G3651
α-Glucosidase from Bacillus stearothermophilus
lyophilized powder, ≥50 units/mg protein
Synonym(s):
α-D-Glucoside glucohydrolase, Maltase
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About This Item
Recommended Products
form
lyophilized powder
Quality Level
specific activity
≥50 units/mg protein
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
foreign activity
β-Glucosidase, α−galactosidase and β−galactosidase ≤0.1%
greener alternative category
relevant disease(s)
diabetes (management of non-insulin-dependent diabetes mellitus)
storage temp.
2-8°C
General description
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch hydrolysis research. For more information see the article in biofiles.
Application
α-glucosidase is potential enzyme for the biosynthesis of complex carbohydrates.
Biochem/physiol Actions
α-glucosidase hydrolyzes carbohydrates by acting on 1,4-α linkages. Inhibition of α-glucosidase is a prominent target in the management of non-insulin-dependent diabetes mellitus.
Unit Definition
One unit will liberate 1.0 μmole of D-glucose from p-nitrophenyl α-D-glucoside per min at pH 6.8 at 37 °C.
Physical form
Lyophilized powder containing potassium phosphate buffer salt
Analysis Note
Activity using maltose as substrate at pH 6.0 at 25 deg C is ~2X greater than that obtained using p-nitrophenyl-α-D-glucoside as substrate at pH 6.8 at 37 °C.
Protein determined by biuret.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
inhibitor
substrate
Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Arzu Coleri Cihan et al.
Cell biochemistry and function, 30(1), 69-81 (2011-10-27)
Two different α-glucosidase-producing thermophilic E134 strains were isolated from a hot spring in Kozakli, Turkey. Based on the phenotypic, phylogenetic and chemotaxonomic evidence, the strain was proposed to be a species of G. toebii. Its thermostable exo-α-1,4-glucosidases also were characterized
B Setlow et al.
Journal of applied microbiology, 120(5), 1326-1335 (2016-01-26)
This study was to determine the sources, location and identity of α-glucosidases in dormant/germinating/outgrowing spores and growing cells of Geobacillus stearothermophilus ATCC 7953, an enzymatic activity in spores used in rapid tests of steam sterilization. α-Glucosidase activity in spores and
A D Baron
Diabetes research and clinical practice, 40 Suppl, S51-S55 (1998-09-18)
Fasting blood glucose level is usually used to diagnose diabetes, but is not a good predictor of postprandial hyperglycaemia, which is a more accurate measure of the metabolic defect underlying type 2 diabetes. Postprandial blood glucose levels may be elevated
Jenna Magat et al.
The Journal of biological chemistry, 298(12), 102625-102625 (2022-10-29)
Mucopolysaccharidosis type IIIA (MPS IIIA) is a lysosomal storage disorder caused by N-sulfoglucosamine sulfohydrolase (SGSH) deficiency. SGSH removes the sulfate from N-sulfoglucosamine residues on the nonreducing end of heparan sulfate (HS-NRE) within lysosomes. Enzyme deficiency results in accumulation of partially
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