Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins.

摘要: Electrophoretic analysis of the action two commercial enzymes, Neutrase 0.5 and MKC Fungal Protease, on whole casein alpha s-, beta- kappa-caseins from cows' ewes' milk showed that chiefly degraded beta-casein, giving rise to peptides soluble at pH 4.6 detectable by PAGE. In contrast, although Protease caused intense hydrolysis bovine in ovine it resulted more active degradation s- than beta-casein. The latter enzyme did not produce Both enzymes kappa-casein, yielding a breakdown product exhibited an electrophoretic mobility similar produced rennet.