Identification of Soluble Proteins and Interaction with Mannan in Mucilage of Dioscorea opposita Thunb. (Chinese Yam Tuber)

  • MYODA Takao
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • MATSUDA Yosuke
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • SUZUKI Tomonori
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • NAKAGAWA Tomoyuki
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • NAGAI Takeshi
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • NAGASHIMA Toshio
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture

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Abstract

In this study, we analyzed the influence of proteins and polysaccharides on the viscous properties of mucilage extracted from Dioscorea opposita Thunb. (Chinese yam). The viscosity of the mucilage was greatly reduced by treatment with protease or mannanase, although not by treatment with cellulase. These results show that the interactions with mannan of certain soluble proteins in the mucilage play an important role in its viscosity, so we identified the major soluble proteins present. Chinese yam mucilage contained at least nine types of major soluble proteins, some of which showed a high percentage of identity with dioscorin, mannan-binding lectin and other functional proteins in the N-terminal amino acid sequence. From these findings, it was suggested that the viscosity of Chinese yam mucilage may be caused by interaction between mannan and soluble proteins such as mannan-binding lectin.

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Details 詳細情報について

  • CRID
    1390001204456754944
  • NII Article ID
    10018441289
  • NII Book ID
    AA11320122
  • DOI
    10.3136/fstr.12.299
  • COI
    1:CAS:528:DC%2BD2sXitVClu7w%3D
  • ISSN
    18813984
    13446606
  • Text Lang
    en
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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