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


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.


Sodium Acetate Buffer Pepstatin Acid Proteinase Phenylmethanesulfonyl Fluoride Amylolytic Activity 


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Literature cited

  1. 1.
    T. Nakadai and S. Nasuno, J. Ferment. Technol.,54, 872 (1976).Google Scholar
  2. 2.
    Y. Tsujita and A. Endo, Biochim. Biophys. Acta,445, 194 (1976).CrossRefGoogle Scholar
  3. 3.
    R. Davidson, A. Gertler, T. Hofmann, Biochem. J.,147, 45 (1975).CrossRefGoogle Scholar
  4. 4.
    L. S. Lobareva and V. M. Stepanova, Usp. Biol. Khim.,19, 83 (1978).Google Scholar
  5. 5.
    N. P. Denisova, V. P. Zhemkov, and E. N. Morozova, Mikol, Fitopatol.,13, 127 (1979).Google Scholar
  6. 6.
    Y. Tsujita and A. Endo, J. Biochem.,81, 1063 (1977).CrossRefGoogle Scholar
  7. 7.
    W. S. Rickert and P. A. McBride-Warren, Can. J. Biochem.,54, 120 (1976).CrossRefGoogle Scholar
  8. 8.
    N. M. Azarenkova, T. I. Vaganova, A. Ya. Strongin, and V. M. Stepanov, Biokhimiya,41, 20 (1976).Google Scholar
  9. 9.
    L. A. Lyublinskaya, L. V. Lastovetskaya, T. V. Shekhvatova, T. I. Vaganova, and V. M. Stepanov, Khim. Prir. Soedin., 75 (1976).Google Scholar
  10. 10.
    L. A. Lyublinskaya, T. I. Vaganova, L. D. Yakusheva, E. S. Oksenoit, and V. M. Stepanov, IVth All-Union Symposium on the Chemistry of Proteins and Peptides [in Russian], Minsk (1977), p. 197.Google Scholar
  11. 11.
    S. I. Virovets, V. F. Martynov, and M. I. Titov, Zh. Obshch. Khim.,38, 2337 (1968).Google Scholar
  12. 12.
    M. M. Bradford, Anal. Biochem.,72, 248 (1976).CrossRefGoogle Scholar
  13. 13.
    R. M. Attia and S. A. Ali, Z. Bacteriol., II,132, 193 (1977).Google Scholar
  14. 14.
    M. P. Filatova, R. M. Krit, G. S. Suchkova, G. A. Ravde', and V. T. Ivanov, Bioorgan. Khim.,1, 437 (1975).Google Scholar
  15. 15.
    V. M. Stepanov, L. S. Lobareva, and N. Y. Maltsev, Biochim. Biophys. Acta,151, 719 (1968).CrossRefGoogle Scholar
  16. 16.
    E. R. Marle, J. Chem. Soc.,101, 305 (1912).CrossRefGoogle Scholar
  17. 17.
    J.-C. Cripon, Biochemie, 58, 747 (1976).CrossRefGoogle Scholar
  18. 18.
    W.-J. Chang, S. Horiuchi, K. Takahashi, M. Yamasaki, and Y. Yamada, J. Biochem.,80, 975 (1976).CrossRefGoogle Scholar
  19. 19.
    C. W. Ward, Anal. Biochem.,74, 242 (1976).CrossRefGoogle Scholar

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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