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

G. A. Morris, T. J. Foster, S. E. Harding

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

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 s0 T,b = 845S, Mw ∼ 2.8 × 108, hydrodynamic radius ∼77.8 nm, and ks/[η] = 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.

Original languageEnglish
Pages (from-to)764-767
Number of pages4
JournalBiomacromolecules
Volume1
Issue number4
DOIs
Publication statusPublished - 11 Oct 2000
Externally publishedYes

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