Emulsifying Properties of Peptides Obtained from the Hydrolyzates of β-Casein

Abstract

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. © 1987, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.