| Abstrakt: |
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 H2O2decomposition, 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 (kinat 30°C). The thermal stability was determined by the rate of enzyme thermal inactivation at 45°C (kin*, s-1). Catalase fromP. piceumdisplayed the maximum activity, which was higher than the activity of catalase from bovine liver. The operational stability of catalase fromP. piceumwas 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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