Polymorphism of acid and neutral .ALPHA.-glucosidases in banana pulp:Changes in apparent pIs and affinity to Con A of the enzymes during ripening.

  • KONISHI Yôtarô
    Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
  • KITAZATO Sachiko
    Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
  • ASANO Ryôko
    Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
  • NAKATANI Nobuji
    Department of Food and Nutrition, Faculty of Science of Living, Osaka City University

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We observed the presence of acid and neutral α-glucosidases with optimum pHs of 4.5 and 6.5, respectively, and their multiple forms in banana pulp. By chromatofocusing analysis, each α-glucosidase from preclimacteric bananas was found to be of pI > 7.4, which disappeared upon ripening, although another form with pI 5 as a major component appeared instead. It is unknown whether this phenomenon is due to protein de novo synthesis and/or post-translational modifications of the enzyme. A large amount of acid α-glucosidase from preclimacteric bananas was shown to be a glycoprotein that bound to a Con A-Sepharose column. While this type of enzyme decreased during ripening, it remained a possibility that sugar components of the enzyme might be processed during ripening. The neutral α-glucosidase had no affinity to the column through ripening. These results provide preliminary information on the mechanism of appearance of α-glucosidase multiforms as well as on a useful strategy for purification of acid and neutral α-glucosidases from banana pulp at various stages of ripening.

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詳細情報 詳細情報について

  • CRID
    1390282681437171840
  • NII論文ID
    110006325492
  • NII書誌ID
    AA00515312
  • DOI
    10.1271/bbb1961.55.1089
  • COI
    1:CAS:528:DyaK3MXkt1Kjurw%3D
  • ISSN
    18811280
    00021369
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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