Chemistry of Natural Compounds

, Volume 17, Issue 3, pp 288–293 | Cite as

Isolation and characterization of an acid proteinase fromAspergillus oryzae

  • V. I. Shitova
  • M. A. Samartsev
  • S. V. Kulikov
  • N. V. Belyakov
Article
  • 24 Downloads

Abstract

The heat stability, substrate specificity, and the pH optima of activation and inhibition of an acid proteinase isolated from the industrial preparation amilorizin Pkh have been studied. The enzyme has been found active in the hydrolysis of chromophoric peptide substrates of the type of Dnp-Gly-Gly-X-Arg-OH, where X = Phe, Met, Trp. Inhibition of the enzymatic activity by pepstatin and covalent inhibitors of carboxylic proteinases show that this enzyme belongs to the proteinases of the pepsin type.

Keywords

Sodium Acetate Buffer Pepstatin Acid Proteinase Phenylmethanesulfonyl Fluoride Amylolytic Activity 

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Copyright information

© Plenum Publishing Corporation 1982

Authors and Affiliations

  • V. I. Shitova
  • M. A. Samartsev
  • S. V. Kulikov
  • N. V. Belyakov

There are no affiliations available

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