title: [Characterization of highly purified metalloprotease produced by Bacillus subtilis].
abstract: Proteolytic enzyme produced by Bacillus subtilis is characterized as typical metalloprotease with a molecular weight of 27.9 kD; the enzyme shows its highest activity at pH 7.0-9.0, possesses substrate specificity with respect to different proteins, its temperature optimum is 52 degrees C and its specific activity exceeds that of all known commercial analogues. At 37 degrees C the enzyme is half inactivated in 72 hours.
authors.affiliation: State Unitary Enterprise Immunopreparat, Ufa, Russia.
authors.forename: A F
authors.initials: AF
authors.lastname: Khaziev
authors.forename: N A
authors.initials: NA
authors.lastname: Mikhaĭlova
authors.forename: M M
authors.initials: MM
authors.lastname: Alsynbaev
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification; D003470:Culture Media; D004789:Enzyme Activation; D007700:Kinetics; D045726:Metalloproteases / Q000032:analysis* / Q000302:isolation & purification; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D045726:Metalloproteases