title: [Purification and characterization of milk-clotting enzymes from oyster mushroom (Pleurotus ostreatus (Fr.) Kumm.)].
abstract: Three enzymes with milk-clotting activity have been isolated from the fruiting bodies of Pleurotus ostreatus (Fr.) Kumm.) by (NH4)2SO4 precipitation, gel chromatography on Sephadex G75, and ion exchange chromatography on carboxymethylcellulose (CMC). Isoelectric points of the enzymes, as determined by isoelectrofocusing, equaled 4.2, 6.7, and 8.8. Inhibition analysis showed that the enzymes with isoelectric points of 4.2 and 6.7 belong to the class of metal-dependent proteinases, while the enzyme with the isoelectric point of 8.8 belongs to the serine protease class.
authors.forename: G V
authors.initials: GV
authors.lastname: Lebedeva
authors.forename: M T
authors.initials: MT
authors.lastname: Proskuriakov
mesh_terms: D000818:Animals; D002417:Cattle; D048690:Fruiting Bodies, Fungal / Q000201:enzymology*; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification*; D007526:Isoelectric Point; D045726:Metalloproteases / Q000737:chemistry / Q000302:isolation & purification*; D008892:Milk; D020076:Pleurotus / Q000201:enzymology*; D057057:Serine Proteases / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D005656:Fungal Proteins; D045726:Metalloproteases; D057057:Serine Proteases