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. 1983 Feb 1;209(2):561-4.
doi: 10.1042/bj2090561.

The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins

A R Orlando, P Ade, D Di Maggio, C Fanelli, L Vittozzi

The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins

A R Orlando et al. Biochem J. .

Abstract

A new alpha-amylase (EC 3.2.1.1) from Bacillus subtilis was purified by affinity chromatography. The molecular weight of the purified enzyme, estimated from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 93000, which is very different from the molecular weights of two well-characterized amylases from B. subtilis. Electrofocusing showed an isoelectric point of 5. Amylase shows a broad maximum of activity between pH 6 and 7; maximal inhibition of enzyme by wheat-protein alpha-amylase inhibitors is displayed at pH 7.

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