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

Authors
  • A R Orlando
  • P Ade
  • D Di Maggio
  • C Fanelli
  • L Vittozzi
Publication Date
Feb 01, 1983
Source
PMC
Keywords
Disciplines
  • Biology
License
Unknown

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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