Mechanism of Alanine Hyperproduction by Arthrobacter oxydans HAP-1: Metabolic Shift to Fermentation under Nongrowth Aerobic Conditions

Author:

Hashimoto Shin-ichi1,Katsumata Ryoichi1

Affiliation:

1. Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 3-6-6 Asahi-machi, Machida-shi, Tokyo 194-8533, Japan

Abstract

ABSTRACT Arthrobacter oxydans HAP-1 hyperproduces dl -alanine in a non-growth-associated manner. We found that decreased activities of pyruvate dehydrogenase and of the enzyme catalyzing NADH oxidation in the stationary phase are paralleled by a shift of pyruvate metabolism to alanine synthesis by l -alanine dehydrogenase. We propose that this enzyme functions as an electron sink even under aerobic conditions.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference22 articles.

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3. Calton G. J. The enzymatic preparation of l -alanine Biocatalytic production of amino acids and derivatives. Rozzell J. D. Wagner E. 1992 60 74 John Wiley & Sons Inc. New York N.Y

4. Overproduction of alanine by Arthrobacter strains with glucose-nonrepressible l-alanine dehydrogenase.;Hashimoto S.;Biotechnol. Lett.,1993

5. l-Alanine fermentation by an alanine racemase deficient mutant of the dl-alanine hyperproducing bacterium, Arthrobacter oxydans HAP-1.;Hashimoto S.;J. Ferment. Bioeng.,1998

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