Abstract
This article reviews the latest developments in understanding the mechanisms of heat-induced aggregation of whey proteins, in particular β-lactoglobulin. The influences of the reaction conditions (pH, concentration, temperature, ionic strength) on protein aggregation are briefly described. The aggregation process can be interpreted using reaction schemes consisting of several, complex intermediate states. The aggregates and intermediates are held together via disulphide bridges and non-covalent interactions, mainly hydrophobically driven associations.
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