Purification, Characterization, and Subsite Affinities of Thermoactinomyces vulgaris R-47 Maltooligosaccharide-metabolizing Enzyme Homologous to Glucoamylases

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A maltooligosaccharide-metabolizing enzyme from <I>Thermoactinomyces vulgaris</I> R-47 (TGA) homologous to glucoamylases does not degrade starch efficiently unlike most glucoamylases such as fungal glucoamylases (Uotsu-Tomita <I>et al.</I>, <I>Appl. Microbiol. Biotechnol.</I>, <B>56</B>, 465–473 (2001)). In this study, we purified and characterized TGA, and determined the subsite affinities of the enzyme. The optimal pH and temperature of the enzyme are 6.8 and 60°C, respectively. Activity assays with 0.4% substrate showed that TGA was most active against maltotriose, but did not prefer soluble starch. Kinetic analysis using maltooligosaccharides ranging from maltose to maltoheptaose revealed that TGA has high catalytic efficiency for maltotriose and maltose. Based on the kinetics, subsite affinities were determined. The <I>A</I><SUB>1</SUB>+<I>A</I><SUB>2</SUB> value of this enzyme was highly positive whereas <I>A</I><SUB>4</SUB>–<I>A</I><SUB>6</SUB> values were negative and little affinity was detected at subsites 3 and 7. Thus, the subsite structure of TGA is different from that of any other GA. The results indicate that TGA is a metabolizing enzyme specific for small maltooligosaccharides.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 68(2), 413-420, 2004-02-23

    公益社団法人 日本農芸化学会

参考文献:  33件中 1-33件 を表示

被引用文献:  3件中 1-3件 を表示

各種コード

  • NII論文ID(NAID)
    10013142121
  • 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
    6868502
  • 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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