Description

• General description: 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]
• 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].
• 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.[4]
• Unit Definition: One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
• Physical form: Lyophilized powder containing (NH4)2SO4, sodium citrate and sodium chloride.
• Other Notes: View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer