Radiolabelling Study of the Heat‐induced Interactions Between α‐Lactalbumin, β‐Lactoglubulin and K‐Casein in Milk and in Buffer Solutions

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Abstract
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.