A Novel Glucanotransferase from a Bacillus circulans Strain That Produces a Cyclomaltopentaose Cyclized by an α-1,6-Linkage

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A novel glucanotransferase, involved in the synthesis of a cyclomaltopentaose cyclized by an α-1,6-linkage [ICG5; <I>cyclo</I>-{→6)-α-<small>D</small>-Glc<I>p</I>-(1→4)-α-<small>D</small>-Glc<I>p</I>-(1→4)-α-<small>D</small>-Glc<I>p</I>-(1→4)-α-<small>D</small>-Glc<I>p</I>-(1→4)-α-<small>D</small>-Glc<I>p</I>-(1→}], from starch, was purified to homogeneity from the culture supernatant of <I>Bacillus circulans</I> AM7. The pI was estimated to be 7.5. The molecular mass of the enzyme was estimated to be 184 kDa by gel filtration and 106 kDa by SDS–PAGE. These results suggest that the enzyme forms a dimer structure. It was most active at pH 4.5 to 8.0 at 50 °C, and stable from pH 4.5 to 9.0 at up to 35 °C. The addition of 1 m<small>M</small> Ca<SUP>2+</SUP> enhanced the thermal stability of the enzyme up to 40 °C. It acted on maltooligosaccharides that have degrees of polymerization of 3 or more, amylose, and soluble starch, to produce ICG5 by an intramolecular α-1,6-glycosyl transfer reaction. It also catalyzed the transfer of part of a linear oligosaccharide to another oligosaccharide by an intermolecular α-1,4-glycosyl transfer reaction. Thus the ICG5-forming enzyme was found to be a novel glucanotransferase. We propose isocyclomaltooligosaccharide glucanotransferase (IGTase) as the trivial name of this enzyme.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(8), 1954-1960, 2006-08-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018528309
  • 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
    8040481
  • 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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