Isolation, enzyme production and characterization of d-aspartate oxidase from Fusarium sacchari var. elongatum Y-105

Mamoru Wakayama, Sadatoshi Nakashima, Kenji Sakai, Mitsuaki Moriguchi

研究成果: Contribution to journalArticle

13 引用 (Scopus)

抜粋

A microorganism that produces d-aspartate-oxidizing enzyme by induction was isolated from soil, and identified as Fusarium sacchari var. elongatum Y-105. The enzyme catalyzed the oxidative deamination of d-aspartate (d-Asp) and produced oxaloacetate, ammonia, and hydrogen peroxide, stoichiometrically. The enzyme is designated "d-Asp oxidase" (EC 1.4.3.1). In addition to d-Asp, the enzyme oxidized d-glutamate (d-Glu) and N-methyl-d-aspartate (NMDA). N-Acetyl-d-Asp and other d- or l-amino acids, however, were inert as substrates. The optimum pH and temperature were 7.5 and 40°C, respectively. The enzyme was stable at pH 9.0 and temperature of 50°C, respectively. The enzyme activity was not inhibited by sodium benzoate which is a specific inhibitor of d-amino acid oxidase from mammals. The enzyme activity was also not affected by carboxylates such as meso- or d-tartarate, citrate, and fumarate which inhibit d-Asp oxidase from rabbits.

元の言語英語
ページ(範囲)377-379
ページ数3
ジャーナルJournal of Fermentation and Bioengineering
78
発行部数5
DOI
出版物ステータス出版済み - 1994
外部発表Yes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology

フィンガープリント Isolation, enzyme production and characterization of d-aspartate oxidase from Fusarium sacchari var. elongatum Y-105' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用