title: Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins.
abstract: 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.
authors.affiliation: Instituto de Fermentaciones Industriales (CSIC), Madrid, España.
authors.forename: R
authors.initials: R
authors.lastname: López-Fandiño
authors.forename: M
authors.initials: M
authors.lastname: Ramos
authors.forename: E
authors.initials: E
authors.lastname: Fernández-García
authors.forename: A
authors.initials: A
authors.lastname: Olano
mesh_terms: D000818:Animals; D001236:Aspergillus oryzae / Q000201:enzymology*; D001412:Bacillus subtilis / Q000201:enzymology*; D002364:Caseins / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D005260:Female; D006863:Hydrogen-Ion Concentration; D012756:Sheep; D012995:Solubility
chemical_list: D002364:Caseins; D010450:Endopeptidases