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Lignin peroxidase in focus for catalytic elimination of contaminants — A critical review on recent progress and perspectives
Abstract
Lignin peroxidase (LiP) seems to be a catalyst for cleaving high-redox potential non-phenolic compounds with an oxidative cleavage of CC and COC bonds. LiP has been picked to seek a practical and cost-effective alternative to the sustainable mitigation of diverse environmental contaminants. LiP has been an outstanding tool for catalytic cleaning and efficient mitigation of environmental pollutants, including lignin, lignin derivatives, dyes, endocrine-disrupting compounds (EDCs), and persistent organic pollutants (POPs) for the past couple of decades. The extended deployment of LiP has proved to be a promising method for catalyzing these environmentally related hazardous pollutants of supreme interest. The advantageous potential and capabilities to act at different pH and thermostability offer its working tendencies in extended environmental engineering applications. Such advantages led to the emerging demand for LiP and increasing requirements in industrial and biotechnological sectors. The multitude of the ability attributed to LiP is triggered by its stability in xenobiotic and non-phenolic compound degradation. However, over the decades, the catalytic activity of LiP has been continuing in focus enormously towards catalytic functionalities over the available physiochemical, conventional, catalyst mediated technology for catalyzing such molecules. To cover this literature gap, this became much more evident to consider the catalytic attributes of LiP. In this review, the ex…
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“Both LiP and MnP can oxidize a wide range of environmental pollutants such as phenolic and non-phenolic compounds, dyes, and xenobiotics (134, 139, 142).”
From Toward the development of a molecular toolkit for the microbial remediation of per-and polyfluoroalkyl substances (2024) · cites this paper as [142]
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Catalytic Transformation of Lignin for the Production of Chemicals and Fuels
Li, C., Zhao, X., Wang, A., Huber, G. W., & Zhang, T. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00155 · Cited by 2,951
Conversion of Biomass into Chemicals over Metal Catalysts
Besson, M., Gallezot, P., & Pinel, C. (2014) · Chemical Reviews · doi:10.1021/cr4002269 · Cited by 1,780
Burakov, A. E., Galunin, E. V., Burakova, I. V., Kucherova, A. E., Agarwal, S., Tkachev, A. G., & Gupta, V. K. (2018) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2017.11.034 · Cited by 1,612
Lignin depolymerisation strategies: towards valuable chemicals and fuels
Xu, C., Arancon, R. A. D., Labidi, J., & Luque, R. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00235k · Cited by 1,031
Vanillin production from lignin and its use as a renewable chemical
Fache, M., Boutevin, B., & Caillol, S. (2016) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.5b01344 · Cited by 902
Mohammadi, N., Khani, H., Gupta, V. K., Amereh, E., & Agarwal, S. (2011) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2011.06.067 · Cited by 818
Hydrothermal conversion of lignin: A review
Kang, S., Li, X., Fan, J., & Chang, J. (2013) · Renewable and Sustainable Energy Reviews · doi:10.1016/j.rser.2013.07.013 · Cited by 552
Kong, W., Fu, X., Wang, L., Alhujaily, A., Zhang, J., Ma, F., Zhang, X., & Yu, H. (2017) · Biotechnology for Biofuels · doi:10.1186/s13068-017-0906-x · Cited by 103
Research works printed but not linked: 311
- Söderholm, 2019, Environmental regulation in the pulp and paper industry: impacts and challenges, Curr. For. Rep., 5, 185, 10.1007/s40725-019-00097-0 · DOI
- A.K. Singh, A. Raj, Emerging and eco-friendly approaches for waste management: a book review. Environ. Sci. Eur. 32(1) (2020) 107. · DOI
- Shahid, 2020, Environmental toxicology and associated human health risks, Environ. Sci. Pollut. Res., 27, 39671, 10.1007/s11356-020-10516-6 · DOI
- Samsami, 2020, Recent advances in the treatment of dye-containing wastewater from textile industries: overview and perspectives, Process Saf. Environ. Prot., 143, 138, 10.1016/j.psep.2020.05.034 · DOI · Paper page
- Talaiekhozani, 2020, Combination of TiO2 microreactor and electroflotation for organic pollutant removal from textile dyeing industry wastewater, Alex. Eng. J., 59, 549, 10.1016/j.aej.2020.01.052 · DOI
- Sonkar, 2021, A novel sequence batch treatment of wastewater using Bacillus sp. IITRDVM-5 mixing with paper mill and sewage sludge powders, Environ. Technol. Innov., 21, 10.1016/j.eti.2020.101288 · DOI
- Rasheed, 2019, Environmentally-related contaminants of high concern: potential sources and analytical modalities for detection, quantification, and treatment, Environ. Int., 122, 52, 10.1016/j.envint.2018.11.038 · DOI
- Cohen, 2009, Characterization of catechol derivative removal by lignin peroxidase in aqueous mixture, Bioresour. Technol., 100, 2247, 10.1016/j.biortech.2008.11.007 · DOI
- Bilal, 2018, Peroxidases-assisted removal of environmentally-related hazardous pollutants with reference to the reaction mechanisms of industrial dyes, Sci. Total Environ., 644, 1, 10.1016/j.scitotenv.2018.06.274 · DOI · Paper page
- Bilal, 2020, Environmental impact of lignocellulosic wastes and their effective exploitation as smart carriers — a drive towards greener and eco-friendlier biocatalytic systems, Sci. Total Environ., 722, 10.1016/j.scitotenv.2020.137903 · DOI
- Zhang, 2020, Production of metal oxides nanoparticles based on poly-alanine/chitosan/reduced graphene oxide for photocatalysis degradation, anti-pathogenic bacterial and antioxidant studies, Int. J. Biol. Macromol., 164, 1584, 10.1016/j.ijbiomac.2020.07.291 · DOI
- Lu, 2020, Cr2O3/cellulose hybrid nanocomposites with unique properties: facile synthesis, photocatalytic, bactericidal and antioxidant application, J. Photochem. Photobiol. B Biol., 205, 111842, 10.1016/j.jphotobiol.2020.111842 · DOI
- Cen, 2020, Synthesis and structure of iron–copper/hollow magnetic/metal–organic framework/coordination sites in a heterogeneous catalyst for a Fenton-based reaction, Catal. Sci. Technol., 10, 6687, 10.1039/D0CY01027H · DOI
- Wang, 2020, Preparation of CuS/polyvinyl alcohol-chitosan nanocomposites with photocatalysis activity and antibacterial behavior against G+/G− bacteria, Int. J. Biol. Macromol., 155, 36, 10.1016/j.ijbiomac.2020.03.077 · DOI
- Yang, 2020, Biosynthesis of nano bimetallic Ag/Pt alloy from Crocus sativus L. extract: biological efficacy and catalytic activity, J. Photochem. Photobiol. B Biol., 212, 10.1016/j.jphotobiol.2020.112025 · DOI
- Huang, 2020, Synthesis of Co3S4-SnO2/polyvinylpyrrolidone-cellulose heterojunction as highly performance catalyst for photocatalytic and antimicrobial properties under ultra-violet irradiation, Int. J. Biol. Macromol., 162, 220, 10.1016/j.ijbiomac.2020.06.092 · DOI
- Wang, 2020, Fabrication and structural of the Ag2S-MgO/graphene oxide nanocomposites with high photocatalysis and antimicrobial activities, J. Photochem. Photobiol. B Biol., 207, 111882, 10.1016/j.jphotobiol.2020.111882 · DOI
- Gupta, 2014, A novel magnetic Fe@Au core–shell nanoparticles anchored graphene oxide recyclable nanocatalyst for the reduction of nitrophenol compounds, Water Res., 48, 210, 10.1016/j.watres.2013.09.027 · DOI
- Rajendran, 2016, Ce3+-ion-induced visible-light photocatalytic degradation and electrochemical activity of ZnO/CeO2 nanocomposite, Sci. Rep., 6, 31641, 10.1038/srep31641 · DOI
- Saleh, 2011, Functionalization of tungsten oxide into MWCNT and its application for sunlight-induced degradation of rhodamine B, J. Colloid Interface Sci., 362, 337, 10.1016/j.jcis.2011.06.081 · DOI
- Saravanan, 2013, Comparative study on photocatalytic activity of ZnO prepared by different methods, J. Mol. Liq., 181, 133, 10.1016/j.molliq.2013.02.023 · DOI
- Devaraj, 2016, Fabrication of novel shape Cu and Cu/Cu2O nanoparticles modified electrode for the determination of dopamine and paracetamol, J. Mol. Liq., 221, 930, 10.1016/j.molliq.2016.06.028 · DOI
- Saravanan, 2013, Enhanced photocatalytic activity of ZnO/CuO nanocomposite for the degradation of textile dye on visible light illumination, Mater. Sci. Eng. C, 33, 91, 10.1016/j.msec.2012.08.011 · DOI
- Gupta, 2015, Bioadsorbents for remediation of heavy metals: current status and their future prospects, Environ. Eng. Res., 20, 1, 10.4491/eer.2015.018 · DOI
- Suhas, 2016, Cellulose: a review as natural, modified and activated carbon adsorbent, Bioresour. Technol., 216, 1066, 10.1016/j.biortech.2016.05.106 · DOI
- Gupta, 2013, Chromium removal from water by activated carbon developed from waste rubber tires, Environ. Sci. Pollut. Res., 20, 1261, 10.1007/s11356-012-0950-9 · DOI · Paper page
- Leal, 2018, Textile wastewater treatment using low-cost adsorbent aiming the water reuse in dyeing process, J. Environ. Chem. Eng., 6, 2705, 10.1016/j.jece.2018.04.008 · DOI
- Crini, 2019, Conventional and non-conventional adsorbents for wastewater treatment, Environ. Chem. Lett., 17, 195, 10.1007/s10311-018-0786-8 · DOI
- Gupta, 2013, Sorption of pollutants by porous carbon, carbon nanotubes and fullerene—an overview, Environ. Sci. Pollut. Res., 20, 2828, 10.1007/s11356-013-1524-1 · DOI
- Falade, 2017, Peroxidase production and ligninolytic potentials of fresh water bacteria Raoultella ornithinolytica and Ensifer adhaerens, Biotechnol. Rep. (Amst), 16, 12, 10.1016/j.btre.2017.10.001 · DOI
- Majeke, 2020, Synergistic codon optimization and bioreactor cultivation toward enhanced secretion of fungal lignin peroxidase in Pichia pastoris: enzymatic valorization of technical (industrial) lignins, Enzyme Microb. Technol., 139, 10.1016/j.enzmictec.2020.109593 · DOI
- Kapich, 2010, Oxidizability of unsaturated fatty acids and of a non-phenolic lignin structure in the manganese peroxidase-dependent lipid peroxidation system, Enzyme Microb. Technol., 46, 136, 10.1016/j.enzmictec.2009.09.014 · DOI
- Seo, 2018, In silico-designed lignin peroxidase from Phanerochaete chrysosporium shows enhanced acid stability for depolymerization of lignin, Biotechnol. Biofuels, 11, 1
- Kirk, 1987, Enzymatic “combustion”: the microbial degradation of lignin, Annu. Rev. Microbiol., 41, 465, 10.1146/annurev.mi.41.100187.002341 · DOI
- Kent Kirk, 1990, [27] Lignin peroxidase from fungi: Phanerochaete chrysosporium, 159, 10.1016/0076-6879(90)88029-A · DOI
- Hirai, 2005, Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624, FEMS Microbiol. Lett., 246, 19, 10.1016/j.femsle.2005.03.032 · DOI
- Johansson, 1993, Isozymes of lignin peroxidase and manganese (II) peroxidase from the white-rot basidiomycete Trametes versicolor: II. Partial sequences, peptide maps, and amino acid and carbohydrate compositions, Biophysics, 300, 57
- Sugiura, 2009, Cloning and homologous expression of novel lignin peroxidase genes in the white-rot fungus Phanerochaete sordida YK-624, Biotechnol. Biochem., 73, 1793, 10.1271/bbb.90152 · DOI
- Moilanen, 1996, Manganese and malonate are individual regulators for the production of lignin and manganese peroxidase isozymes and in the degradation of lignin by Phlebia radiata, Biotechnology, 45, 792
- Vares, 1994, Secretion of ligninolytic enzymes and mineralization of 14C-ring-labelled synthetic lignin by three Phlebia tremellosa strains, E. Microbiol., 60, 569
- Hatakka, 1994, Lignin-modifying enzymes from selected white-rot fungi: production and role from in lignin degradation, FEMS Microbiol. Rev., 13, 125, 10.1111/j.1574-6976.1994.tb00039.x · DOI
- Sarkanen, 1991, Lignin peroxidase: toward a clarification of its role in vivo, J. J. B. C., 266, 3636
- Baciocchi, 2001, Oxidation of non-phenolic β-O-aryl-lignin model dimers catalysed by lignin peroxidase. Comparison with the oxidation induced by potassium 12-tungstocobalt(III)ate, J. Chem. Soc. Perkin Trans., 2, 1506, 10.1039/b101362i · DOI
- Pointing, 2001, Feasibility of bioremediation by white-rot fungi, Appl. Microbiol. Biotechnol., 57, 20
- Piontek, 1993, Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 Å resolution, FEBS Lett., 315, 119, 10.1016/0014-5793(93)81146-Q · DOI
- Martínez, 2002, Molecular biology and structure-function of lignin-degrading heme peroxidases, Enzym. Microb. Technol., 30, 425, 10.1016/S0141-0229(01)00521-X · DOI
- Khindaria, 1996, Stabilization of the veratryl alcohol cation radical by lignin peroxidase, Biochemistry, 35, 6418, 10.1021/bi9601666 · DOI
- Sharma, 2016, Chapter 2 - fruit and vegetable processing waste: renewable feed stocks for enzyme production, 23
- Mester, 2000, Oxidation mechanism of ligninolytic enzymes involved in the degradation of environmental pollutants, Int. Biodeterior. Biodegradation, 46, 51, 10.1016/S0964-8305(00)00071-8 · DOI
- Lee, 2019, Bacterial valorization of lignin: strains, enzymes, conversion pathways, Biosens. Perspect., 7
- Tien, 1988, Lignin peroxidase of Phanerochaete chrysosporium, 238, 10.1016/0076-6879(88)61025-1 · DOI
- Johjima, 1999, Direct interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium, Proc. Natl. Acad. Sci., 96, 1989, 10.1073/pnas.96.5.1989 · DOI
- Podgornik, 1999, Decolorization rate of dyes using lignin peroxidases of Phanerochaete chrysosporium, Chemosphere, 38, 1353, 10.1016/S0045-6535(98)00537-2 · DOI
- Min, 2015, A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and β-ether lignin dimer, Sci. Rep., 5, 8245, 10.1038/srep08245 · DOI
- Ayuso-Fernández, 2019, Peroxidase evolution in white-rot fungi follows wood lignin evolution in plants, Proc. Natl. Acad. Sci., 116, 17900, 10.1073/pnas.1905040116 · DOI
- Falade, 2017, Lignin peroxidase functionalities and prospective applications, MicrobiologyOpen, 6, 10.1002/mbo3.394 · DOI
- Zhong, 2015, Reduction of facial pigmentation of melasma by topical lignin peroxidase: a novel fast-acting skin-lightening agent, Exper. Ther. Med., 9, 341, 10.3892/etm.2014.2118 · DOI
- Draelos, 2015, A split-face evaluation of a novel pigment-lightening agent compared with no treatment and hydroquinone, J. Am. Acad. Dermatol., 72, 105, 10.1016/j.jaad.2014.09.011 · DOI
- Mauricio, 2011, A randomized and placebo‐controlled study to compare the skin‐lightening efficacy and safety of lignin peroxidase cream vs. 2% hydroquinone cream, J. Cosmet. Dermatol., 10, 253, 10.1111/j.1473-2165.2011.00581.x · DOI
- Sung, 2019, Recombinant lignin peroxidase-catalyzed decolorization of melanin using in-situ generated H2O2 for application in whitening cosmetics, Int. J. Biol. Macromol., 136, 20, 10.1016/j.ijbiomac.2019.06.026 · DOI
- Bilal, 2020, Ligninolytic enzymes mediated ligninolysis: an untapped biocatalytic potential to deconstruct lignocellulosic molecules in a sustainable manner, Cat. Lett., 150, 524, 10.1007/s10562-019-03096-9 · DOI
- Bilal, 2019, Lignin peroxidase immobilization on Ca-alginate beads and its dye degradation performance in a packed bed reactor system, Biocat. Agri. Biotechnol., 20
- Bilal, 2021, Ligninolysis Potential of Ligninolytic Enzymes: A Green and Sustainable Approach to Bio-transform Lignocellulosic Biomass into High-Value Entities, 99, 151, 10.1007/698_2020_631 · DOI
- Holzbaur, 1988, Structure and regulation of a lignin peroxidase gene from Phanerochaete chrysosporium, Biochem. Biophys. Res. Commun., 155, 626, 10.1016/S0006-291X(88)80541-2 · DOI
- Saldarriaga-Hernández, 2020, Biotransformation of lignocellulosic biomass into industrially relevant products with the aid of fungi-derived lignocellulolytic enzymes, Int. J. Biol. Macromol., 161, 1099, 10.1016/j.ijbiomac.2020.06.047 · DOI
- Poulos, 1993, Crystallographic refinement of lignin peroxidase at 2 A, J. Biol. Chem., 268, 4429, 10.1016/S0021-9258(18)53627-9 · DOI
- Edwards, 1993, Crystal structure of lignin peroxidase, Proc. Natl. Acad. Sci., 90, 750, 10.1073/pnas.90.2.750 · DOI
- Kersten, 1990, Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes, Biochem. J., 268, 475, 10.1042/bj2680475 · DOI
- Niku-Paavola, 1988, Ligninolytic enzymes of the white-rot fungus Phlebia radiata, Biochem. J., 254, 877, 10.1042/bj2540877 · DOI
- Arora, 2001, Comparison of two assay procedures for lignin peroxidase, Enzym. Microb. Technol., 28, 602, 10.1016/S0141-0229(01)00302-7 · DOI
- Manimekalai, 2000, Removal of hazardous compounds by lignin peroxidase from Phanerochaete chrysosporium, Bioprocess Eng., 22, 29, 10.1007/PL00009096 · DOI
- Ayed, 2005, Involvement of lignin peroxidase in the decolourization of black olive mill wastewaters by Geotrichum candidum, Lett. Appl. Microbiol., 40, 7, 10.1111/j.1472-765X.2004.01626.x · DOI
- Christian, 2005, Mediator role of veratryl alcohol in the lignin peroxidase-catalyzed oxidative decolorization of Remazol Brilliant Blue R, Enzym. Microb. Technol., 36, 327, 10.1016/j.enzmictec.2004.09.006 · DOI
- Alam, 2009, Optimization of decolorization of methylene blue by lignin peroxidase enzyme produced from sewage sludge with Phanerocheate chrysosporium, J. Hazard. Mater., 162, 708, 10.1016/j.jhazmat.2008.05.085 · DOI
- Ma, 2015, Catalytic oxidation of biorefinery lignin to value‐added chemicals to support sustainable biofuel production, ChemSusChem, 8, 24, 10.1002/cssc.201402503 · DOI
- Sharma, 2019, Biological pretreatment of lignocellulosic biomass for biofuels and bioproducts: an overview, Waste Biomass Valor., 10, 235, 10.1007/s12649-017-0059-y · DOI · Paper page
- Shin, 2019, Studies of advanced lignin valorization based on various types of lignolytic enzymes and microbes, Bioresour. Technol., 289, 121728, 10.1016/j.biortech.2019.121728 · DOI
- Binod, 2019, Enzymes for second generation biofuels: recent developments and future perspectives, Bioresour. Technol. Rep., 5, 317, 10.1016/j.biteb.2018.06.005 · DOI
- Kondo, 2014, Biodegradation, bioethanol production from alkaline-pretreated sugarcane bagasse by consolidated bioprocessing using Phlebia sp. MG-60, Int. Biodeterior. Biodegradation, 88, 62, 10.1016/j.ibiod.2013.12.008 · DOI
- López-Abelairas, 2013, Optimisation of the biological pretreatment of wheat straw with white-rot fungi for ethanol production, Bioprocess Biosyst. Eng., 36, 1251, 10.1007/s00449-012-0869-z · DOI
- Hammel, 1993, Ligninolysis by a purified lignin peroxidase, J. Biol. Chem., 268, 12274, 10.1016/S0021-9258(18)31385-1 · DOI
- Valli, 1990, Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: role of veratryl alcohol in lignin biodegradation, Biochemistry, 29, 8535, 10.1021/bi00489a005 · DOI
- Vazquez-Duhalt, 1994, Lignin peroxidase oxidation of aromatic compounds in systems containing organic solvents, Appl. Environ. Microbiol., 60, 459, 10.1128/aem.60.2.459-466.1994 · DOI
- Wong, 2009, Biotechnology, structure and action mechanism of ligninolytic enzymes, Appl. Biochem. Biotechnol., 157, 174, 10.1007/s12010-008-8279-z · DOI
- Sigoillot, 2012, Fungal strategies for lignin degradation, 263, 10.1016/B978-0-12-416023-1.00008-2 · DOI
- Edwards, 1993, Crystal structure of lignin peroxidase, Proc. Natl. Acad. Sci. U. S. A., 90, 750, 10.1073/pnas.90.2.750 · DOI
- Poulos, 1993, Crystallographic refinement of lignin peroxidase at 2 A, J. Biol. Chem., 268, 4429, 10.1016/S0021-9258(18)53627-9 · DOI
- Biko, 2020, Microbial lignin peroxidases: applications, production challenges and future perspectives, Enzyme Microb. Technol., 141, 10.1016/j.enzmictec.2020.109669 · DOI
- Nayana, 2020, Dataset on optimization of lignin peroxidase production by Endomelanconiopsis sp. under submerged fermentation using one factor at a time approach, Data Brief, 29, 10.1016/j.dib.2020.105244 · DOI
- Parveen, 2020, Lignin peroxidase-based cross-linked enzyme aggregates (LiP-CLEAs) as robust biocatalytic materials for mitigation of textile dyes-contaminated aqueous solution, Environ. Technol. Innov., 101226
- Riyadi, 2020, Enzymatic and genetic characterization of lignin depolymerization by Streptomyces sp. S6 isolated from a tropical environment, Sci. Rep., 10, 7813, 10.1038/s41598-020-64817-4 · DOI
- Falade, 2017, Peroxidase production and ligninolytic potentials of fresh water bacteria Raoultella ornithinolytica and Ensifer adhaerens, Biotechnol. Rep., 16, 12, 10.1016/j.btre.2017.10.001 · DOI
- van Bloois, 2010, A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily, Appl. Microbiol. Biotechnol., 86, 1419, 10.1007/s00253-009-2369-x · DOI · Paper page
- Kirby, 2005, Actinomycetes and lignin degradation, Adv. Appl. Microbiol., 58, 125, 10.1016/S0065-2164(05)58004-3 · DOI
- Mane, 2008, Degradation of textile dye reactive navy–blue Rx (Reactive blue–59) by an isolated Actinomycete Streptomyces krainskii SUK–5, Malay. J. Microbiol., 4, 1
- Bonnarme, 1990, Mn (II) regulation of lignin peroxidases and manganese-dependent peroxidases from lignin-degrading white rot fungi, Appl. Environ. Microbiol., 56, 210, 10.1128/aem.56.1.210-217.1990 · DOI
- Hakala, 2006, Differential regulation of manganese peroxidases and characterization of two variable MnP encoding genes in the white-rot fungus Physisporinus rivulosus, Appl. Microbiol. Biotechnol., 73, 839, 10.1007/s00253-006-0541-0 · DOI
- Jiménez-Tobon, 2003, In situ localization of manganese peroxidase production in mycelial pellets of Phanerochaete chrysosporium, Microbiology, 149, 3121, 10.1099/mic.0.26451-0 · DOI
- Kamitsuji, 2004, Production and induction of manganese peroxidase isozymes in a white-rot fungus Pleurotus ostreatus, Appl. Microbiol. Biotechnol., 65, 287, 10.1007/s00253-003-1543-9 · DOI
- Lankinen, 2005, Manganese peroxidase of Agaricus bisporus: grain bran-promoted production and gene characterization, Appl. Microbiol. Biotechnol., 66, 401, 10.1007/s00253-004-1731-2 · DOI
- Conesa, 2000, Studies on the production of fungal peroxidases in Aspergillus niger, Appl. Environ. Microbiol., 66, 3016, 10.1128/AEM.66.7.3016-3023.2000 · DOI
- Irie, 2001, Homologous expression of recombinant manganese peroxidase genes in ligninolytic fungus Pleurotus ostreatus, Appl. Microbiol. Biotechnol., 55, 566, 10.1007/s002530000540 · DOI
- R. Datta, A. Kelkar, D. Baraniya, A. Molaei, A. Moulick, R.S. Meena, P.J.S. Formanek, Enzymatic degradation of lignin in soil: a review, Sustainability, 9(7) (2017) 1163. · DOI
- Tuomela, 2000, Biodegradation of lignin in a compost environment: a review, Bioresour. Technol., 72, 169, 10.1016/S0960-8524(99)00104-2 · DOI
- Gonçalves, 2020, Bioprospecting microbial diversity for lignin valorization: dry and wet screening methods, Front. Microbiol., 11, 1081, 10.3389/fmicb.2020.01081 · DOI
- Falade, 2019, Biochemical and molecular characterization of a novel dye-decolourizing peroxidase from Raoultella ornithinolytica OKOH-1, Int. J. Biol. Macromol., 121, 454, 10.1016/j.ijbiomac.2018.10.045 · DOI
- Tian, 2016, Isolation of bacterial strains able to metabolize lignin and lignin-related compounds, Lett. Appl. Microbiol., 63, 30, 10.1111/lam.12581 · DOI
- Vignali, 2018, Characterization and use of a bacterial lignin peroxidase with an improved manganese-oxidative activity, Appl. Microbiol. Biotechnol., 102, 10579, 10.1007/s00253-018-9409-3 · DOI
- Zhou, 2017, Screening and identification of lignin-degrading bacteria in termite gut and the construction of LiP-expressing recombinant Lactococcus lactis, Microb. Pathog., 112, 63, 10.1016/j.micpath.2017.09.047 · DOI
- de Gonzalo, 2016, Bacterial enzymes involved in lignin degradation, J. Biotechnol., 236, 110, 10.1016/j.jbiotec.2016.08.011 · DOI
- Tien, 1983, Lignin-degrading enzyme from the hymenomycete Phanerochaete chrysosporium Burds, Science, 221, 661, 10.1126/science.221.4611.661 · DOI
- Johansson, 1993, Isozymes of lignin peroxidase and manganese (II) peroxidase from the white-rot basidiomycete Trametes versicolor: I. Isolation of enzyme forms and characterization of physical and catalytic properties, Arch. Biochem. Biophys., 300, 49, 10.1006/abbi.1993.1007 · DOI
- Aarti, 2015, Lignin degradation: a microbial approach, Indian J. Biol. Sci., 1, 119
- Dashtban, 2010, Fungal biodegradation and enzymatic modification of lignin, Int J Biochem Mol Biol, 1, 36
- Blodig, 2001, Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism, J. Mol. Biol., 305, 851, 10.1006/jmbi.2000.4346 · DOI
- Renganathan, 1986, Role of molecular oxygen in lignin peroxidase reactions, Arch. Biochem. Biophys., 246, 155, 10.1016/0003-9861(86)90459-5 · DOI
- Andrawis, 1988, Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium, J. Biol. Chem., 263, 1195, 10.1016/S0021-9258(19)57285-4 · DOI
- Marquez, 1988, Spectroscopic and kinetic properties of the oxidized intermediates of lignin peroxidase from Phanerochaete chrysosporium, J. Biol. Chem., 263, 10549, 10.1016/S0021-9258(18)38004-9 · DOI
- Behere, 1985, Unique cyanide nitrogen-15 nuclear magnetic resonance chemical shift values for cyano-peroxidase complexes. Relevance to the heme active-site structure and mechanism of peroxide activation, Biochim. Biophys. Acta (BBA)-Prot. Struct. Mol. Enzymol., 832, 319, 10.1016/0167-4838(85)90265-1 · DOI
- Chance, 1986, Cytochrome c peroxidase compound ES is identical with horseradish peroxidase compound I in iron-ligand distances, Biochemistry, 25, 1266, 10.1021/bi00354a011 · DOI
- Blodig, 2001, Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism, J. Mol. Biol., 305, 851, 10.1006/jmbi.2000.4346 · DOI
- Blodig, 1999, Evidence from spin-trapping for a transient radical on tryptophan residue 171 of lignin peroxidase, J. A. Biophys., 370, 86, 10.1006/abbi.1999.1365 · DOI
- Tien, 1986, Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds, J. Biol. Chem., 261, 1687, 10.1016/S0021-9258(17)35994-X · DOI
- Ator, 1987, Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase, J. Biol. Chem., 262, 1542, 10.1016/S0021-9258(19)75669-5 · DOI
- Choinowski, 1999, The crystal structure of lignin peroxidase at 1.70 Å resolution reveals a hydroxy group on the Cβ of tryptophan 171: a novel radical site formed during the redox cycle, J. Mol. Biol., 286, 809, 10.1006/jmbi.1998.2507 · DOI
- Doyle, 1998, Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis, Biochemistry, 37, 15097, 10.1021/bi981633h · DOI
- Timofeevski, 2000, Substrate specificity of lignin peroxidase and a S168W variant of manganese peroxidase, Arch. Biochem. Biophys., 373, 147, 10.1006/abbi.1999.1562 · DOI
- Sollewijn Gelpke, 2002, Lignin peroxidase oxidation of veratryl alcohol: effects of the mutants H82A, Q222A, W171A, and F267L, Biochemistry, 41, 3498, 10.1021/bi011930d · DOI
- Johjima, 2002, Veratryl alcohol binding sites of lignin peroxidase from Phanerochaete chrysosporium, J. Mol. Catal. B Enzym., 17, 49, 10.1016/S1381-1177(01)00079-0 · DOI
- Francesca Gerini, 2003, Molecular dynamics simulations of lignin peroxidase in solution, Biophys. J., 84, 3883, 10.1016/S0006-3495(03)75116-9 · DOI
- Wariishi, 1989, Lignin peroxidase compound III: formation, inactivation, and conversion to the native enzyme, FEBS Lett., 243, 165, 10.1016/0014-5793(89)80122-X · DOI
- Cai, 1992, Kinetic studies on the formation and decomposition of compounds II and III. Reactions of lignin peroxidase with H2O2, J. Biol. Chem., 267, 11149, 10.1016/S0021-9258(19)49888-8 · DOI
- Barr, 1994, Conversion of lignin peroxidase compound III to active enzyme by cation radicals, Arch. Biochem. Biophys., 312, 511, 10.1006/abbi.1994.1339 · DOI
- Janusz, 2017, Lignin degradation: microorganisms, enzymes involved, genomes analysis and evolution, FEMS Microbiol. Rev., 41, 941, 10.1093/femsre/fux049 · DOI · Paper page
- Abdel-Hamid, 2013, Insights into lignin degradation and its potential industrial applications, 1, 10.1016/B978-0-12-407679-2.00001-6 · DOI
- Falade, 2017, Lignin peroxidase functionalities and prospective applications, MicrobiologyOpen, 6, 10.1002/mbo3.394 · DOI
- Kirk, 1986, Ligninase of Phanerochaete chrysosporium. Mechanism of its degradation of the non-phenolic arylglycerol β-aryl ether substructure of lignin, Biochem. J., 236, 279, 10.1042/bj2360279 · DOI
- Miki, 1986, Mechanism of beta-aryl ether dimeric lignin model compound oxidation by lignin peroxidase by Phanerochaete chrysosporium, Biochemistry, 25, 4790, 10.1021/bi00365a011 · DOI
- Furukawa, 2014, Microbial enzyme systems for lignin degradation and their transcriptional regulation, Front. Biol., 9, 448, 10.1007/s11515-014-1336-9 · DOI
- Paliwal, 2015, Evaluating the potential of immobilized bacterial consortium for black liquor biodegradation, Environ. Sci. Pollut. Res., 22, 6842, 10.1007/s11356-014-3872-x · DOI
- Baciocchi, 2001, Isotope‐effect profiles in the oxidative N‐demethylation of N,N‐dimethylanilines catalysed by lignin peroxidase and a chemical model, Eur. J. Org. Chem., 2001, 2305, 10.1002/1099-0690(200106)2001:12<2305::AID-EJOC2305>3.0.CO;2-E · DOI
- Harvey, 1990, Oxidation of phenolic compounds by ligninase, J. Biotechnol., 13, 169, 10.1016/0168-1656(90)90102-H · DOI
- Ivancich, 2001, Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes, Biochemistry, 40, 6860, 10.1021/bi002826j · DOI
- Ghaedi, 2015, Modeling of competitive ultrasonic assisted removal of the dyes — Methylene blue and Safranin-O using Fe3O4 nanoparticles, Chem. Eng. J., 268, 28, 10.1016/j.cej.2014.12.090 · DOI
- Dil, 2016, Modeling of quaternary dyes adsorption onto ZnO–NR–AC artificial neural network: analysis by derivative spectrophotometry, J. Ind. Eng. Chem., 34, 186, 10.1016/j.jiec.2015.11.010 · DOI
- Gupta, 1997, Process development for the removal of zinc and cadmium from wastewater using slag—a blast furnace waste material, Sep. Sci. Technol., 32, 2883, 10.1080/01496399708002227 · DOI
- Saravanan, 2014, Preparation and characterization of V2O5/ZnO nanocomposite system for photocatalytic application, J. Mol. Liq., 198, 409, 10.1016/j.molliq.2014.07.030 · DOI
- Gupta, 2014, Potential of activated carbon from waste rubber tire for the adsorption of phenolics: effect of pre-treatment conditions, J. Colloid Interface Sci., 417, 420, 10.1016/j.jcis.2013.11.067 · DOI
- Saleh, 2012, Photo-catalyzed degradation of hazardous dye methyl orange by use of a composite catalyst consisting of multi-walled carbon nanotubes and titanium dioxide, J. Colloid Interface Sci., 371, 101, 10.1016/j.jcis.2011.12.038 · DOI
- Khani, 2010, Multi-walled carbon nanotubes-ionic liquid-carbon paste electrode as a super selectivity sensor: application to potentiometric monitoring of mercury ion(II), J. Hazard. Mater., 183, 402, 10.1016/j.jhazmat.2010.07.039 · DOI
- Saravanan, 2015, ZnO/Ag/CdO nanocomposite for visible light-induced photocatalytic degradation of industrial textile effluents, J. Colloid Interface Sci., 452, 126, 10.1016/j.jcis.2015.04.035 · DOI
- Ahmaruzzaman, 2011, Rice husk and its ash as low-cost adsorbents in water and wastewater treatment, Ind. Eng. Chem. Res., 50, 13589, 10.1021/ie201477c · DOI
- Adler, 1977, Technology, lignin chemistry—past, present and future, Wood Sci. Technol., 11, 169, 10.1007/BF00365615 · DOI
- Schoemaker, 1985, On the mechanism of enzymatic lignin breakdown, FEBS Lett., 183, 7, 10.1016/0014-5793(85)80942-X · DOI
- Tien, 1984, Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase, Proc. Natl. Acad. Sci., 81, 2280, 10.1073/pnas.81.8.2280 · DOI
- Kim, 1989, Constitutive expression of nitrogenase system in Klebsiella oxytoca by gene targeting mutation to the chromosomal nifLA operon, J. Biotechnol., 10, 293, 10.1016/0168-1656(89)90073-4 · DOI
- Dodson, 1987, Production and properties of an extracellular peroxidase from Coriolus versicolor which catalyses Cα-Cβ cleavage in a lignin model compound, FEMS Microbiol. Lett., 42, 17
- Banci, 1999, Lignin and Mn peroxidase-catalyzed oxidation of phenolic lignin oligomers, Biochemistry, 38, 3205, 10.1021/bi982139g · DOI
- Galau, 1977, Significance of rare mRNA sequences in liver, Arch. Biochem. Biophys., 179, 584, 10.1016/0003-9861(77)90147-3 · DOI
- Hammel, 1985, Mechanism of oxidative C alpha-C beta cleavage of a lignin model dimer by Phanerochaete chrysosporium ligninase. Stoichiometry and involvement of free radicals, J. Biol. Chem., 260, 8348, 10.1016/S0021-9258(17)39479-6 · DOI
- Hammel, 1986, Oxidation of polycyclic aromatic hydrocarbons and dibenzo [p]-dioxins by Phanerochaete chrysosporium ligninase, J. Biol. Chem., 261, 16948, 10.1016/S0021-9258(19)75982-1 · DOI
- Harvey, 1985, Single-electron transfer processes and the reaction mechanism of enzymic degradation of lignin, FEBS Lett., 183, 13, 10.1016/0014-5793(85)80943-1 · DOI
- Wariishi, 1991, Reactions of lignin peroxidase compounds I and II with veratryl alcohol. Transient-state kinetic characterization, J. Biol. Chem., 266, 20694, 10.1016/S0021-9258(18)54764-5 · DOI
- Romero, 2019, Binding and catalytic mechanisms of veratryl alcohol oxidation by lignin peroxidase: a theoretical and experimental study, Comput. Struct. Biotechnol. J., 17, 1066, 10.1016/j.csbj.2019.07.002 · DOI
- Khindaria, 1995, Veratryl alcohol oxidation by lignin peroxidase, Biochemistry, 34, 16860, 10.1021/bi00051a037 · DOI
- Abdelaziz, 2016, Biological valorization of low molecular weight lignin, Biotechnol. Adv., 34, 1318, 10.1016/j.biotechadv.2016.10.001 · DOI
- Lundell, 1993, Lignin peroxidase L3 from Phlebia rediata: pre‐steady‐state and steady‐state studies with veratryl alcohol and a non‐phenolic lignin model compound 1‐(3,4‐dimethoxyphenyl)‐2‐(2‐methoxyphenoxy) propane‐1,3‐diol, Eur. J. Biochem., 211, 391, 10.1111/j.1432-1033.1993.tb17562.x · DOI
- Baciocchi, 2002, The mediation of veratryl alcohol in oxidations promoted by lignin peroxidase: the lifetime of veratryl alcohol radical cation, Biochem. Biophys. Res. Commun., 293, 832, 10.1016/S0006-291X(02)00306-6 · DOI
- Bilal, 2019, Emerging contaminants of high concern and their enzyme-assisted biodegradation — a review, Environ. Int., 124, 336, 10.1016/j.envint.2019.01.011 · DOI · Paper page
- Chatha, 2017, Enzyme-based solutions for textile processing and dye contaminant biodegradation—a review, Environ. Sci. Pollut. Res., 24, 14005, 10.1007/s11356-017-8998-1 · DOI
- Bilal, 2019, Agarose-chitosan hydrogel-immobilized horseradish peroxidase with sustainable bio-catalytic and dye degradation properties, Int. J. Biol. Macromol., 124, 742, 10.1016/j.ijbiomac.2018.11.220 · DOI
- da Silva Santos, 2018, Chronic effects of carbamazepine on zebrafish: behavioral, reproductive and biochemical endpoints, Ecotoxicol. Environ. Saf., 164, 297, 10.1016/j.ecoenv.2018.08.015 · DOI
- Shao, 2019, Toxicity of 10 organic micropollutants and their mixture: implications for aquatic risk assessment, Sci. Total Environ., 666, 1273, 10.1016/j.scitotenv.2019.02.047 · DOI
- Stamm, 2016, Chapter four — Unravelling the impacts of micropollutants in aquatic ecosystems: interdisciplinary studies at the interface of large-scale ecology, 183, 10.1016/bs.aecr.2016.07.002 · DOI
- Ngweme, 2021, Occurrence of organic micropollutants and human health risk assessment based on consumption of Amaranthus viridis, Kinshasa in the Democratic Republic of the Congo, Sci. Total Environ., 754, 142175, 10.1016/j.scitotenv.2020.142175 · DOI
- Ben, 2019, Human health risk assessment of antibiotic resistance associated with antibiotic residues in the environment: a review, Environ. Res., 169, 483, 10.1016/j.envres.2018.11.040 · DOI
- H. Ren, R. Tröger, L. Ahrens, K. Wiberg, D. Yin, Screening of organic micropollutants in raw and drinking water in the Yangtze River Delta, China. Environ. Sci. Eur. 32(1) (2020) 67. · DOI
- Lim, 2020, Removal of organic micropollutants in anaerobic membrane bioreactors in wastewater treatment: critical review, Environ. Sci. Water Res. Technol., 6, 1230, 10.1039/C9EW01058K · DOI
- Varga, 2019, Enzymatic treatment and subsequent toxicity of organic micropollutants using oxidoreductases — a review, J. Clean. Prod., 221, 306, 10.1016/j.jclepro.2019.02.135 · DOI
- Ullah, 2018, Cypermethrin induced toxicities in fish and adverse health outcomes: its prevention and control measure adaptation, J. Environ. Manag., 206, 863, 10.1016/j.jenvman.2017.11.076 · DOI
- Rezg, 2014, Bisphenol A and human chronic diseases: current evidences, possible mechanisms, and future perspectives, Environ. Int., 64, 83, 10.1016/j.envint.2013.12.007 · DOI
- Bilal, 2018, “Smart” chemistry and its application in peroxidase immobilization using different support materials, Int. J. Biol. Macromol., 119, 278, 10.1016/j.ijbiomac.2018.07.134 · DOI
- Bilal, 2019, Multi-point enzyme immobilization, surface chemistry, and novel platforms: a paradigm shift in biocatalyst design, Crit. Rev. Biotechnol., 39, 202, 10.1080/07388551.2018.1531822 · DOI
- Bilal, 2017, Immobilized ligninolytic enzymes: an innovative and environmental responsive technology to tackle dye-based industrial pollutants — a review, Sci. Total Environ., 576, 646, 10.1016/j.scitotenv.2016.10.137 · DOI · Paper page
- Tien, 1984, Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase, Proc. Natl. Acad. Sci., 81, 2280, 10.1073/pnas.81.8.2280 · DOI
- Tien, 1984, Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase, Proc. Natl. Acad. Sci. U. S. A., 81, 2280, 10.1073/pnas.81.8.2280 · DOI
- Hu, 2013, Mesoporous silicas synthesis and application for lignin peroxidase immobilization by covalent binding method, J. Environ. Sci. (China), 25, 181, 10.1016/S1001-0742(12)60008-4 · DOI
- X. Wang, B. Yao, X. Su, Linking enzymatic oxidative degradation of lignin to organics detoxification, Int. J. Mol. Sci. 19(11) (2018) 3373. · DOI
- Yadav, 2017, The role of peroxidase in the enzymatic oxidation of phenolic compounds to quinones from Luffa aegyptiaca (gourd) fruit juice, Green Chem. Lett. Rev., 10, 154, 10.1080/17518253.2017.1336575 · DOI
- Burakov, 2018, Adsorption of heavy metals on conventional and nanostructured materials for wastewater treatment purposes: a review, Ecotoxicol. Environ. Saf., 148, 702, 10.1016/j.ecoenv.2017.11.034 · DOI · Paper page
- Gupta, 2011, Removal of the hazardous dye—tartrazine by photodegradation on titanium dioxide surface, Mater. Sci. Eng. C, 31, 1062, 10.1016/j.msec.2011.03.006 · DOI
- Saravanan, 2016, Conducting PANI stimulated ZnO system for visible light photocatalytic degradation of coloured dyes, J. Mol. Liq., 221, 1029, 10.1016/j.molliq.2016.06.074 · DOI
- Gupta, 2002, Removal of lindane and malathion from wastewater using bagasse fly ash—a sugar industry waste, Water Res., 36, 2483, 10.1016/S0043-1354(01)00474-2 · DOI
- Asfaram, 2015, Removal of basic dye Auramine-O by ZnS:Cu nanoparticles loaded on activated carbon: optimization of parameters using response surface methodology with central composite design, RSC Adv., 5, 18438, 10.1039/C4RA15637D · DOI
- Saravanan, 2014, Visible light degradation of textile effluent using novel catalyst ZnO/γ-Mn2O3, J. Taiwan Inst. Chem. Eng., 45, 1910, 10.1016/j.jtice.2013.12.021 · DOI
- Nekouei, 2015, Kinetic, thermodynamic and isotherm studies for acid blue 129 removal from liquids using copper oxide nanoparticle-modified activated carbon as a novel adsorbent, J. Mol. Liq., 201, 124, 10.1016/j.molliq.2014.09.027 · DOI
- Mittal, 2010, Removal and recovery of Chrysoidine Y from aqueous solutions by waste materials, J. Colloid Interface Sci., 344, 497, 10.1016/j.jcis.2010.01.007 · DOI
- Saravanan, 2013, Visible light induced degradation of methylene blue using CeO2/V2O5 and CeO2/CuO catalysts, Mater. Sci. Eng. C, 33, 4725, 10.1016/j.msec.2013.07.034 · DOI
- Saravanan, 2013, ZnO/Ag nanocomposite: an efficient catalyst for degradation studies of textile effluents under visible light, Mater. Sci. Eng. C, 33, 2235, 10.1016/j.msec.2013.01.046 · DOI
- Saravanan, 2013, Synthesis, characterization and photocatalytic activity of novel Hg doped ZnO nanorods prepared by thermal decomposition method, J. Mol. Liq., 178, 88, 10.1016/j.molliq.2012.11.012 · DOI
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Narayanan, M., Ali, S. S., & El-Sheekh, M. (2023) · Journal of Environmental Management · doi:10.1016/j.jenvman.2023.117532 · Cited by 221
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Metadata
- Authors
- Singh, A. K., Bilal, M., Iqbal, H. M. N., & Raj, A.
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 177
- Pages
- 58-82
- ISSN
- 0141-8130
- Cited by
- 116
- References
- 8
- Language
- en
- Licence
- Funders
- Sistema Nacional de Investigadores (735340)
- University Grants Commission
- Academy of Scientific and Innovative Research
- Consejo Nacional de Ciencia y Tecnología
- Department of Biotechnology, Ministry of Science and Technology, India (BT/PR20460/BCE/8/1386/2016)
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