Targeted processing of casein micelles (CM) requires a basic understanding of their molecular structure as well as their interactions with each other and with other components. In this study, angle- and concentration-dependent static and dynamic light scattering is applied to investigate changes in the molecular weight, size, and intermolecular interactions of CM after the addition of \textgreek{b}-lactoglobulin (\textgreek{b}-Lg) and calcium chloride. Addition of a surplus of \textgreek{b}-Lg impairs the colloidal stability of CM. In the presence of 0.5wt{%} \textgreek{b}-Lg and natural calcium chloride concentrations (10mM), the molecular weight of CM is reduced and the radius of gyration is increased. Both changes can be explained by the release of \textgreek{a}S2-casein and \textgreek{k}-casein, which were determined in higher concentration free in solution by High performance liquid chromatography. In contrast, the structure of casein micelles is not altered by the presence of \textgreek{b}-Lg at elevated calcium chloride concentrations. The repulsive forces between the CM show no significant dependence on \textgreek{b}-Lg for all calcium chloride concentrations tested.     «

Targeted processing of casein micelles (CM) requires a basic understanding of their molecular structure as well as their interactions with each other and with other components. In this study, angle- and concentration-dependent static and dynamic light scattering is applied to investigate changes in the molecular weight, size, and intermolecular interactions of CM after the addition of \textgreek{b}-lactoglobulin (\textgreek{b}-Lg) and calcium chloride. Addition of a surplus of \textgreek{b}-Lg i...     »