Mannitol and Mannitol Dehydrogenases in Conidia of Aspergillus oryzae

Author:

Horikoshi Koki1,Iida Shigeji1,Ikeda Yonosuke1

Affiliation:

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

Abstract

Horikoshi, Koki (The Institute of Physical and Chemical Research, Tokyo, Japan), Shigeji Iida, and Yonosuke Ikeda . Mannitol and mannitol dehydrogenases in conidia of Aspergillus oryzae . J. Bacteriol. 89: 326–330. 1965.—A sugar alcohol was isolated from the conidia of Aspergillus oryzae and identified as d -mannitol. Two types of d -mannitol dehydrogenases, nicotinamide adenine dinucleotide phosphate-linked and nicotinamide adenine dinucleotide-linked, were found in the conidia. Substrate specificities, p H optima, Michaelis-Menton constants, and the effects of inhibitors were studied. d -Mannitol was converted to fructose by the dehydrogenases. Synthesis of d -mannitol dehydrogenases was not observed during germination; the content of d -mannitol decreased at an early stage of germination. It was assumed, therefore, that d -mannitol might be used as the source of endogenous respiration and provide energy for the germination.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference10 articles.

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5. O'CONNOR R. J. AND H. HALVORSON. 1960. L-alanine dehydrogenase: the possible initial binding site for L-alanine in aerobic spores. Bacteriol. Proc. p. 66.

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