Purification and Some Properties of Pectinesterase from Fruits of a Miniature-Fruited Red Type Tomato.

DOI 1 Citations 22 References Open Access
  • INARI Taeko
    Department of Nutrition and Food Science, Faculty of Home Economics, Gifu Women's University The United Graduate School of Agricultural Science, Gifu University
  • YAMAGUCHI Ryo
    The United Graduate School of Agricultural Science, Gifu University
  • KATO Koji
    The United Graduate School of Agricultural Science, Gifu University
  • TAKEUCHI Tokuo
    Department of Nutrition and Food Science, Faculty of Home Economics, Gifu Women's University

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Description

A pectinesterase (E.C. 3.1.1.11, pectin pectylhydrolase) from the ripening stage of fruits of a miniature-fruited red type tomato (Mini-tomato) was purified 247 fold with yield of 26% by ammonium sulfate fractionation, affinity chromatography, and gel filtration. The molecular weight of the enzyme was found to be 15,000 by gel filtration and SDSPAGE. The optimum activity was at pH 7.0 and at 50°C. The enzyme was stable between pH 6 and 7 and at temperatures below 50°C. The Km value was estimated to be 0.48% for citrus pectin as the substrate. Chelating reagents were the effective inhibitors of the enzyme.

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Details 詳細情報について

  • CRID
    1390001204454485120
  • NII Article ID
    30039678422
    10013007865
  • NII Book ID
    AA11320122
  • DOI
    10.3136/fstr.6.54
  • COI
    1:CAS:528:DC%2BD3cXjtVygtLw%3D
  • ISSN
    18813984
    13446606
    http://id.crossref.org/issn/13446606
  • Text Lang
    en
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
    • OpenAIRE
  • Abstract License Flag
    Disallowed

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