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Cow Milk Proteins: Twenty-Five Years of Progress¹

Department of Food Science and Human Nutrition, Michigan State University, East Lansing 48824

ABSTRACT

Introduction

Before assessing the progress in our understanding of the milk protein system of cow's milk since 1955, it seems appropriate to recall the level of knowledge at that time. As early as 1925 Linderstrøm-Lang questioned the homogeneity of casein, which was in opposition to Hammersten's contention that it was a homogeneous compound. In 1939, Mellander, utilizing the newly introduced Tiselius moving-boundary electrophoretic technique, reported that casein showed three boundaries, which he designed -, ß-, and -casein in order of decreasing mobility. This event marked the genesis of a nomenclature system for caseins based upon electrophoretic resolution. By 1952, three discrete components, corresponding to the three electrophoretic boundaries, had been separated from isoelectric casein by utilizing their unique solubility characteristics at specific pH and temperature in dissociating solvents, viz., urea and alcohol.

Detailed electrophoretic studies of the principal component, -casein, under various experimental conditions revealed that this seemingly homogeneous fraction consisted of more than one component.

¹ Michigan Agricultural Experiment Station Journal Article No. 9600.

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