Effects of partial denaturation on surface properties of ovalbumin and lysozyme.

• KATO Akio

  Department of Agricultural Chemistry, Yamaguchi University

• TSUTSUI Noriko

  Department of Agricultural Chemistry, Yamaguchi University

• MATSUDOMI Naotoshi

  Department of Agricultural Chemistry, Yamaguchi University

• KOBAYASHI Kunihiko

  Department of Agricultural Chemistry, Yamaguchi University

• NAKAI Shuryo

  Department of Food Science, University of British Columbia

抄録

The effects of partial denaturation were investigated on the surface properties of ovalbumin and lysozyme. The surface tension of proteins decreased greatly as denaturation proceeded. The emulsifying and foaming properties of the proteins were remarkably improved by heat denaturation without coagulation. The emulsifying properties of the proteins increased with denaturation, and correlated linearly with surface hydrophobicity. On the other hand, the protein foaming properties incresed with denaturation, correlating curvilinearly with surface hydrophobicity. The foaming power and foam stability of SDS-bound ovalbumin did not improve as much with those of heatdenatured ovalbumin, although surface hydrophobicity increased to the same extent as by heat denaturation. The relationship between the conformation and functionality of proteins is discussed.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 45 (12), 2755-2760, 1981

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390282681441039872
• NII論文ID: 130000028674
• DOI: 10.1271/bbb1961.45.2755
• COI: 1:CAS:528:DyaL38Xksl2itQ%3D%3D
• ISSN: 18811280
• ISSN: 00021369
• ISSN: http://id.crossref.org/issn/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