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Comparative kinetic characterization of catalases of the genusPenicillum
Authors:A N Eremin  R V Mikhailova  D I Metelitsa
Institution:(1) Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Zhodinskaya ul. 5/2, 220141 Minsk, Belarus;(2) Institute of Microbiology, National Academy of Sciences of Belarus, Zhodinskaya ul. 5/2, 220141 Minsk, Belarus
Abstract:Extracellular catalases produced by fungi of the genusPenicillium, i.e.,P. piceum, P. varians, andP. 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 the effective rate of catalase inactivation during enzymatic reaction (k in at 30°C). The thermal stability was determined by the rate of enzyme thermal inactivation at 45°C (k in * , s-1). Catalase fromP. piceum displayed the maximum activity, which was higher than the activity of catalase from bovine liver. The operational stability of catalase fromP. 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 yeastC. boidinii.
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