α-Amylase from Bacillus sp.

Contains starch as an extender.

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-has also been also used to study the ability of corn and starch to protect enzyme activity. The enzyme has been used to compare the effects of bacterial and fungal α-amylase and scalded flour on bread quality and shelflife. It has also been used to determine the optimal levels of these components in order to achieve maximum volume and bread freshness. Furthermore, it has been used to digest hydroxypropylated starch in Korean waxy rice cake to retard retrogradation.

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, isolated from Bacillus subtilis is a dimer and has a monomer molecular weight of 48.9 kDa. α-Amylase is a metalloprotein and contains atleast one mol of calcium ion. The presence of calcium ion increases the stability of the enzyme towards denaturation by heat, acid, or urea. The pH range for activity of this product is 5.0 to 7.5, with the optimum pH range being 6.0-7.0. This product is stable from pH 5.0 to 10.0. The optimum temperature range is 65-75 °C. The effective temperature range is up to 90 °C.

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