Association of Caseins and their Possible Relation to Structure of the Casein Micelle

Abstract

The association properties of the main casein components are reviewed and a model of the casein micelle developed. Electrical repulsion between the micelles is weak, though essential for stabilization. Likewise long-range Vanderwaals forces between the micelles must be weak. The model which emerges from these considerations shows a loose entanglement of ag- and [beta]-casein molecules held together by Ca-bridges and hydrophobic bonds. This [alpha]s-[beta] complex is protected from coagulation with Ca-ions by a superficial layer of [kappa]-casein. Arguments are given for the location of [kappa]-casein and for the presence of apolar patches on the micelle surface.