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Chromatography of Milk Proteins on Anion-Exchange Cellulose¹

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

ABSTRACT

A rapid and highly reproducible method of fractionating milk proteins on anion exchange cellulose (DEAE) is described. Gradients of NaCl concentration were employed for elution in phosphate buffer between pH 7.0 and pH 6.6. Separation of the whey protein fraction from the casein fraction by DEAE cellulose chromatography was complete and clear-cut, without overlapping peaks. Whey protein components were eluted in the range of 0 to 0.2 M NaCl. Casein components began to emerge from the column when the concentration of NaCl in the eluting buffer exceeded 0.2 M. Ten, and possibly 11, chromatographic components were obtained from the casein fraction, and at least eight from the whey fraction.

The method can be used for identifying components in a mixture of proteins, as was illustrated by chromatographic identification of ß-lactoglobulins. By chromatographing purified preparations of -lactalbumin, -casein, ß-casein, -casein, and lactoglobulin their positions on the chromatogram of dialyzed skimmilk were identified. The resolving power obtained was higher than with conventional electrophoresis and, furthermore, it appears to be superior to other methods in establishing the kind and extent of contamination of a given preparation with other protein components. The method allows isolation of protein components of milk under very mild conditions, and should be especially useful for isolating and purifying milk protein components when enzymatic and other biological activities are to be preserved.

¹ This study was supported in part by funds from the California Dairy Industry Advisory Board.