抄録
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 the 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.