ネオプルラナーゼの発見とα-アミラーゼファミリーの提案 Discovery of Neopullulanase and Proposal of α-Amylase Family

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We found a new enzyme, neopullulanase, and proved that the enzyme catalyzes both hydrolysis and transglycosylation at α-(1→4) - and α-(1→6)-glucosidic linkages by one active center. A series of experimental results using neopullulanase indicated that the four reactions described above could be catalyzed in the same mechanism. On the basis of the common catalytic mechanisms and the structural similarities among the enzymes which catalyze the four reactions, we proposed a general concept for an enzyme family, α-amylase family. The substrate specificity and the transglycosylation activity of neopullulanase were altered by site-directed mutagenesis on the basis of information from a threedimesionalstructure predicted by computer-aided molecular modeling. From the standpoint of industrial application, we developed a new way of producing isomalto-oligosaccharide syrup using the transglycosylation reaction of neopullulanase. We also expanded the concept of α-amylase family into branching enzymes and constructed chimeric enzymes of starch branching enzymes I and II isof orms from maize endosperm. The results indicated that the N- and C-terminuses may be involved in determining substrate preference, catalytic capacity, and chain length transfer.

収録刊行物

  • 応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience

    応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience 45(1), 63-70, 1998-03-31

    The Japanese Society of Applied Glycoscience

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各種コード

  • NII論文ID(NAID)
    10008257751
  • NII書誌ID(NCID)
    AN10453916
  • 本文言語コード
    JPN
  • 資料種別
    REV
  • ISSN
    13403494
  • NDL 記事登録ID
    4447479
  • NDL 雑誌分類
    ZP24(科学技術--化学・化学工業--糖・澱粉)
  • NDL 請求記号
    Z17-15
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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