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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

Synonyme(s) :

1,4-α-D-Glucan-glucanohydrolase

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About This Item

Numéro CAS:
9000-90-2
Numéro de classification (Commission des enzymes):
3.2.1.1 (BRENDA, IUBMB)
Numéro CE :
232-565-6
Numéro MDL:
MFCD00081319
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Type

Type XIII-A

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

300-1,500 units/mg protein

Composition

Protein, 5-15% biuret

Caractéristiques du produit alternatif plus écologique

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

Numéro d'accès UniProt

P0DUB6

Autre catégorie plus écologique

Enabling,

Température de stockage

−20°C

Informations sur le gène

human ... AMY1A(276)

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Catégories apparentées

Description générale

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 .

Actions biochimiques/physiologiques

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.

Définition de l'unité

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.

Forme physique

Lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride.

Autres remarques

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Substrat

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P342 + P311

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
Camila Gabriel Kato-Schwartz et al.
Food research international (Ottawa, Ont.), 137, 109462-109462 (2020-11-26)
A practical approach to control glycemia in diabetes is to use plant natural products that delay hydrolysis of complex sugars and promote the diminution of the release of glucosyl units into the blood plasma. Polyphenolics have been described as being
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Protocoles

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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