The structure of casein micelles between pH 5·5 and 6·7 as determined by light-scattering, electron microscopy and voluminosity experiments

Summary Hydrodynamic radii from inelastic light-scattering experiments and radii of gyration from Zimm plots give an indication of the change of average casein micelle size when the pH is changed. Combination of the results of both types of measurements gives information on changes in the micelle protein matrix, i.e. changes in the voluminosity. The voluminosity was also determined by the pellet method and by electron microscopy which also provided comparative data on size parameters.