Further observations on the size, shape, and hydration of casein micelles from novel analytical ultracentrifuge and capillary viscometry approaches.

The size, shape, and hydration of casein micelles were estimated using a combination of sedimentation velocity (time-derivative analysis) in the analytical ultracentrifuge and capillary viscometry applied to skimmed milk. On the basis of sedimentation time-derivative and Wales-van Holde analyses the casein micelles appear as large spherical molecules of s0T,b = 845S, Mw approximately 2.8 x 10(8), hydrodynamic radius approximately 77.8 nm, and ks/[eta] = 1.6. The molecular hydration (i.e., the extent of chemically bound and physically entrained solvent) was calculated to be 3.4 g/g. These results appear to be in good agreement with comparable results from electron microscopy and dynamic light scattering.