Emulsifying Properties of Peptides Obtained from the Hydrolyzates ofβ-Casein
- 1 January 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 51 (1) , 161-166
- https://doi.org/10.1080/00021369.1987.10867991
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 (f 193 — 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.This publication has 1 reference indexed in Scilit:
- The Influence of Peptide Chain Length on Taste and Functional Properties of Enzymatically Modified Soy ProteinPublished by American Chemical Society (ACS) ,1979