Isolation and characterization of salt-tolerant glutaminases from marine Micrococcus luteus K-3

Mitsuaki Moriguchi, Kenji Sakai, Ryoji Tateyama, Yoichi Furuta, Mamoru Wakayama

研究成果: ジャーナルへの寄稿学術誌査読

67 被引用数 (Scopus)

抄録

Marine Micrococcus luteus K-3 constitutively produced two salt-tolerant glutaminases, designated glutaminase I and II. Glutaminase I was homogeneously purified about approximately, 1620-fold with a 4% yield, and was a dimer with a molecular weight of about 86,000. Glutaminase II was partially purified about 190-fold with a 0.04% yield. The molecular weight of glutaminase II was also 86,000. Maximum activity of glutaminase I was observed at pH 8.0, 50°C and 8-16% NaCl. The optimal pH and temperature of glutaminase II were 8.5 and 50°C. The activity of glutaminase II was not affected by the presence of 8 to 16% NaCl. The presence of 10% NaCl enhanced thermal stability of glutaminase I. Both enzymes catalyzed the hydrolysis of l-glutamine, but not its hydroxylaminolysis. The Km values for l-glutamine were 4.4 (glutaminase I) and 6.5 mM (glutaminase II). Neither of the glutaminases were activated by the addition of 2 mM phosphate or 2 mM sulfate. p-Chloromercuribenzoate (0.01 mM) significantly inhibited glutaminase I, but not glutaminase II. The conserved sequences LA**V and V**GGT*A were observed in the N-terminal amino acid sequences of glutaminase I, similar to that for other glutaminases.

本文言語英語
ページ(範囲)621-625
ページ数5
ジャーナルJournal of Fermentation and Bioengineering
77
6
DOI
出版ステータス出版済み - 1994
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 応用微生物学とバイオテクノロジー

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