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Gel Filtration of Acid Casein and Skimmilk on Sephadex^{1, 2,}

Department of Food Science and Technology, University of California, Davis

ABSTRACT

The calcium caseinate-phosphate complex of milk exists as micelles which vary in size. The molecular weight of the micelles is of the order of millions, and it has been reported that they are excluded from Sephadex G-100 (1, 4). On the other hand, the molecular weights of monomeric casein components are relatively small (2, 8), and they can be expected to penetrate into the gel matrix of both Sephadex G-200 and G-100. The casein components are aggregated at neutral pH and room temperature and they tend to form various complexes with each other. These aggregates and complexes are dissociated into smaller units, probably monomers, under certain conditions such as the presence of urea, extremes of pH, and low temperature (3, 6, 9). Although the behavior of -casein on gel filtration has been reported (5), the fractionation of whole casein on Sephadex has not been studied. Such a study, together with the behavior of a sample of skimmilk on Sephadex gel, is the subject of the present communication.

¹ This investigation was supported by U.S. Public Health Service Research Grant EF-00424 from the Division of Environmental Engineering and Food Protection.

² Presented at the annual meeting of the American Dairy Science Association at Lexington, Kentucky, 1965.