G0660
α-Glucosidase from Saccharomyces cerevisiae
recombinant, expressed in proprietary host, lyophilized powder, ≥100 units/mg protein
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recombinant
expressed in proprietary host
Quality Level
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
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.
inhibitor
substrate
Product No.
Description
Pricing
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Synthesis and biological evaluation of 3-arylcoumarin derivatives as potential anti-diabetic agents.
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
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)
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)
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