Krasnoyarsk, Krasnoyarsk, Russian Federation
Krasnoyarsk, Krasnoyarsk, Russian Federation
Krasnoyarsk, Krasnoyarsk, Russian Federation
Krasnoyarsk, Krasnoyarsk, Russian Federation
An extracellular enzyme with oxidase activity was isolated from the mycelium of the higher fungus Neonothopanus nambi by mild treatment of the biomass with β-glucosidase. A substrate specificity and some properties of the isolated extracellular oxidase were studied in the present work. Experiments revealed that the extracellular oxidase exhibited activity with most phenolic compounds chosen as model substrates. It is important to note that the enzyme exhibited a catalytic function in the reactions without the addition of exogenous hydrogen peroxide and other mediators. The highest catalytic activity of the enzyme was observed with veratryl alcohol and dihydric phenols, hydroquinone and guaiacol. The enzyme showed lower activity with aromatic azo compounds (ABTS, DAB, o-dianisidine). In reactions with dihydric phenol resorcinol and monophenol, the enzyme efficiency was extremely low. The kinetic parameters of the enzymatic reactions with actively oxidized substrates were determined. The addition of a divalent metal ion chelator (EDTA) did not affect the activity of the enzyme, while the addition of the SH reagent (DTT) increased the catalytic efficiency of the studied oxidase. The totality of the data obtained indicates that the extracellular oxidase of the N. nambi fungus catalyzes the oxidation of a wide range of aromatic compounds under slightly acidic and neutral conditions without the addition of additional mediators (in particular, hydrogen peroxide). This creates the prerequisites for studying the applicability of the enzyme in biomedical analytics.
higher fungi, basidiomycete Neonothopanus nambi, extracellular oxidase, veratryl alcohol, phenolic compounds
1. Zhang D., Gersberg R.M., Ng W.J., Tan S.K. Removal of pharmaceuticals and personal care products in aquatic plant-based systems: A review. Environmental Pollution, 2014, vol. 184, doi:https://doi.org/10.1016/j.envpol.2013.09.009.
2. Wang X., Yao B., Su X. Linking enzymatic oxidative degradation of lignin to organics detoxification. International Journal of Molecular Sciences, 2018, vol. 19, doi:https://doi.org/10.3390/ijms19113373.
3. Morsi R., Bilal M., Iqbal H.M.N., Ashraf S.S. Laccases and peroxidases: The smart, greener and futuristic biocatalytic tools to mitigate recalcitrant emerging pollutants. Science of The Total Environment, 2020, vol. 714, doi:https://doi.org/10.1016/j.scitotenv.2020.136572.
4. Savino S., Fraaije M.W. The vast repertoire of carbohydrate oxidases: An overview. Biotechnology advances, 2021, vol. 51, doi:https://doi.org/10.1016/j.biotechadv.2020.107634.
5. Sousa A.C., Martins L.O., Robalo M.P. Laccases: Versatile biocatalysts for the synthesis of heterocyclic cores. Molecules, 2021, vol. 26, doi:https://doi.org/10.3390/molecules26123719.
6. Martinkova L., Kotik M., Markova E., Homolka L. Biodegradation of phenolic compounds by Basidiomycota and its phenol oxidases: A review. Chemosphere, 2016, vol. 149, doi:https://doi.org/10.1016/J.CHEMOSPHERE.2016.01.022.
7. Martinez A.T., Ruiz-Duenas F.J., Camarero S. et al. Oxidoreductases on their way to industrial biotransformations. Biotechnology Advances, 2017, vol. 35, doi:https://doi.org/10.1016/j.biotechadv.2017.06.003.
8. Li F., Ma W., Wu X., Wang Y., He J. Luminol, horseradish peroxidase, and glucose oxidase ternary functionalized graphene oxide for ultrasensitive glucose sensing. Analytical and Bioanalytical Chemistry, 2018, vol. 410, doi:https://doi.org/10.1007/s00216-017-0752-5.
9. Nikolaivits E., Dimarogona M., Karagiannaki I., Chalima A., Fishman A., Topakas E. Versatile fungal polyphenol oxidase with chlorophenol bioremediation potential: characterization and protein engineering. Applied and Environmental Microbiology, 2018, vol. 84, doi:https://doi.org/10.1128/AEM.01628-18.
10. Tu T., Wang Y., Huang H., Wang Y., Jiang X., Wang Z., Yao B., Luo H. Improving the thermostability and catalytic efficiency of glucose oxidase from Aspergillus niger by molecular evolution. Food Chemistry, 2019, vol. 281, doi:https://doi.org/10.1016/j.foodchem.2018.12.099.
11. Jankowski N., Koschorreck K., Urlacher V.B. High-level expression of aryl-alcohol oxidase 2 from Pleurotus eryngii in Pichia pastoris for production of fragrances and bioactive precursors. Applied Microbiology and Biotechnology, 2020, vol. 104, doi:https://doi.org/10.1007/s00253-020-10878-4.
12. Shebanova A.D., Chernykh A.M., Baskunov B.P., Gaidina A.S., Myasoedova N.M., Renfeld Z.V., Ponamoreva O.N., Kolomytseva M.P. Novel biocatalyst from Microthielavia ovispora VKM F-1735 for industrial dye decolorization in the absence of mediators. Process Biochemistry, 2021, vol. 109, doi:https://doi.org/10.1016/j.procbio.2021.07.009.
13. Tamaru Y., Umezawa K., Yoshida M. Characterization of an aryl-alcohol oxidase from the plant saprophytic basidiomycete Coprinopsis cinerea with broad substrate specificity against aromatic alcohols. Biotechnology Letters, 2018, vol. 40, no. 7, doi:https://doi.org/10.1007/s10529-018-2534-3.
14. Wang N., Ren K., Jia R., Chen W., Sun R. Expression of a fungal manganese peroxidase in Escherichia coli: a comparison between the soluble and refolded enzymes. BMC Biotechnology, 2016. vol. 16, no. 87, doi:https://doi.org/10.1186/s12896-016-0317-2.
15. Zdarta J., Meyer A.S., Jesionowski T., Pinelo M. Developments in support materials for immobilization of oxidoreductases: a comprehensive review. Advances in Colloid and Interface Science, 2018, vol. 258, doi:https://doi.org/10.1016/j.cis.2018.07.004.
16. Athamneh K., Alneyadi A., Alsadik A., Wong T.S., Ashraf S.S. Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases. PLOS ONE, 2022, vol. 17, doi:https://doi.org/10.1371/journal.pone.0262492.
17. Liu X., DengW., Yang Y. Characterization of a novel laccase LAC-Yang1 from white-rot fungus Pleurotus ostreatus strain Yang1 with a strong ability to degrade and detoxify chlorophenols. Molecules, 2021, vol. 26, doi:https://doi.org/10.3390/molecules26020473.
18. Cleveland M., Lafond M., Xia F.R., Chung R., Mulyk P., Hein J.E., Brumer H. Two Fusarium copper radical oxidases with high activity on aryl alcohols. Biotechnology and Biofuels, 2021, vol. 14, doi:https://doi.org/10.1186/s13068-021-01984-0.
19. Kimani V., Ullrich R., Buttner E., Herzog R., Kellner H., Jehmlich N., Hofrichter M., Liers K. First Dye-decolorizing peroxidase from an ascomycetous fungus secreted by Xylaria grammica. Biomolecules, 2021, vol. 11, doi:https://doi.org/10.3390/biom11091391.
20. Ferreira P., Carro J., Balcells B., Martinez A.T., Serrano A. Expanding the physiological role of aryl-alcohol flavooxidases as quinone reductases. Applied and Environmental Microbiology, 2023, vol. 89, doi:https://doi.org/10.1128/aem.01844-22.
21. Ronzhin N.O., Posokhina E.D., Mogilnaya O.A., Bondar V.S. Extracellular oxidases of basidiomycete Neonothopanus nambi: isolation and some properties. Doklady Biochemistry and Biophysics, 2020, vol. 490, no. 1, doi:https://doi.org/10.1134/S1607672920010135.
22. Mogilnaya O., Ronzhin N., Posokhina E., Bondar V. Extracellular oxidase from the Neonothopanus nambi fungus as a promising enzyme for analytical applications. The Protein Journal, 2021, vol. 40, no. 5, doi:https://doi.org/10.1007/s10930-021-10010-z.
23. Maryskova M., Linhartova L., Novotny V., Rysova M., Cajthaml T., Sevcu A. Laccase and horseradish peroxidase for green treatment of phenolic micropollutants in real drinking water and wastewater. Environmental Science and Pollution Research, 2021, vol. 28, doi:https://doi.org/10.1007/s11356-021-12910-0.
