Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5541119 | International Dairy Journal | 2017 | 11 Pages |
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 (â¼0.5 g gâ1 protein), water associated with the κ-casein brush (â¼1.0 g gâ1 protein) and water entrapped in the casein micelles (â¼1.8 g gâ1 protein), yielding a total micellar hydration of â¼3.3 g gâ1 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.
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Authors
Thom Huppertz, Inge Gazi, Hannemieke Luyten, Hans Nieuwenhuijse, Arno Alting, Erix Schokker,