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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

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

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

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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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
Phan Van Kiem et al.
Molecules (Basel, Switzerland), 25(11) (2020-06-03)
Gymnema sylvestre, a medicinal plant, has been used in Indian ayurvedic traditional medicine for the treatment of diabetes. Phytochemical investigation of Gymnema sylvestre led to the isolation of five new pregnane glycosides, gymsylosides A-E (1-5) and four known oleanane saponins
Nguyen Phuong Thao et al.
Journal of analytical methods in chemistry, 2018, 2794904-2794904 (2018-06-05)
As part of an ongoing search for new natural products from medicinal plants to treat type 2 diabetes, two new compounds, a megastigmane sesquiterpenoid sulfonic acid (1) and a new cyclohexylethanoid derivative (2), and seven related known compounds (3-9) were
P R Flanagan et al.
The Biochemical journal, 173(2), 553-563 (1978-08-01)
Maltase-glucoamylase, a microvillous membrane ectoenzyme, was solubilized from rat intestinal mucosa by digestion with papain and subsequently purified to homogeneity with an overall yield of 10--20%. An antibody to the purified enzyme formed a single precipitin line in immunodiffusion experiments

Protocols

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

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