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About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-565-6
NACRES:
NA.54
MDL number:
Specific activity:
300-1,500 units/mg protein
type
Type XIII-A
form
lyophilized powder
specific activity
300-1,500 units/mg protein
composition
Protein, 5-15% biuret
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
storage temp.
−20°C
Quality Level
Gene Information
human ... AMY1A(276)
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Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
Physical form
Lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride.
Application
α-Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. Product A1031 is from human saliva, is type IIA, and is supplied as a lyophilized powder. α-Amylase has been used in various plant studies, such as metabolism studies in Arabidopsis . α-Amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity .
Biochem/physiol Actions
α-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose.
General description
Human α-amylase is made up of 496 amino acids in a single polypeptide chain, which is encrypted on chromosome 1. These are produced either in the salivary glands or the pancreas. The salivary and pancreatic α-amylases have homologous primary sequence but exhibit different cleavage patterns.
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 ethanol research. For more information see the article in biofiles.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Lana Zupancic Cepic et al.
Oral diseases, 26(5), 1072-1080 (2020-03-04)
This study aimed to characterize surface properties such as roughness (Ra) and surface-free energy (SFE) of glazed and polished yttria-stabilized zirconia and to evaluate in vitro adherence of fungus Candida albicans and salivary bacteria, Staphylococcus epidermidis, mixed with C. albicans
Digestive enzyme inhibitors from grains as potential components of nutraceuticals.
D Piasecka-Kwiatkowska, et al.
J. Nutr. Sci. Vitaminol., 58, 217-220 (2012)
G D Brayer et al.
Protein science : a publication of the Protein Society, 4(9), 1730-1742 (1995-09-01)
The structure of human pancreatic alpha-amylase has been determined to 1.8 A resolution using X-ray diffraction techniques. This enzyme is found to be composed of three structural domains. The largest is Domain A (residues 1-99, 169-404), which forms a central
Priscila Brigide et al.
Food & function, 10(8), 4802-4810 (2019-07-19)
The present work evaluated the effect of different processes in relation to mineral content and its bioavailability, as well as the effect of phytate and oxalate contents in biofortified beans. The following treatments were evaluated: raw beans (RB), cooked and
Guadalupe Lavado et al.
Foods (Basel, Switzerland), 10(8) (2021-08-28)
The effect of nitrate/nitrite (0, 37.5, 75, and 150 mg/kg) in the dry-cured loin formulation on the formation of lipid and protein oxidation products during in vitro digestion was evaluated. Dry-cured loins formulated with nitrate/nitrite resulted in significantly less lipid
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