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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:
9001-42-7
Enzyme Commission number:
3.2.1.20 (BRENDA, IUBMB)
EC Number:
232-604-7
MDL number:
MFCD00081321
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.

P38158
P53341

greener alternative category

Enabling,

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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
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)
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
Rutger Hermsen et al.
Molecular systems biology, 11(4), 801-801 (2015-04-12)
When bacteria are cultured in medium with multiple carbon substrates, they frequently consume these substrates simultaneously. Building on recent advances in the understanding of metabolic coordination exhibited by Escherichia coli cells through cAMP-Crp signaling, we show that this signaling system
Bernard Ntezimana et al.
Foods (Basel, Switzerland), 10(11) (2021-11-28)
The present study emphasizes the effect of withering time set at 4 ± 0.5 h (WT4), 6 ± 0.5 h (WT6), 8 ± 0.5 h (WT8), 10 ± 0.5 h (WT10), and 12 ± 0.5 h (WT12) on the sensory
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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)

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