Molecular Cloning and Sequence Analysis of a Gene Encoding an Aspartic Proteinase from Aspergillus Oryzae

  • M. Takeuchi
  • K. Ogura
  • T. Hamamoto
  • Y. Kobayashi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 362)

Abstract

Aspergillus oryzae is one of the most important filamentous fungi used as koji in traditional Japanese fermentation industries such as sake, shoyu and miso manufacturing industries.1 A. oryzae secretes a number of hydrolases such as proteinases, amylases and lipases.2 The koji is used as enzyme source and starters of the fermented foods. In the proteinaceous fermented foods, aspartic proteinases play an important role, since the fermentation is carried out at acidic conditions. Accordingly, many studies on the physicochemical and enzymatic properties of `the proteinases purified from A. oryzae have been done.3 Several forms of the aspartic proteinases have been purified and characterized from A. oryzae 4 and it has been proved to have trypsinogen-kinase activity which is capable of activating trypsinogen and chymotrypsinogen.5 But limited information is available on the structure, function and gene organization of the enzymes. In order to clarify their diversity, structure and function at the molecular level, cloning and analysis of aspartic proteinase genes were carried out.

Keywords

Fermentation Codon Lipase Cysteine Aspergillus 

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • M. Takeuchi
    • 1
  • K. Ogura
    • 1
  • T. Hamamoto
    • 1
  • Y. Kobayashi
    • 1
  1. 1.Laboratory of Molecular Biology and Microbial Chemistry TokyoUniversity of Agriculture and TechnologyFuchu, TokyoJapan

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