
Recommended Products
form
liquid
specific activity
≥2600 units/g
concentration
≥2600 units/g
storage temp.
2-8°C
Related Categories
General description
A β-galactosidase preparation produced by submerged fermentation of a selected strain of the yeast Kluyveromyces lactis.
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.
Legal Information
A product of Novozyme Corp.
Lactozyme is a registered trademark of Novozymes Corp.
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
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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Robert E Ward et al.
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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
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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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