Casein: Micellar Structure (Dual-Binding Model)

This article traces the genesis and development of the dual-binding model of the casein micelle. It summarizes the pertinent physicochemical properties of the individual caseins, concentrating on those which govern their interactions and self-assembly. Based on a polymerization approach, the two binding pathways are through the serine phosphate clusters of the calcium-sensitive caseins across mineral calcium phosphate nanoclusters, and hydrophobic interactions between groupings of nonpolar residues in the hydrophobic-rich regions of the proteins. The dual-binding model of the micelle plausibly explains the structure of the micelle, its stability and integrity, but more importantly offers a route to understanding the functional behavior of the casein micelle in situations of technological importance.