Work

Emulsifying Properties of Peptides Obtained from the Hydrolyzates ofβ-Casein

Year: 1987

Type: article

Abstract: 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.

Source: Agricultural and Biological Chemistry

DOI: 10.1080/00021369.1987.10867991

Authors: Soo Won Lee, Makoto Shimizu, Shuichi Kaminogawa, Kunio Yamauchi

Institution: The University of Tokyo

Language: English

Topic: Protein Hydrolysis and Bioactive Peptides

Subfield: Food Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2087536717

FWCI: 2.961

Cites: 2

Cited by: 51

Related to: 10