Gene Cloning, Purification and Characterization of Thermostable Alanine Dehydrogenase of Bacillus stearothermophilus

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概要

• 論文の詳細を見る

• The alanine dehydrogenase(L-alanine : NAD^+ oxidoreductase, deaminating, EC 1.4.1.1)gene of Bacillus stearothermophilus IFO12550 was cloned and expressed in Escherichia coli C600 with a recombinant plasmid, pICD301,which was constructed from pBR322 and the alanine dehydrogenase gene derived from B. stearother-mophilus. The enzyme overproduced in the clone was purified about 30 fold to homogeneity by heat treatment and two subsequent steps with a yield of 46%. The enzyme of E. coli-pICD301 was immunochemically identical with that of B. stearothermophilus. The enzyme has a molecular weight of about 240,000 and consists of six subunits identical in molecular weight(40,000). The enzyme is not inactivated by heat treatment : at pH 7.2 and 75℃ for 30min; at 55℃ and various pHs between 6.0 and 11.5 for 10 min. The enxymological properties are very similar to those of the mesophilic B. sphaericus enzyme(Ohshima, T. and Soda, K., Eur. J. Biochem., 100,29-39,1979)except for thermostability.

• 社団法人日本生物工学会の論文
• 1990-03-25

著者

• Esaki Nobuyoshi

  Kyoto Univ.

• Esaki Nobuyoshi

  Nstitute For Chemical Research Kyoto University

• Esaki Nobuyoshi

  Institute for Chemical Research, Kyoto University

• SODA Kenji

  Institute for Chemical Research, Kyoto University

• Soda Kenji

  Institute For Chemical Resarch Kyoto University

• Tanaka H

  Department Of Bioresources Chemistry Faculty Of Agriculture Okayama University

• Esaki Nobuyoshi

  Institute For Chemical Resarch Kyoto University

• Tanaka Hidehiko

  Faculty Of Engineering Department Of Information Engineering The University Of Tokyo

• Soda K

  Department Of Biotechnology Kansai University

• Nagasaki S

  Department Of Bioresources Science Kochi University

• SAKAMOTO YONEKAZU

  (Present address)

• NAGATA SHINNJI

  Department of Agricultural Chemistry, Kochi University

• Sakamoto Y

  Osaka Univ. Osaka Jpn

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