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A1031

Sigma-Aldrich

α-Amylase from human saliva

greener alternative

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

CAS Number:
9000-90-2
Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
EC Number:
232-565-6
MDL number:
MFCD00081319
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

type

Type XIII-A

Quality Level

200

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

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UniProt accession no.

P0DUB6

greener alternative category

Enabling,

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

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P342 + P311

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)

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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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
Aleix Lluansí et al.
Frontiers in microbiology, 12, 716307-716307 (2021-10-29)
Inflammatory bowel disease (IBD), including its two main categories (Crohn's disease and ulcerative colitis), has been linked both to gut microbiota and to diet. Bread is a daily food that has a potential capacity as a prebiotic. Our aim was
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
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Protocols

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

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