プルラン分解酵素の構造と機能に関する研究 Study on Structure and Function of Pullulan-Hydrolyzing Enzymes

この論文にアクセスする

この論文をさがす

著者

    • 殿塚 隆史 TONOZUKA Takashi
    • 東京農工大学農学部応用生物科学科 Department of Applied Biological Science, Tokyo University of Agriculture and Technology
    • 坂野 好幸 SAKANO Yoshiyuki
    • 東京農工大学農学部応用生物科学科 Department of Applied Biological Science, Tokyo University of Agriculture and Technology

抄録

α-Amylases from Thermoactinomyces vulgaris R-47 (TVA I and TVA II) hydrolyze pullulan to produce panose, and isopullulanase (IPU) from Aspeygillus niger ATCC 9642 hydrolyzes Pullulan to produce isopanose. The structure/function relationships of these pullulan-hydrolyzing enzymes were studied. The crystal structure of TVA II has been determined. TVA II is composed of domain A/B, which has a (β/α) <SUB>8</SUB> barrel structure with a small component called domain B; domain C, which contains the C-terminus; and domain N, which contains the N-terminus. Although the role of domain N for the enzyme activity has been unclear, it is unique in the structures of the α-amylase family. We modified some amino acid residues in region II, one of the four regions conserved in α-amylase family enzymes, of the TVA I by means of site-directed mutagenesis. The action pattern of the mutated enzyme for pullulan was greatly altered and it produced maltotriose from pullulan. The ipuA gene encoding IPU has been isolated. Although IPU does not hydrolyze dextran, IPU showed a high amino acid sequence similarity with dextranases. The ipuA gene was expressed in Aspeygillus oryzae, and the substrate properties of the recombinant IPU were identical with those of the native enzyme.

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 46(2), 179-186, 1999-06-30

    The Japanese Society of Applied Glycoscience

参考文献:  30件中 1-30件 を表示

各種コード

  • NII論文ID(NAID)
    10008258988
  • 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
    4785912
  • 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 
ページトップへ