SELECTION AND STUDYING OF THE BIOSYNTHETIC ABILITY OF MANGANESE PEROXIDASE (MNP) OF MUSHROOM STRAINS, ORIENTING THE APPLICATION TO DEGRADE LIGNIN
Keywords:
Degrading lignin, increasing production, Manganese peroxidase, Pleurotus sp. PL3, selectionAbstract
Manganese peroxidase (MnP) is an enzyme that is able to degrade lignin and some toxic organic compounds. MnP is biosynthesized by fungi, bacteria and actinomycetes. In this study, the result of the selection of MnP biosynthetic fungal strains and their MnP biosynthetic potential are presented. Research results have selected the fungal strain Pleurotus sp. PL3 with the strongest MnP activity among the 8 investigated strains. MnP biosynthetic activity of Pleurotus sp. PL3 strain reached 2.03 U/mL in PDA medium supplemented with 0.5% NH4NO3, 3% glucose, pH 7.0, temperature culture 30°C for 9 days culture. This research is the basis for the production of MnP enzyme to degrade lignin in the wood processing industry.
References
1. Abdel-Hamid A.M., Solbiati J.O., Cann I.K., 2013. Insights into lignin degradation and its potential industrial applications. Advances in Applied Microbiology, 82: Elsevier; 1-28.
2. Kumar A. and Kumar Arora P., 2022, Biotechnological applications of Manganese peroxidases for sustainable management, Front. Environ. Sci., 10(26), https://doi.org/10.3389/fenvs.2022.875157.
3. Arunkumar M., Sheik A., Shahul H, 2014. Hyper-production of manganese peroxidase by mutant Pleurotus ostreatus MTCC 142 and its applications in biodegradation of textile azo dyes. Desalination Water Treat 56(2): 509-520.
4. Qin, X., Zhang, J., Zhang, X., and Yang, Y., 2014. Induction, purification and characterization of a novel manganese peroxidase from Irpex Lacteus CD2 and its application in the decolorization of different types of dye. PLoS One 9, e113282. doi:10.1371/journal.pone.0113282
5. Torres E. and Ayala M., 2010. Biocatalysis Based on Heme Peroxidases: Peroxidases as Potential Industrial Biocatalysts. Springer Berlin, Heidelberg. DOI: https://doi.org/10.1007/978-3-642-12627-7
6. Ginterová A., Polster M. & Janotková O., 1980. The relationship between Pleurotus ostreatus and Aspergillus flavus and the production of aflatoxin. Folia Microbiologica, 25: 332-336
7. Gonzalo de G., Colpa D.I., Habibb M.H.M., Fraaije M.W., 2016. Bacterial enzyme involved in lignin degradation. Journal of Biotechnology 236: 110-119.
8. Moldes D., Couto S.R., Cameselle C., Sanromán M.A., 2003. Study of the degradation of dyes by MnP of Phanerochaete chrysosporium produced in a fixed-bed bioreactor. Chemosphere 51: 295-303.
9. Vivekanand V., Dwivedi P., Pareek N., Singh R.P., 2011. Banana peel: a potential substrate for laccase production by Aspergillus fumigatus VkJ2.4.5 in solid-state fermentation. Appl. Biochem. Biotechnol. 165: 204-220.
10. Yuan Z. Y. & Jiang T. J., 2003. Horseradish peroxidase, in: J. R. Whitaker, A. Voragen, D. W. S. Wong (Eds.). Handbook of Food Enzymology, Marcel Dekker Inc., New York, pp. 403-411.
11. Nguyen D.H., Nguyen T.T.H., Le T.H., Hoang T.Q., Truong Q.T., Nguyen N.L., and Park S.M., 2017. Screening and Production of Manganese Peroxidase from Fusarium sp. on Residue Materials. Mycobiology. 45(1): 52-56.
12. Zhao X., Huang X., Yao J., Zhou Y., and Jia R., 2015. Fungal growth and Manganese peroxidase production in a deep tray solid-state bioreactor, and in vitro decolorization of poly R-478 by MnP. J. Microbiol. Biotechnol. 25(6): 803-813.
13. Hofrichter M., Lundell T., and hatakka A., 1999. Conversion of Milled Pine Wood by Manganese peroxidase from Phlebia radiate. Appl. Environ. Microbiol. 67(10): 4588-4593.
14. Hakala K., Lundell T., Galkin S., Maijala P., Kalkkinen N., Hatakka A., 2005. Manganese peroxidases, laccases and oxalic acid from the selective white-rot fungus Physisporinus rivulosus grown on spruce wood chips. Enzyme and Microbial Technol., 36 (4): 461-468.
15. Sellami K., Couvert A., Nasrallah N., Maachi R., Abouseoud M., 2022. Peroxidase enzymes as green catalysts for bioremediation and biotechnological applications: A review. Science of the Total Environment, 806, pp.150500. ff10.1016/j.scitotenv.2021.150500ff. ffhal-03464657