α-Amylase from porcine pancreas

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.

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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 . α-Amylase, from porcine pancreas, has been used to remove starch during the study of starch metabolism and ripening in tomatoes .

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. The pH optimum is at 7.

Package size based on α-amylase activity

Contains lactose

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

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