A1031
α-Amylase from human saliva
Type XIII-A, lyophilized powder, 300-1,500 units/mg protein
Synonym(s):
1,4-α-D-Glucan-glucanohydrolase
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About This Item
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type
Type XIII-A
Quality Level
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
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UniProt accession no.
greener alternative category
storage temp.
−20°C
Gene Information
human ... AMY1A(276)
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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.
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.
Unit Definition
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.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
substrate
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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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