Emulsifying Properties of a Mixture of Peptides Derived from the Enzymatic Hydrolyzates of Bovine Caseins
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概要
- 論文の詳細を見る
β-CN(f 193-209), a hydrophobic peptide of 17 residues obtained from the chymosin hydrolyzate of β-casein, had little emulsifying activity (EA) at a neutral pH. When mixed with a hydrophilic glycomacropeptide (GMP) derived from κ-casein however, the EA of β-CN(f193-209) increased greatly. The mixing ratio of the peptides affected the EA as well as the adsorption of the peptides to oil droplets. Scanning electron microscopy indicated that the peptide film surrounding the emulsified oil droplets was thick and rough compared to the protein film. An amphipathic structure formed by some interaction between the hydrophilic GMP and the hydrophobic β-CN(f193-209) might contribute to the formation of the thick peptide film and stabilize the emulsified oil.
- 社団法人 日本農芸化学会の論文
著者
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Yamauchi Kunio
Department Of Agricultural Chemistry The University Of Tokyo
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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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LEE Soo
Department of Agricultural Chemistry, The University of Tokyo
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