Proteolytic activities of Suparen and Rennilase on buffalo, cow, and goat whole casein and beta-casein

The proteolytic specificity and activity of Mucor miehei protease (Rennilas e) and Endothia parasitica protease (Suparen) on buffalo, cow, and goat who le casein and beta-casein (CN) were studied by analyzing the degradation pr oducts. The results suggest that Rennilase hydrolyzes casein of the three s pecies in a manner similar to that of chymosin, resulting in the formation of alpha(s1)-I and beta-I, -II, -III as initial degradation fragments of al pha(s1)- and beta-CN. alpha(s1)-I was also the initial breakdown product of alpha(s1)-CN by Suparen. Contrary to Rennilase, Suparen showed a higher af finity toward beta-CN and hydrolyzes beta-CN, giving rise to degradation pr oducts characterized by mobility lower than that of beta-CN. Increasing NaC l concentration (>3%) reduced the proteolysis of beta-CN of the three speci es by Rennilase but not by Suparen. The hydrolysis of alpha(s1)-CN and alph a(s1)-I by the two enzymes was enhanced in the presence of NaCl.