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 <I>Bombyx mori</I> by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward <I>N</I>-acetylchitopentaose (GlcNAc<SUB>5</SUB>) and 10 toward glycolchitin. The optimum temperature was 60 °C toward GlcNAc<SUB>5</SUB> 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 <I>N</I>-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 <I>N</I>-acetylchitooligosaccharides, suggesting, together with the <I>N</I>-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases.

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  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 70(1), 252-262, 2006-01-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018535676
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    7791791
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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