Merck, A3176-500KU, α-Amylase from porcine pancreas

General description
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 . α-Amylase, from porcine pancreas, has been used to remove starch during the study of starch metabolism and ripening in tomatoes .
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. 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.
Packaging
Package size based on α-amylase activity
Analysis Note
Contains lactose
Other Notes
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