Changes in the Emulsifying and Foaming Properties of Proteins during Heat Denaturation
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概要
- 論文の詳細を見る
Changes in the emulsifying and foaming properties of ovalbumin, 7S globulin, κ-casein, β-lactoglobulin and bovine serum albumin were followed during heat denaturation, and these surface properties were correlated with the corresponding surface hydrophobicity, in order to investigate the role of surface hydrophobicity in the surface properties of proteins. The surface hydrophobicity of ovalbumin, 7S globulin and κ-casein increased with heat denaturation, while that of β-lactoglobulin and bovine serum albumin decreased. The emulsifying activity and emulsion stability of proteins correlated linearly with surface hydrophobicity, although protein structure changed greatly during heat denaturation. On the other hand, the foaming power of proteins correlated curvilinearly with surface hydrophobicity during heat denaturation. No significant correlation was observed between the foam stability and the surface hydrophobicity of proteins. On the basis of these results, the relationships between the surface properties and the structure of proteins are discussed.
- 社団法人 日本農芸化学会の論文
著者
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Kato A
Teijin Ltd. Tokyo Jpn
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KOBAYASHI Kunihiko
Department of Pediatrics, Hokkaido University Graduate School of Medicine
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MATSUDOMI Naotoshi
Department of Agricultural Chemistry, Yamaguchi University
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KATO Akio
Department of Agricultural Chemistry, Yamaguchi University
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OSAKO Yukiko
Department of Agricultural Chemistry, Yamaguchi University
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Matsudomi Naotoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Yamaguchi University
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Kato Akio
Department Of Agricultural Chemistry Faculty Of Agriclture Yamaguchi University
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Kobayashi Kunihiko
Department Of Agricultural Chemistry Faculty Of Agriclture Yamaguchi University
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