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

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Abstract
.alpha.s-Caseins were isolated from buffalo''s and cow''s milk and hydrolyzed with rennet, bovine pepsin, microbial proteases from Mucor miehei, M. pusillus Lindt, and Endothia parasitica. Rate of hydrolysis was followed by determining unaltered .alpha.s-casein in the digest after acrylamide gel electrophoresis. Rate of hydrolysis of .alpha.s-casein from the 2 spp. with the different enzymes was comparable, being more rapid with microbial enzymes, particularly E. parasitica protease. Electrophoretic patterns of degradation products of buffalo''s and cow''s .alpha.s-casein produced by microbial rennets were not identical.