Purification and Properties of Isocitrate Lyase from Candida brassicae E-17

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概要

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• Isocitrate lyase (EC 4.1.3.1) was purified from acetate-grown cells of Candida brassicae E-17,by ammonium sulfate fractionation and DEAE-cellulose and Sephadex G-200 gel filtration column chromatographies. The purified enzyme was electrophoretically homogeneous. THe molecular weight of this enzyme was 290,000 by gel filtration, and it was composed of four identical subunits whose molecular weights were 71,000 each. The pH and temperature optima were 6.8 and 37℃, respectively. The enzyme was stabel from pH 6.0 to 7.0. The enzyme was activated by Mg^<2+> and the maximum activity was obtained with a concentration of 8 mM Mg^<2+>. The enzyme was also activated by Mn^<2+> and Ba^<2+>. The activity of this enzyme was stimulated by reducing agents. The K_m values for DL-isocitrate were 1.5 mM in sodium phosphate buffer and 0.62 mM in imidazole-HCl buffer.

• 公益社団法人日本生物工学会の論文
• 1989-03-25

著者

• NAKAMURA Kazuo

  Department of Management and Information Systems Science Nagaoka University of Technology

• Amano Yoshifumi

  Department Of Applied Chemistry And Biotechnology Faculty Of Engineering Yamanashi University

• NAKADATE MASAO

  Tama Biochemical Co., Ltd.,

• KAGAMI MOTOO

  Department of Fermentation Technology, Faculty of Engineering, Yamanashi, University

• Nakadate Masao

  Tama Biochemical Co. Ltd.

• Kagami Motoo

  Department Of Fermentation Technology Faculty Of Engineering Yamanashi University

• Nakamura Kazuo

  Department Of Biochemistry Kitasato University School Of Medicine

• AMANO YOSHIFUMI

  Department of Fermentation Technology, Faculty of Engineering, Yamanashi, University

• Nakamura Kazuo

  Department of Applied Chemistry and Biotechnology, Faculty of Engineering, Yamanashi University

• NAKAMURA KAZUO

  Department of Fermentation Technology, Faculty of Engineering, Yamanashi, University

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