Purification, Characterization, and Gene Sequencing of a Catalase from an Alkali- and Halo-tolerant Bacterium,<i>Halomonas</i>sp. SK1

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  • PHUCHAROEN Krisana
    <i>Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University</i>
  • HOSHINO Kiichi
    <i>Morin Chemical Industrial Co., Ltd.</i>
  • TAKENAKA Yuuki
    <i>Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University</i>
  • SHINOZAWA Takao
    <i>Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University</i>

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  • Purification, Characterization, and Gene Sequencing of a Catalase from an Alkali- and Halo-tolerant Bacterium, Halomonas sp. SK1.

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  An alkali- and halo-tolerant bacterium with high catalase activity was isolated and identified as a new species of the genus Halomonas. Its catalase (HktA) was simply purified by two steps of liquid chromatography. A 71.4% yield of the catalase was obtained with 97% purity on SDS-PAGE. The specific activity of HktA (57,900 U/mg protein) was two times higher than that of bovine liver catalase. The purified enzyme is inhibited by KCN, NH2OH, NaN3, and 3-amino-1,2,4-triazole, active at pH 5.0-11.0, thermo-sensitive, and KCl- tolerant. HktA is suggested to be a typical catalase, a homotetrameric protein containing heme groups in the active sites. The nucleotide sequence of the catalase gene (hktA) comprises 1,530 bp, encoding a protein of 509 amino acid residues. The deduced amino acid sequence of the hktA shares 99% identity with that of Vibrio rumoiensis S-1T.<br>

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