Abstract
Abstract Solubilities of eight genetic types of β-casein (A1A1, A1A2, A1A3, A2A2, A2A3, A1B, A2B, BB) were determined in variable concentrations (5–30 mM) of calcium chloride at pH 6·8 ± 0·02 and 37°C. Solubilities of β-casein types were dependent on initial protein and CaCl2 concentrations. The addition of Ca2+ (final concentrations of 10 and 30 mM) to 0·19% β-casein solutions of different polymorphs resulted in precipitation of the protein to the extent of 7·89–72·11, and 40·53–96·32%, respectively. Compared to other phenotypes, β-caseins A1A1, A1A2 and A1B were the least precipitated upon addition of CaCl2. Least squares analyses of the data indicated that the presence of κ-casein protected β-casein A1A1 the most, and β-casein BB the least against precipitation by addition of 20 mM Ca2+. κ-Casein AB, in most cases, was the best stabilizer of different β-casein types as compared to the BB and AA phenotypes. The stabilizing ability of each κ-casein type was dependent on the type of β-casein present as well as the κ-casein to β-casein ratio in the model systems.
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