Action of milk clotting enzymes on alphas-caseins from buffalo's and cow's milk.

alphaS-Caseins were isolated from buffalo's and cow's milk and hydrolyzed with rennet, bovine pepsin, microbial proteases from Mucor miebei, Mucor pusillus Lindt, and Endotbia parasitica. The rate of hydrolysis was followed by determining the unaltered alphaS-casein in the digest after acrylamide gel electrophoresis. The rate of hydrolysis of alphaS-casein from the two species with the different enzymes was comparable, being more rapid with microbial enzymes particularly Endotbia parasitica protease. However, the electrophoretic patterns of the degradation products of buffalo's and cow's alphaS-casein produced by microbial rennets were not identical.