Purification and Characterization of a Novel Isozyme of Chitinase from<i>Bombyx mori</i>

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  • KABIR Khondkar Ehteshamul
    Department of Biological Science, Faculty of Agriculture, Yamaguchi University
  • HIROWATARI Daizo
    Department of Biological Science, Faculty of Agriculture, Yamaguchi University
  • WATANABE Katsuhiro
    Department of Biological Science, Faculty of Agriculture, Yamaguchi University
  • KOGA Daizo
    Department of Biological Science, Faculty of Agriculture, Yamaguchi University

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  • Purification and Characterization of a Novel Isozyme of Chitinase from Bombyx mori

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75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward N-acetylchitopentaose (GlcNAc5) and 10 toward glycolchitin. The optimum temperature was 60 °C toward GlcNAc5 and 25 °C toward glycolchitn. The enzyme was stable at pH 7–10 and below 40 °C. Kinetic analysis and reaction-pattern analysis using glycolchitin and N-acetylchitooligosacchraides as substrates indicated that 75-kDa chitinase is an endo- or random-type hydrolytic enzyme to produce the β anomeric product and that it prefers the longer N-acetylchitooligosaccharides, suggesting, together with the N-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases.

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