Trehalase in Conidia of Aspergillus oryzae

Author:

Horikoshi Koki1,Ikeda Yonosuke1

Affiliation:

1. Department of Microbiology, The Institute of Physical and Chemical Research, Komagome, Bunkyo-ku, Tokyo, Japan

Abstract

Horikoshi, Koki (The Institute of Physical and Chemical Research, Bunkyo-ku, Tokyo, Japan), and Yonosuke Ikeda . Trehalase in conidia of Aspergillus oryzae . J. Bacteriol. 91: 1883–1887. 1966.—Trehalases (soluble trehalase and coat-bound trehalase) were found in the conidia of Aspergillus oryzae , and the total activity of the trehalases increased during the germination process. The soluble trehalase was purified by diethylaminoethyl-cellulose column chromatography; its optimal p H, Michaelis constant, and heat stability were studied. In vitro, the trehalases were competitively inhibited by d -mannitol, which was also contained in the conidia. Since the trehalose content in the conidia decreased at an early stage of germination, it was assumed that trehalase might begin to hydrolyze trehalose after the inhibitory effect of d -mannitol decreased.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference15 articles.

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