Sigma-Aldrich α-Amylase from Bacillus licheniformis. Type XII-A, saline solution, ≥500 units/mg protein (biuret). 1000000 units

α-Amylase is a member of the endo-amylase family. Its molecular weight is 57.6 kDa. α-Amylase is composed of three functional domains namely A, B and C. Domain A is a barrel-shaped (β/α)₈ structure and is the largest domain. Domain B is linked to domain A via disulfide bond and is present between domain A and C. Domain C is composed of β-sheets and is connected to domain A via a polypeptide chain.[1]
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α-Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. Product A3403 is from Bacillus licheniformis and is type XII-A. α-Amylase, from Sigma, has been used in various plant studies, such as metabolism studies in Arabidopsis [2].

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.

Aqueous solution containing sodium chloride and sucrose

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

A product of Novozyme Corp.

Termamyl is a registered trademark of Novozymes Corp.

Reported to be heat stable at temperatures as high as ∼90 °C.