A hydrophobic peptide of 17 residues, /?-CN (fl93~209), and a hydrophilic peptide of 25 residues, /?-CN (fl ~25), were isolated from enzyme hydrolyzates of bovine /?-casein.The emulsifying activity (EA) of both peptides was low at a neutral pH.In the acidic or alkaline condition, however, jft-CN (fl93~2Q9) showed high EA values.jft-CN (fl ~25) also showed high EAvalues at acidic pHs.These peptides are shown to be more surface active at pH 3 than at pH 7.
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LEE et al. (1987) studied this question.