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Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties

  • BIOCHEMISTRY, BIOPHYSICS, AND MOLECULAR BIOLOGY
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Abstract

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.

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Authors and Affiliations

  1. Institute of Biophysics, Federal Research Center “Krasnoyarsk Scientific Center”, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russia

    N. O. Ronzhin, O. A. Mogilnaya, K. S. Artemenko, E. D. Posokhina & V. S. Bondar

  2. Siberian Federal University, Krasnoyarsk, Russia

    E. D. Posokhina

Authors
  1. N. O. Ronzhin
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  2. O. A. Mogilnaya
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  3. K. S. Artemenko
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  4. E. D. Posokhina
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  5. V. S. Bondar
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Correspondence to N. O. Ronzhin.

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The authors declare that they have no conflict of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.

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Translated by M. Batrukova

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Ronzhin, N.O., Mogilnaya, O.A., Artemenko, K.S. et al. Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties. Dokl Biochem Biophys 490, 38–42 (2020). https://doi.org/10.1134/S1607672920010135

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