Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties

Autor:	E. D. Posokhina, O. A. Mogilnaya, K. S. Artemenko, Vladimir S. Bondar, N. O. Ronzhin
Rok vydání:	2020
Předmět:	Biophysics Biochemistry Catalysis Fungal Proteins 03 medical and health sciences chemistry.chemical_compound Extracellular Biomass Hydrogen peroxide Mycelium Neonothopanus nambi 030304 developmental biology chemistry.chemical_classification 0303 health sciences Oxidase test Phenol biology 030302 biochemistry & molecular biology Temperature Hydrogen Peroxide General Chemistry General Medicine Hydrogen-Ion Concentration Alcohol oxidase Ampyrone Oxygen Alcohol Oxidoreductases Kinetics Enzyme chemistry Chromatography Gel biology.protein Agaricales Oxidoreductases Oxidation-Reduction Peroxidase
Zdroj:	Doklady Biochemistry and Biophysics. 490:38-42
ISSN:	1608-3091 1607-6729
DOI:	10.1134/s1607672920010135
Popis:	Using the original technique of treating biomass with β-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80–85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with Km = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has Km value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22–35 and 55–70°C, and pH optimums are 6 and 5, respectively.
Databáze:	OpenAIRE
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