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Radiolabelling Study of the Heat‐induced Interactions Between α‐Lactalbumin, β‐Lactoglubulin and K‐Casein in Milk and in Buffer Solutions
Author(s) -
NOH BONGSOO,
RICHARDSON TOM,
CREAMER LAWRENCE K.
Publication year - 1989
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1989.tb07906.x
Subject(s) - lactalbumin , casein , chemistry , whey protein , micelle , beta lactoglobulin , chromatography , disulfide bond , alpha lactalbumin , nucleation , food science , biochemistry , organic chemistry , aqueous solution
Radiolabeled α‐lactalbumin, β‐lactoglobulin and κ‐casein were added to milk prior to heating it at 95°C for up to 20 min. The distribution of these proteins between the micellar and serum phases and between various sized aggregates were determined chromatographically. The results from these and other supplementary experiments were consistent with a model of whey proteins denaturing in milk during heat treatment and using κ‐casein as a nucleation site for the formation of heat‐induced complexes involving disulfide bonding. These heat‐induced complexes, like κ‐casein itself, remained associated with the external surface of the casein micelle and continued to enlarge with additional heat treatment.