Keywords
enzymatic activity
immobilization
greenhouse gas emissions
How to Cite
Abstract
Laccases (benzodiol: oxygen oxidoreductases, EC 1.10.3.2) belong to the so-called blue-copper oxidase family and are coppercontaining enzymes that are involved in oxidative processes by catalyzing the oxidation of various compounds with molecular oxygen, including o- and w-diphenols, aminophenols, polyphenols, polyamines, aryl diamines, phenolic substructures of lignin, and also some inorganic ions. The physiological functions of laccases are diverse: participation in the formation of pigments and the formation of fruiting bodies of fungi, detoxification of phenols, catalysis of the oxidation of non-phenolic lignin units (C4-esterified) to radicals.
Laccase activity increases due to the introduction of Cu2+, Mg2+ and Na+, but is strongly inhibited by Fe2+, Ag+, l-cysteine, dithiothreitol and NaN3. In the lower soil layers, the activity of laccase shows a significant increase when supplied with mineral N, the addition of compost leads to increased activity in the surface layer.
The prospects for the practical use of oxidases increased after the discovery of the possibility of enhancing their action using redox mediators, which are substrates of these enzymes, during the oxidation of which highly redox potential and chemically active products are formed. Biocatalytic systems created by nano-technologies (bacterial nanocellulose, carbon nanotubes, magnetic nanoflowers etc.) increase the reaction efficiency by increasing the surface area and loading capacity, and reducing the mass transfer resistance. The effectiveness of immobilization is highly dependent on the process conditions, the properties of the enzyme and the material of the carrier. In particular, a clear correlation was established between the redox potential of the substrate and the efficiency of homogeneous catalysis.
Of particular note is the effect of laccase on soil emissions of CO2 and other greenhouse gases. Participating in the polymerization of soluble phenols, they thereby contribute to humification, forming stable humic fractions that bind soil carbon.
The data presented indicate that soil laccase is an important factor in the functionality of soil, but they need to be studied in more detail in order to understand the mechanisms that regulate their activity.
References
Gorbacheva, M.A. (2009), Biocatalytic properties of laccases from various sources. Diss. Cand. Chem. sciences. M.: IBC, 146 p. (in Russian)
Leontievsky, A.A. (2002), Ligninases of basidiomycetes. Diss. Doct. biol. sciences. M.: IBPM, 266 p. (in Russian)
Morozova, O.V., Shumakovich, G.P., Gorbacheva, M.A., Shleev, S.B. and Yaropolov, A.I. (2007), Blue laccases. Biochemistry, vol. 72, N 10, pp. 1396—1412. (in Russian)
Shleev, S.V. (2010), The functioning, mechanism of regulation of activity and the possible practical use of blue copper-containing oxidases. Diss. Doct. biol. sciences. M.: IBC, 322 p. (in Russian)
Ashe, B., Nguyen, L.N., Hai, F.I., Lee, D.-J. and Nghiem, L. D. (2016), Impacts of redox-mediator type on trace organic contaminants degradation by laccase: Degradation efficiency, laccase stability and effluent toxicity. International Biodeterioration and Biodegradation, vol. 113, pp. 169—176.
Bansal, M., Kumar, D., Chauhan, G.S. and Kaushik, A. (2018), Preparation, characterization and trifluralin degradation of laccase-modified cellulose nanofibers. Materials Science for Energy Technologies, vol. 1, N 1, pp. 29—37.
Bourbonnais, R. and Paice, M.G. (1990), Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation. FEBS Lett., vol. 267, N 1, pp. 99—102.
Bressler, D.C., Fedorak, P.M. and Pickard, M.A. (2000), Oxidation of carbazole, N-ethylcarbazole, fluorene and dibenzothiophene by the laccase of Coriolopsis gallica. Biotechnology Letters, vol. 22, pp. 1119— 1125.
Carlos, S.N., Adinarayana, K. and Vikas, K. (2018), Enzymes in human and animal nutrition. Academic Press, pp. 133—161.
Das, R., Li, G., Mai, B. and An, T. (2018), Spore cells from BPA degrading bacteria Bacillus sp. GZB displaying high laccase activity and stability for BPA degradation. Science of The Total Environment, vol. 640— 641, pp. 798—806.
Fu, M., Xing, J. and Ge, Z. (2019), Preparation of laccase-loaded magnetic nanoflowers and their recycling for efficient degradation of bisphenol A. Science of The Total Environment, vol. 651, pt. 2, pp. 2857— 2865.
Gianfreda, L., Xu, F. and Bollag, J.-M. (1999), Laccases: a useful group of oxidoreductive enzymes. Bioremediation Journal, N 3(1), pp. 1—26.
Glazunova, O.A., Polyakov, K.M., Moiseenko, K.V., Kurzeev, S.A. and Fedorova, T.V. (2018), Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi. International Journal of Biological Macromolecules, vol. 118, part A, pp. 406—418.
Goh, K.M. (2011), Carbon sequestration and stabilization in soils: Implications for soil productivity and climate change. Soil Science and Plant Nutrition, vol. 50, N 4, pp. 467—476.
Gold, M.H. and Alic, M. (1993), Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Microbiol. Rev., vol. 57, N 3, pp. 605—622.
Hernández-Monjaraz, W.S., Caudillo-Pérez, C., Salazar- Sánchez, P.U. and Macías-Sánchez, K.L. (2018), Influence of iron and copper on the activity of laccases in Fusarium oxysporum f. sp. lycopersici. Brazilian Journal of Microbiology, vol. 49, N 1, pp. 269—275.
Jensen, K.A., Evans, К.M.C., Kirk, Т.K. and Hammel, К.E. (1994), Biosynthetic pathway for veratryl alcohol in the ligninolytic fungus Phanerochaete chrysosporium. Appl. Environ. Microbiol., vol. 60, N 2, pp. 709—714.
Johannes, C., Majcherczyk, A. and Huttermann, A. (1996), Degradation of anthracene by laccase of Trametes versicolor in the presence of different mediator compounds. Appl. Microbiol. Biotechnol., vol. 46, pp. 313—317.
Kang, K.-H., Dec, J., Park, H. and Bollag, J.-M. (2002), Transformation of the fungicide cyprodinil by a laccase of Trametes villosa in the presence of phenolic mediators and humic acid. Wat. Res., vol. 36, pp. 4907—4915.
Leontievsky, A.A., Vared, T., Lankinen, P., Shergill, J., Pozdnyakova, N., Myasoedova, N.M., Kalkkinen, N., Golovleva, L.A., Cammack, R., Thruston, C. and Hatakka, A. (1997), Blue and yellow laccases of ligninolytic fungi. FEMS Microbiol. Lett., vol. 156, pp. 9—14.
Ling, L., Wu, R.-N., Meng, H., Li, X.-Y. and Gu J.-D. (2016), Seasonal and spatial variations in diversity and abundance of bacterial laccase-like genes in sediments of a subtropical mangrove ecosystem. International Biodeterioration and Biodegradation, vol. 114, pp. 260— 267.
Lonappan, L., Liu, Y., Rouissi, T., Brar, S.K., Verma, M. and Surampalli, R.Y. (2018), Adsorptive immobilization of agro-industrially produced crude laccase on various micro-biochars and degradation of diclofenac. Science of the Total Environment, vol. 640—641, pp. 1251—1258.
Luis, P., Kellner, H., Martin, F. and Buscot, F. (2005), A molecular method to evaluate basidiomycete laccase gene expression in forest soils. Geoderma, vol. 128, N 1—2, pp. 18—27.
Mayer, A.M. and Staples, R.C. (2002), Laccase: new functions for an old enzyme. Phytochemistry, vol. 60, pp. 551—565.
Mazzon, M., Cavani, L., Margon, A. and Sorrenti, G. (2018), Changes in soil phenol oxidase activities due to long-term application of compost and mineral N in a walnut orchard. Geoderma, vol. 316, pp. 70—77.
Mougin, C., Kollmann, A. and Jolivalt, C. (2002), Enhanced production of laccase in the fungus Trametes versicolor by the addition of xenobiotics. Biotechnology Letters, vol. 24, pp. 139—142.
Naghdi, M., Taheran, M, Brar, S.K., Kermanshahipour, A., Verma, M. and Surampalli, R.Y. (2018), Pinewood nanobiochar: A unique carrier for the immobilization of crude laccase by covalent bonding. International Journal of Biological Macromolecules, vol. 115, pp. 563—571.
Navada, K.K. and Kulal, A. (2019), Enzymatic degradation of chloramphenicol by laccase from Trametes hirsuta and comparison among mediators. International biodeterioration and biodegradation, vol.138, pp. 63—69.
Osikoya, A.O., Opoku, F., Dikio, E.D. and Govender, P.P. (2019), High-throughput 2D heteroatom graphene bioelectronic nanosculpture: A combined experimental and theoretical study. ACS Appl. Mater. Interfaces, pp. 11238—11250.
Partavian, A., Mikkelsen, T.N. and Vestergård, M. (2015), Plants increase laccase activity in soil with long-term elevated CO2 legacy. European Journal of Soil Biology, vol. 70, pp. 97—103.
Qi, L., Liang, S. and Huang, Q. (2018), Laccase induced degradation of perfluorooctanoic acid in a soil slurry. Journal of Hazardous Materials, vol.359, pp. 241—247.
Santana, T.T., Linde, G.A., Colauto, N.B. and do Valle, J.S. (2018), Metallic-aromatic compounds synergistically induce Lentinus crinitus laccase production. Biocatalysis and Agricultural Biotechnology, vol. 16, pp. 625—630.
Skoronski, E., Souza, D.H., Ely, C., Broilo, F., Fernandes, M., Fúrigo, A. and Ghislandi, M.G. (2017), Immobilization of laccase from Aspergillus oryzae on graphene nanosheets. International Journal of Biological Macromolecules, vol. 99, pp. 121—127.
Vignault, A., Pascual, O., Jourdes, M., Moine, V., Fermaud, M., Roudet, J., Canals, J.M., Teissedre, P.-L. and Zamora, F. (2019), Impact of enological tannins on laccase activity. Special Macrowine, vol 53, N 1.
Wu, Y., Jiang, Y., Jiao, J., Liu, M., Hu, F., Griffiths, B.S. and Li, H. (2014), Adsorption of Trametes versicolor laccase to soil iron and aluminum minerals: Enzyme activity, kinetics and stability studies. Colloids and Surfaces B: Biointerfaces, vol. 114, pp. 342—348.
Yuan, H., Chen, L., Hong, F.F. and Zhu, M. (2018), Evaluation of nanocellulose carriers produced by four different bacterial strains for laccase immobilization. Carbohydrate Polymers, vol. 196, pp. 457—464.
Zdarta, J., Antecka, K., Frankowski, R., Zgo A a-GrzeB kowiak, A., Ehrlich, H. and Jesionowski, T. (2018), The effect of operational parameters on the biodegradation of bisphenols by Trametes versicolor laccase immobilized on Hippospongia communis spongin scaffolds. Science of the Total Environment, vol. 615, pp. 784—795.
Zeng, J., Zhu, Q., Wu, Y. and Lin, X. (2016), Oxidation of polycyclic aromatic hydrocarbons using Bacillus subtilis CotA with high laccase activity and copper independence. Chemosphere, vol. 148, vol. 1—7.
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