Ion-exchange fast protein liquid chromatography: optimization of the purification of caseins using a non-denaturing detergent

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Abstract
The separation of bovine milk proteins by fast protein liquid chromatography has been studied by ion-exchange chromatography on Mono S and Mono Q columns. The use of a non-ionic detergent, octyl-glucoside, made possible the separation of the four major casein components (αs1, αs2, β and κ) as well as minor caseins on the Mono S column using urea-containing buffers at pH 3·5. There was, however, considerable overlap between the αs1 and αs2-casein peaks. A good resolution was obtained with a low concentration of urea (3·5 M) and detergent (0·1%). These conditions allowed the separation of casein components in their native state in less than 50 min. The purity of isolated κ-casein was further improved by a second separation on a Mono Q column.