Emulsifying Properties of a Peptide from Peptic Hydrolysates of Soy Glycinin

  • TSUMURA Kazunobu
    New Ingredients Research Institute, Tsukuba R&D Center, Fuji Oil Co., Ltd.
  • KUGIMIYA Wataru
    New Ingredients Research Institute, Tsukuba R&D Center, Fuji Oil Co., Ltd.
  • INOUYE Kuniyo
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

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抄録

Soy glycinin was hydrolyzed by pepsin under controlled conditions. The emulsifying activity of the hydrolysates was found to be higher than that of glycinin. Fractionation of the peptides was performed in order to determine which peptides in the hydrolysates contributed to the enhanced emulsifying activity. A peptide fragment from an acidic subunit of glycinin A1a, corresponding to residues 209-275, was purified and was found to have a higher emulsifying activity at pH 4.0 than that of the original hydrolysate. Based on the hydropathic index, it is expected that the peptide possesses amphiphilic structure.

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詳細情報 詳細情報について

  • CRID
    1390001204455854592
  • NII論文ID
    130000061567
  • NII書誌ID
    AA11320122
  • DOI
    10.3136/fstr.11.46
  • COI
    1:CAS:528:DC%2BD2MXhtVClu73L
  • ISSN
    18813984
    13446606
  • 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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