As mentioned in the 'DESCRIPTION' section, this product is a lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride. This product is not tested for purity. However, buffer salts are expected to be the bulk of the non-protein content.
A1031
α-Amylase from human saliva
Type XIII-A, lyophilized powder, 300-1,500 units/mg protein
Synonyme(s) :
1,4-α-D-Glucan-glucanohydrolase
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1000 UNITS
114,00 €
5000 UNITS
414,00 €
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1000 UNITS
114,00 €
5000 UNITS
414,00 €
About This Item
Produits recommandés
Type
Type XIII-A
Niveau de qualité
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
Autre catégorie plus écologique
Température de stockage
−20°C
Informations sur le gène
human ... AMY1A(276)
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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.[1]
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 [2]. α-Amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity [3].
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.[4]
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
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
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
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Certificats d'analyse (COA)
Lot/Batch Number
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Les clients ont également consulté
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
Protocoles
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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Hi, could you let me know what the remaining composition is when the product contains 5-15% protein? Thank you!
1 réponse-
Utile ?
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Please let me know the storage temperature and storage period when it is dissolved in water
1 réponse-
The stability of this material in solution has not been investigated. However, various sources suggest that solutions may be stored in working aliquots at -20°C for several months.
Utile ?
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What is the recommended method for dissolving alpha amylase obtained from human saliva, specifically A1031?
1 réponse-
The recommended method is to dissolve the enzyme in 1mM calcium chloride (CaCl2).
Utile ?
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Could you please tell me the weight (mg or gram) of sample A1031?
1 réponse-
This product is sold based on units of activity. The activity specification is 300 - 1500 U/mg. The unit per milligram value is reported in the lot-specific Certificate of Analysis and will range from 0.67 to 3.3 mg for the 1000 U pack size.
See the link below to review a sample Certificate:
https://www.sigmaaldrich.com/certificates/sapfs/PROD/sap/certificate_pdfs/COFA/Q14/A1031-1KU0000270112.pdfUtile ?
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