Emulsifying Properties of Peptides Obtained from the Hydrolyzates of β-Casein(Food & Nutrition)
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概要
- 論文の詳細を見る
A hydrophobic peptide of 17 residues, β-CN (f193〜209), and a hydrophilic peptide of 25 residues, β-CN (f1〜25), were isolated from enzyme hydrolyzates of bovine β-casein. The emulsifying activity (EA) of both peptides was low at a neutral pH. In hte acidic or alkaline condition, however, β-CN (f193〜209) showed high EA values. β-CN (f1〜25) also showed high EA values at acidic pHs. These peptides are shown to be more surface active at pH 3 than at pH 7.
- 社団法人日本農芸化学会の論文
- 1987-01-23
著者
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LEE Soo
Department of Environmental Engineering, Sun Moon University
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SHIMIZU Makoto
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The U
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YAMAUCHI Kunio
Department of Agricultural Chemistry, The University of Tokyo
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KAMINOGAWA Shuichi
Department of Food Science and Technology, College of Bioresource Sciences, Nihon University
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Lee Soo
Department Of Chemistry (bk21) And Research Institute Of Natural Science Gyeongsang National Univers
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Yamauchi K
Univ. Tokyo Tokyo Jpn
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Yamauchi Kunio
Department Of Agricultural Chemistry The University Of Tokyo
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Kaminogawa S
Dep. Of Food Sci. And Technol. Nihon Univ.
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Shimizu M
Department Of Physics Faculty Of Science Tohoku University
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Kaminogawa Shuichi
Department Of Agricultural Chemistry Faculty Of Engineering The University Of Tokyo
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Shimizu Makoto
Department Of Agricultural Chemistry Faculty Of Engineering The University Of Tokyo
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Lee Soo
Department Of Agricultural Chemistry The University Of Tokyo
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