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Journal of Dairy Science Vol. 74 No. 8 2403-2409
© 1991 by American Dairy Science Association ®
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Separation of Major Casein Fractions Using Cation-Exchange Fast Protein Liquid Chromatography

C. M. Hollar 1, A.J.R. Law 1, D. G. Dalgleish 1, and R. J. Brown 1

1 Western Dairy Foods Research Center, Nutrition and Food Sciences Department, Utah State University, Logan 84322-8700

Whole casein was separated into ß-casein, kappa-casein, alphas1-casein, and alphas2-casein fractions using cation-exchange fast protein liquid chromatography. The gamma-caseins and several unidentified peaks were also separated. A urea-acetate buffer at pH 5 and a NaCl gradient from 0 to .26 M were used to separate the casein fractions. Several gamma-caseins and unidentified fractions eluted first, followed by three ß-casein peaks, several gamma-casein and unidentified peaks, kappa-casein, alphas1-casein, and alphas2-casein. Some gamma-caseins eluted with ß-casein. The four major caseins, which accounted for over 90% of the whole casein fractions, were accounted for with this method, and the calculated compositions correlated well with values obtained using anion-exchange fast protein liquid chromatography at pH 7.

Key Words: casein separation • fast protein liquid chromatography

Submitted on January 14, 1991
Accepted on March 18, 1991




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Copyright © 1991 by the American Dairy Science Association ®.