Action of Milk Clotting Enzymes on αs-Caseins from Buffalo's and Cow's Milk

Abstract

α s-Caseins were isolated from buffalo's and cow's milk and hydrolyzed with rennet, bovine pepsin, microbial proteases from Mucor miehei, Mucor pusillus Lindt, and Endothia parasitica. The rate of hydrolysis was followed by determining the unaltered αs-casein in the digest after acrylamide gel electrophoresis. The rate of hydrolysis of αs-casein from the two species with the different enzymes was comparable, being more rapid with microbial enzymes particularly Endothia parasitica protease. However, the electrophoretic patterns of the degradation products of buffalo's and cow's αs-casein produced by microbial rennets were not identical. © 1977, American Dairy Science Association. All rights reserved.