Hydration of casein micelles and caseinates: Implications for casein micelle structure

Abstract

By studying the hydration of casein micelles using a variety of techniques, a distinction could be made between water that appeared bound by the protein (∼0.5 g g−1 protein), water associated with the κ-casein brush (∼1.0 g g−1 protein) and water entrapped in the casein micelles (∼1.8 g g−1 protein), yielding a total micellar hydration of ∼3.3 g g−1 protein, in line with casein micelle voluminosity derived from intrinsic viscosity measurements. For caseinate particles, however, the main contributor to intrinsic viscosity was not protein hydration but the non-spherical particle shape. These non-spherical particles in caseinate are likely to be naturally present as primary casein particles (PCP) in casein micelles. PCP could be used to build casein micelles by controlled introduction of micellar salts. Based on the findings of this study, casein micelles could be described as a porous network of non-spherical PCP linked by calcium phosphate nanoclusters.