López-Fandiño R, Ramos M, Fernández-García E, Olano A
Instituto de Fermentaciones Industriales (CSIC), Madrid, España.
J Dairy Res. 1991 Nov;58(4):461-7. doi: 10.1017/s0022029900030065.
Electrophoretic analysis of the action of two commercial enzymes, Neutrase 0.5 and MKC Fungal Protease, on whole casein and alpha s-, beta- and kappa-caseins from cows' and ewes' milk showed that Neutrase 0.5 chiefly degraded beta-casein, giving rise to peptides soluble at pH 4.6 detectable by PAGE. In contrast, although MKC Fungal Protease caused intense hydrolysis of bovine beta-casein, in ovine casein it resulted in more active degradation of alpha s- than beta-casein. The latter enzyme did not produce peptides soluble at pH 4.6 detectable by PAGE. Both enzymes degraded kappa-casein, yielding a breakdown product that exhibited an electrophoretic mobility similar to that of the breakdown product produced by the action of commercial rennet.
对两种商业酶（Neutrase 0.5和MKC真菌蛋白酶）作用于全酪蛋白以及来自牛奶和羊奶的αs-、β-和κ-酪蛋白的电泳分析表明，Neutrase 0.5主要降解β-酪蛋白，产生在pH 4.6时可溶的肽，通过聚丙烯酰胺凝胶电泳（PAGE）可检测到。相比之下，尽管MKC真菌蛋白酶能强烈水解牛β-酪蛋白，但在羊酪蛋白中，它对αs-酪蛋白的降解比对β-酪蛋白的降解更活跃。后一种酶不会产生通过PAGE可检测到的在pH 4.6时可溶的肽。两种酶都能降解κ-酪蛋白，产生一种降解产物，其电泳迁移率与商业凝乳酶作用产生的降解产物相似。
