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Journal of Dairy Science Vol. 51 No. 5 792-794
© 1968 by American Dairy Science Association ®
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Degradation of Casein Fractions by Rennet Extract

R. A. Ledford, J. H. Chen and K. R. Nath

Department of Food Science, Cornell University, Ithaca, New York

ABSTRACT

The proteolytic activity of commercial rennet on purified fractions of {alpha}s- and ß-casein was studied. Products of proteolysis, soluble in 5% trichloroacetic acid, were examined by gel-filtration and by absorbancy at 280 mµ. Residual casein fractions were determined by polyacrylamide-gel electrophoresis.

Rennet enzymes appear to preferentially degrade {alpha}s-casein. ß-casein evidently is more resistant to rennet proteolysis than a.-casein. These findings confirm results of our studies with whole casein and sug- gest that successful rennet substitutes need to have the delicate differential proteolytie characteristics of rennet.






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Copyright © 1968 by the American Dairy Science Association ®.