Mode of binding of ionic materials to casein micelles

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Abstract
SUMMARY: The proportion of materials which adsorb to casein micelles and accelerate milk coagulation, and remain bound on dilution of the micelle suspension with milk dialysate was determined. This was higher than expected from the postulate that equilibration took place between the solution and many equivalent binding sites on the micelle. This suggests that binding involved either or both hydrophobic interactions and multipoint attachment to charged groups. The location of the additive binding sites in the micelle was investigated using models Na caseinate and hydroxyapatite at pH 6·6. Materials which accelerated coagulation bound to either or both models. Those with the greatest effect on milk coagulation probably bound primarily to the casein rather than to the colloidal calcium phosphate moiety of casein micelles.