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A4268

Sigma-Aldrich

α-Amylase from porcine pancreas

greener alternative

Type I-A, PMSF treated, saline suspension, 700-1400 units/mg protein (E1%/280)

Synonyme(s) :

β-N-acetylglucosaminidase porcine placenta, PPA, al1,4 glucan-4-glucanohydrolase,, porcine pancreas α-amylase

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About This Item

Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

Porcine pancreas

Type

Type I-A

Forme

saline suspension

Activité spécifique

700-1400 units/mg protein (E1%/280)

Poids mol.

51-54 kDa

Caractéristiques du produit alternatif plus écologique

Waste Prevention
Design for Energy Efficiency
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sustainability

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Technique(s)

activity assay: suitable

Adéquation

suitable for hydrolysis, synthesis of oligosaccharides and polysaccharides, and sugar modification

Application(s)

diagnostic assay manufacturing

Autre catégorie plus écologique

Température de stockage

2-8°C

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Description générale

Molecular mass: 51-54 kDa.
α-Amylase isolated from porcine pancreas is a glycoprotein. It is a single polypeptide chain of ~475 residues containing two SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability. Chloride ions are necessary for activity and stability. The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.
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. α-Amylase, from Sigma, has been used in various plant studies, such as metabolism studies in Arabidopsis .

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. α -Amylase, from porcine pancreas, is a glycoprotein that consists of a single polypeptide chain of approximately 475 residues containing 2 SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability.

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

Suspension in 2.9 M NaCl solution containing 3 mM CaCl2.

Notes préparatoires

2× crystallized

Inhibiteur

Réf. du produit
Description
Tarif

Substrat

Pictogrammes

Health hazard

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

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Doudou Huang et al.
Drug design, development and therapy, 15, 5001-5010 (2021-12-25)
Diabetes is a common disease caused by a combination of genetic and environmental factors, which was the top three diseases threatening human health. Therefore, it is necessary to seek more efficient hypoglycemic drugs. The main objective of this study was
Lijiao Kan et al.
Food chemistry, 361, 130047-130047 (2021-05-25)
Inhibition of maltase, sucrase, isomaltase and glucoamylase activity by acarbose, epigallocatechin gallate, epicatechin gallate and four polyphenol-rich tea extract from white, green, oolong, black tea, were investigated by using rat intestinal enzymes and human Caco-2 cells. Regarding rat intestinal enzyme
Annabel Bijttebier et al.
Carbohydrate research, 345(2), 235-242 (2009-12-08)
Amylopectin fine structures were studied following limited hydrolysis of gelatinised waxy maize starch by amylases with a different level of inner chain attack (LICA). This was done by size exclusion chromatography as well as by debranching the (partially hydrolysed) amylopectin
Saber Abdelkader Saidi et al.
Heliyon, 8(12), e11954-e11954 (2022-12-09)
The study evaluated the phytochemical composition of Ephedra alata and its effects on α-amylase and lipase enzymes and diabetic-induced liver-kidney-testes toxicities to determine the anti-diabetic, anti-obesity, and anti-toxic potentials of the plant. Obesity was induced by a high-fat and fructose
Bjarte Aarmo Lund et al.
Molecules (Basel, Switzerland), 26(23) (2021-12-11)
The determination of the temperature dependence of enzyme catalysis has traditionally been a labourious undertaking. We have developed a new approach to the classical Arrhenius parameter estimation by fitting the change in velocity under a gradual change in temperature. The

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