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G0660

Sigma-Aldrich

α-Glucosidase from Saccharomyces cerevisiae

greener alternative

recombinant, expressed in proprietary host, lyophilized powder, ≥100 units/mg protein

Synonym(s):

α-D-Glucosidase, α-D-Glucoside glucohydrolase, Maltase from yeast

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in proprietary host

form

lyophilized powder

specific activity

≥100 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

UniProt accession no.

greener alternative category

shipped in

wet ice

storage temp.

2-8°C

Gene Information

bakers yeast ... MAL12(853209) , MAL32(852602)

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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

For the determination of α-amylase and the synthesis of various 1′-O-sucrose and 1-O-fructose esters

Biochem/physiol Actions

Hydrolysis of terminal, non-reducing 1→4-linked D-glucose residues with release of D-glucose.

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 pH 7.15 and Approx. 70% lactose

Analysis Note

Protein determined by biuret.

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)

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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M Ali et al.
Journal of enzyme inhibition and medicinal chemistry, 35(1), 692-701 (2020-03-12)
A new series of thiobarbituric (thiopyrimidine trione) enamine derivatives and its analogues barbituric acid derivatives was synthesised, characterised, and screen for in vitro evaluation of α-glucosidase enzyme inhibition and anti-glycation activity. This series of compounds were found to inhibit α-glucosidase activity
Yuheng Hu et al.
Journal of enzyme inhibition and medicinal chemistry, 34(1), 15-30 (2018-10-27)
A variety of substituted 3-arylcoumarin derivatives were synthesised through microwave radiation heating. The method has characteristics of environmental friendliness, economy, simple separation, and purification process, less by-products and high reaction yield. Those 3-arylcoumarin derivatives were screened for antioxidant, α-glucosidase inhibitory
Qiulian He et al.
Journal of oleo science, 71(6), 863-873 (2022-05-19)
In this study, some phenolic compounds including 4-Hexylresorcinol, 5-Pentadecylresorcinol, 5-Tricosylresorcinol, Bilobol, and Urushiol were tested against α-glycosidase enzyme from Saccharomyces cerevisiae and sorbitol dehydrogenase enzymes from sheep liver. These compounds determined good inhibition properties against α-glycosidase and sorbitol dehydrogenase (SDH)
Ton That Huu Dat et al.
Antibiotics (Basel, Switzerland), 10(12) (2021-12-25)
Mangrove plant endophytic bacteria are prolific sources of bioactive secondary metabolites. In the present study, twenty-three endophytic bacteria were isolated from the fresh roots of the mangrove plant Rhizophora apiculata. The identification of isolates by 16S rRNA gene sequences revealed
Chengcheng Zhang et al.
Frontiers in nutrition, 9, 854680-854680 (2022-05-17)
Olive leaves, which are the most abundant byproducts of the olive industry, offer multiple health benefits. The investigation of the phytochemical profiles and relevant biological activities is an essential step toward transforming these low-value byproducts into value-added ones. This study

Protocols

Enzymatic Assay of α-Glucosidase by the Modified Boehenger Procedure (EC 3.2.1.20)

Enzymatic Assay of α-Glucosidase by the Modified Boehenger Procedure (EC 3.2.1.20)

Enzymatic Assay of α-Glucosidase by the Modified Boehenger Procedure (EC 3.2.1.20)

Enzymatic Assay of α-Glucosidase by the Modified Boehenger Procedure (EC 3.2.1.20)

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