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Merck

G3651

Sigma-Aldrich

α-Glucosidase from Bacillus stearothermophilus

greener alternative

lyophilized powder, ≥50 units/mg protein

Sinónimos:

α-D-Glucoside glucohydrolase, Maltase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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.

inhibitor

Referencia del producto
Descripción
Precios

substrate

Referencia del producto
Descripción
Precios

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Sanaid Ghauri et al.
3 Biotech, 11(4), 167-167 (2021-04-06)
Diabetes mellitus is a metabolic disorder of carbohydrate metabolism. The management of Diabetes mellitus with phytochemicals is hallmark of this research. Citrus species are known for their health benefits and are used as traditional food in South East Asia. The
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
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
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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