[Comparative kinetic characteristics of catalase of Penicillium species molds].
Extracellular catalases produced by fungi of the genus Penicillium: P. piceum, P. varians and P. kapuscinskii were purified by consecutive filtration of culture liquids. The maximum reaction rate of H2O2 decomposition, the Michaelis constants and specific catalytic activities of isolated catalases were determined. The operational stability was characterized by effective rate of catalase inactivation during enzymatic reaction (kin at 30 degrees C). The thermal stability was determined by the rate of enzyme thermal inactivation at 45 degrees C (k*[symbol: see text]H, s-1). Catalase from P. piceum displayed the maximum activity, which was higher than the activity of catalase from bovine liver. The operational stability of catalase from P. piceum was twofold to threefold higher than the stability of catalase from bovine liver. The physicochemical characteristics of catalases of fungi are better than the characteristics of catalase from bovine liver and intracellular catalase of yeast C. boidinii.
Eremin
A N
AN
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus.
Mikhaĭlova
R V
RV
Metelitsa
D I
DI
D000818:Animals; D002175:Candida / Q000201:enzymology; D002374:Catalase / Q000378:metabolism*; D002384:Catalysis; D002417:Cattle; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010407:Penicillium / Q000201:enzymology*; D013045:Species Specificity; D013696:Temperature
D002374:Catalase
Sravnitel'naia kineticheskaia kharakteristika katalaz gribov roda Penicillium.