Heterologous Expression and Functional Characterization of a Novel Chitinase from the Chitinolytic Bacterium Chitiniphilus shinanonensis

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<I>Chitiniphilus shinanonensis</I> strain SAY3<SUP>T</SUP> is a chitinolytic bacterium isolated from moat water of Ueda Castle in Nagano Prefecture, Japan. Fifteen genes encoding putative chitinolytic enzymes (<I>chiA-chiO</I>) have been isolated from this bacterium. Five of these constitute a single operon (<I>chiCDEFG</I>). The open reading frames of <I>chiC</I>, <I>chiD</I>, <I>chiE</I>, and <I>chiG</I> show sequence similarity to family 18 chitinases, while <I>chiF</I> encodes a polypeptide with two chitin-binding domains but no catalytic domain. Each of the five genes was successfully expressed in <I>Escherichia coli</I>, and the resulting recombinant proteins were characterized. Four of the recombinant proteins (ChiC, ChiD, ChiE, and ChiG) exhibited endo-type chitinase activity toward chitinous substrates, while ChiF showed no chitinolytic activity. In contrast to most endo-type chitinases, which mainly produce a dimer of <I>N</I>-acetyl-<small>D</small>-glucosamine (GlcNAc) as final product, ChiG completely split the GlcNAc dimer into GlcNAc monomers, indicating that it is a novel chitinase.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 76(3), 517-522, 2012-03-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10030750647
  • 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
    023553798
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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