Comparative Kinetic Characterization of Catalases of the Genus Penicillum

• Published in: Applied biochemistry and microbiology Vol. 36; no. 3; pp. 221 - 226
• Main Authors: Eremin, AN, Mikhailova, R V, Metelitsa, DI
• Format: Journal Article
• Language: English
• Published: 2000
• Subjects: Penicillium
• ISSN: 0003-6838
• DOI: 10.1007/BF02742569

Extracellular catalases produced by fungi of the genus Penicillium, i.e., P. piceum, P. varians, and P.kapuscinskii, were purified by consecutive filtration of culture liquids. The maximum reaction rate of H sub(2)O sub(2) 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 sub(in) at 30 degree C). The thermal stability was determined by the rate of enzyme thermal inactivation at 45 degree C (k* sub(in), S sub(-) super(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.