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Calculation of the Molecular Size of -Casein Fractions Obtained by Gel-Filtration after Storage and Rennin Action¹

Department of Food Science, University of Illinois, Urbana

ABSTRACT

-Casein yielded three different peaks on Sephadex G-200 with 0.2 N NaOH at 4 C (4). Since the effects of strong bases on dextran-gel and on other reference proteins have not been well established, calculation of the molecular size of -casein peaks is of uncertain accuracy.

Published relationships between molecular size and effluent volume, V_e, of a substance may be classified into two groups; one of which is related to the molecular weight and the other to the particle size and shape. Squire's (5), and Laurent and Killander's (3) approaches were chosen because other equations have not shown any marked differences from those used in this paper.

Although molecular weight calculations from gel-filtration data are not as accurate as other methods, they may aid in understanding the molecular sieve effect of gel-matrices.

This investigation was undertaken to determine molecular changes in -casein resulting from heating, processing, and storage.

Experimental Procedures

¹ Supported by a grant from the American Dairy Association, 20 Wacker Drive, Chicago, Illinois.