Abstract
In response to increased global industrialization and environmental pollution by toxic xenobiotics, foreign substances transgressing an ecosystem or a living organism, the need for new cost-effective decontamination and remediation methods is greater than ever. This chapter focuses on the role and potential application of fungal enzymes and their respective mechanisms in the bioremediation of various xenobiotics. Fungal bioremediatory enzymes exhibit uniquely broad substrate ranges. Among the enzymes examined herein are laccases (LAC), lignin peroxidases (LiP), manganese peroxidases (MnP), versatile peroxidases (VP), cytochrome P450 monooxygenases (P450), and unspecific peroxygenases (UPO). Each of these enzymes has been demonstrated to transform and remediate toxic xenobiotics to less hazardous or bioactive forms. However, there are nuanced considerations for each class of enzyme. Laccases and peroxidases each have their advantages and limitations; laccases can use molecular oxygen, while peroxidases require a supply of H2O2. On the other hand, peroxidases can function in a wider pH range and carry a high redox potential. P450s represent an incredibly promising and diverse superfamily of enzymes which remain to fully understood as is the case with UPOs. By isolating these enzymes and immobilizing them, the potential adverse effects of introducing a novel species into an already polluted and stressed environment are mitigated. Furthermore, while fungi are quite robust they are limited by environmental toxicity – a limitation that is overcome by employing isolated fungal enzymes. Enzymatic efficiency and longevity are, however, dependent on many variables such as pH, temperature, and environmental availability of various minerals and co-substrates. As a result, further investigation into fungal enzyme bioremediation and enzyme optimization is warranted to realize the tremendous biotechnical potential of these enzymes in the field of xenobiotic bioremediation. Genetic engineering for enzyme optimization and new enzyme immobilization approaches to generate stable and efficient enzyme-based detoxification systems are exciting prospects in development.
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References
Alcalde M, Bulter T, Zumarraga M, Garcia-Arellano H, Mencia M, Plou FJ, Ballesteros A (2005) Screening mutant libraries of fungal laccases in the presence of organic solvents. J Biomol Screen 10:624–631. https://doi.org/10.1177/1087057105277058
Alcalde M, Ferrer M, Plou FJ, Ballesteros A (2006) Environmental biocatalysis: from remediation with enzymes to novel green processes. Trends Biotechnol 24:281–287. https://doi.org/10.1016/j.tibtech.2006.04.002
Amitai G, Adani R, Sod-Moriah G, Rabinovitz I, Vincze A, Leader H, Chefetz B, Leibovitz-Persky L, Friesem D, Hadar Y (1998) Oxidative biodegradation of phosphorothiolates by fungal laccase. FEBS Lett 438:195–200. https://doi.org/10.1016/S0014-5793(98)01300-3
Ang EL, Zhao H, Obbard JP (2005) Recent advances in the bioremediation of persistent organic pollutants via biomolecular engineering. Enzym Microb Technol 37:487–496. https://doi.org/10.1016/j.enzmictec.2004.07.024
Antosova Z, Herkommerova K, Pichova I, Sychrova H (2018) Efficient secretion of three fungal laccases from Saccharomyces cerevisiae and their potential for decolorization of textile industry effluent-a comparative study. Biotechnol Prog 34:69–80. https://doi.org/10.1002/btpr.2559
Aracagok YD, Goker H, Cihangir N (2017) Biodegradation of micropollutant naproxen with a selected fungal strain and identification of metabolites. Z Naturforsch C 72:173–179. https://doi.org/10.1515/znc-2016-0162
Asgher M, Asad MJ, Bhatti HN, Legge RL (2007) Hyperactivation and thermostabilization of Phanerochaete chrysosporium lignin peroxidase by immobilization in xerogels. World J Microbiol Biotechnol 23:525–531. https://doi.org/10.1007/s11274-006-9255-9
Asgher M, Bhatti HN, Ashraf M, Legge RL (2008) Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system. Biodegradation 19:771–783. https://doi.org/10.1007/s10532-008-9185-3
Ayala M, Pickard MA, Vazquez-Duhalt R (2008) Fungal enzymes for environmental purposes, a molecular biology challenge. J Mol Microbiol Biotechnol 15:172–180. https://doi.org/10.1159/000121328
Balcazar-Lopez E, Mendez-Lorenzo LH, Batista-Garcia RA, Esquivel-Naranjo U, Ayala M, Kumar VV, Savary O, Cabana H, Herrera-Estrella A, Folch-Mallol JL (2016) Xenobiotic compounds degradation by heterologous expression of a Trametes Sanguineus Laccase in Trichoderma atroviride. PLoS One 11:e0147997. https://doi.org/10.1371/journal.pone.0147997
Bautista LF, Morales G, Sanz R (2015) Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by laccase from Trametes versicolor covalently immobilized on amino-functionalized SBA-15. Chemosphere 136:273–280. https://doi.org/10.1016/j.chemosphere.2015.05.071
Bilal M, Asgher M (2016) Enhanced catalytic potentiality of Ganoderma lucidum IBL-05 manganese peroxidase immobilized on sol-gel matrix. J Mol Catal B Enzym 128:82–93. https://doi.org/10.1016/j.molcatb.2016.03.013
Bilal M, Asgher M, Iqbal HM, Hu H, Zhang X (2017a) Bio-based degradation of emerging endocrine-disrupting and dye-based pollutants using cross-linked enzyme aggregates. Environ Sci Pollut Res Int 24:7035–7041. https://doi.org/10.1007/s11356-017-8369-y
Bilal M, Asgher M, Parra-Saldivar R, Hu H, Wang W, Zhang X, Iqbal HMN (2017b) Immobilized ligninolytic enzymes: an innovative and environmental responsive technology to tackle dye-based industrial pollutants – a review. Sci Total Environ 576:646–659. https://doi.org/10.1016/j.scitotenv.2016.10.137
Bogan BW, Schoenike B, Lamar RT, Cullen D (1996) Manganese peroxidase mRNA and enzyme activity levels during bioremediation of polycyclic aromatic hydrocarbon-contaminated soil with Phanerochaete chrysosporium. Appl Environ Microbiol 62:2381–2386. https://aem.asm.org/content/62/7/2381
Bollag JM (1992) Decontaminating soil with enzymes. Environ Sci Technol 26:1876–1881. https://doi.org/10.1021/es00034a002
Camarero S, Sarkar S, Ruiz-Duenas FJ, Martinez MJ, Martinez AT (1999) Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J Biol Chem 274:10324–10330. https://doi.org/10.1074/jbc.274.15.10324
Camarero S, Pardo I, Canas AI, Molina P, Record E, Martinez AT, Martinez MJ, Alcalde M (2012) Engineering platforms for directed evolution of Laccase from Pycnoporus cinnabarinus. Appl Environ Microbiol 78:1370–1384. https://doi.org/10.1128/aem.07530-11
Cameron MD, Timofeevski S, Aust SD (2000) Enzymology of Phanerochaete chrysosporium with respect to the degradation of recalcitrant compounds and xenobiotics. Appl Microbiol Biotechnol 54:751–758. https://doi.org/10.1007/s002530000459
Chen A, Zeng G, Chen G, Fan J, Zou Z, Li H, Hu X, Long F (2011) Simultaneous cadmium removal and 2,4-dichlorophenol degradation from aqueous solutions by Phanerochaete chrysosporium. Appl Microbiol Biotechnol 91:811–821. https://doi.org/10.1007/s00253-011-3313-4
Cheng X-B, Jia R, Li P-S, Zhu Q, Tu S-Q, Tang W-Z (2007) Studies on the properties and Co-immobilization of Manganese Peroxidase. Chin J Biotechnol 23:90–96. https://doi.org/10.1016/S1872-2075(07)60006-5
Chmelova D, Ondrejovic M (2016) Purification and characterization of extracellular laccase produced by Ceriporiopsis subvermispora and decolorization of triphenylmethane dyes. J Basic Microbiol 56:1173–1182. https://doi.org/10.1002/jobm.201600152
Christian V, Shrivastava R, Shukla D, Modi H, Vyas BRM (2005a) Mediator role of veratryl alcohol in the lignin peroxidase-catalyzed oxidative decolorization of Remazol Brilliant Blue R. Enzym Microb Technol 36:327–332. https://doi.org/10.1016/j.enzmictec.2004.09.006
Christian V, Shrivastava R, Shukla D, Modi HA, Vyas BR (2005b) Degradation of xenobiotic compounds by lignin-degrading white-rot fungi: enzymology and mechanisms involved. Indian J Exp Biol 43:301–312. http://nopr.niscair.res.in/bitstream/123456789/23105/1/IJEB%2043%284%29%20301-312.pdf
Cresnar B, Petric S (2011) Cytochrome P450 enzymes in the fungal kingdom. Biochim Biophys Acta 1814:29–35. https://doi.org/10.1016/j.bbapap.2010.06.020
Davila-Vazquez G, Tinoco R, Pickard MA, Vazquez-Duhalt R (2005) Transformation of halogenated pesticides by versatile peroxidase from Bjerkandera adusta. Enzym Microb Technol 36:223–231. https://doi.org/10.1016/j.enzmictec.2004.07.015
Deshmukh R, Khardenavis AA, Purohit HJ (2016) Diverse metabolic capacities of fungi for bioremediation. Indian J Microbiol 56:247–264. https://doi.org/10.1007/s12088-016-0584-6
Diano N, Grano V, Fraconte L, Caputo P, Ricupito A, Attanasio A, Bianco M, Bencivenga U, Rossi S, Manco I, Mita L, Del Pozzo G, Mita DG (2007) Non-isothermal bioreactors in enzymatic remediation of waters polluted by endocrine disruptors: BPA as a model of pollutant. Appl Catal B Environ 69:252–261. https://doi.org/10.1016/j.apcatb.2006.07.004
Doddapaneni H, Chakraborty R, Yadav JS (2005) Genome-wide structural and evolutionary analysis of the P450 monooxygenase genes (P450ome) in the white rot fungus Phanerochaete chrysosporium: evidence for gene duplications and extensive gene clustering. BMC Genomics 6:92. https://doi.org/10.1186/1471-2164-6-92
Dodor DE, Hwang H-M, Ekunwe SIN (2004) Oxidation of anthracene and benzo[a]pyrene by immobilized laccase from Trametes versicolor. Enzym Microb Technol 35:210–217. https://doi.org/10.1016/j.enzmictec.2004.04.007
D’Souza DT, Tiwari R, Sah AK, Raghukumar C (2006) Enhanced production of laccase by a marine fungus during treatment of colored effluents and synthetic dyes. Enzym Microb Technol 38:504–511. https://doi.org/10.1016/j.enzmictec.2005.07.005
Dua M, Singh A, Sethunathan N, Johri A (2002) Biotechnology and bioremediation: successes and limitations. Appl Microbiol Biotechnol 59:143–152. https://doi.org/10.1007/s00253-002-1024-6
Falade AO, Nwodo UU, Iweriebor BC, Green E, Mabinya LV, Okoh AI (2017) Lignin peroxidase functionalities and prospective applications. Microbiol Open 6. https://doi.org/10.1002/mbo3.394
Gao L, Yan X (2016) Nanozymes: an emerging field bridging nanotechnology and biology. Sci China Life Sci 59:400–402. https://doi.org/10.1007/s11427-016-5044-3
Gitsov I, Hamzik J, Ryan J, Simonyan A, Nakas JP, Omori S, Krastanov A, Cohen T, Tanenbaum SW (2008) Enzymatic nanoreactors for environmentally benign biotransformations. 1. Formation and catalytic activity of supramolecular complexes of laccase and linear−dendritic block copolymers. Biomacromolecules 9:804–811. https://doi.org/10.1021/bm701081m
Godoy P, Reina R, Calderon A, Wittich RM, Garcia-Romera I, Aranda E (2016) Exploring the potential of fungi isolated from PAH-polluted soil as a source of xenobiotics-degrading fungi. Environ Sci Pollut Res Int 23:20985–20996. https://doi.org/10.1007/s11356-016-7257-1
Gu C, Zheng F, Long L, Wang J, Ding S (2014) Engineering the expression and characterization of two novel laccase isoenzymes from Coprinus comatus in Pichia pastoris by fusing an additional ten amino acids tag at N-terminus. PLoS One 9:e93912. https://doi.org/10.1371/journal.pone.0093912
Guengerich FP (2001a) Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem Res Toxicol 14:611–650. https://doi.org/10.1021/tx0002583
Guengerich FP (2001b) Uncommon P450-catalyzed reactions. Curr Drug Metab 2:93–115. https://doi.org/10.2174/1389200013338694
Han Y, Shi L, Meng J, Yu H, Zhang X (2014) Azo dye biodecolorization enhanced by Echinodontium taxodii cultured with lignin. PLoS One 9:e109786. https://doi.org/10.1371/journal.pone.0109786
Harms H, Schlosser D, Wick LY (2011) Untapped potential: exploiting fungi in bioremediation of hazardous chemicals. Nat Rev Microbiol 9:177. https://doi.org/10.1038/nrmicro2519
Haroune L, Saibi S, Cabana H, Bellenger JP (2017) Intracellular enzymes contribution to the biocatalytic removal of pharmaceuticals by trametes hirsuta. Environ Sci Technol 51:897–904. https://doi.org/10.1021/acs.est.6b04409
Hirosue S, Tazaki M, Hiratsuka N, Yanai S, Kabumoto H, Shinkyo R, Arisawa A, Sakaki T, Tsunekawa H, Johdo O, Ichinose H, Wariishi H (2011) Insight into functional diversity of cytochrome P450 in the white-rot basidiomycete Phanerochaete chrysosporium: involvement of versatile monooxygenase. Biochem Biophys Res Commun 407:118–123. https://doi.org/10.1016/j.bbrc.2011.02.121
Jing R, Kjellerup BV (2018) Biogeochemical cycling of metals impacting by microbial mobilization and immobilization. J Environ Sci 66:146–154. https://doi.org/10.1016/j.jes.2017.04.035
Jones SM, Solomon EI (2015) Electron transfer and reaction mechanism of laccases. Cell Mol Life Sci 72:869–883. https://doi.org/10.1007/s00018-014-1826-6
Junghanns C, Moeder M, Krauss G, Martin C, Schlosser D (2005) Degradation of the xenoestrogen nonylphenol by aquatic fungi and their laccases. Microbiology 151:45–57. https://doi.org/10.1099/mic.0.27431-0
Kadri T, Rouissi T, Kaur Brar S, Cledon M, Sarma S, Verma M (2017) Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by fungal enzymes: a review. J Environ Sci 51:52–74. https://doi.org/10.1016/j.jes.2016.08.023
Karich A, Ullrich R, Scheibner K, Hofrichter M (2017) Fungal unspecific peroxygenases oxidize the majority of organic EPA priority pollutants. Front Microbiol 8:1463. https://doi.org/10.3389/fmicb.2017.01463
Keum YS, Li QX (2004) Fungal laccase-catalyzed degradation of hydroxy polychlorinated biphenyls. Chemosphere 56:23–30. https://doi.org/10.1016/j.chemosphere.2004.02.028
Kour D, Rana KL, Yadav N, Yadav AN, Singh J, Rastegari AA, Saxena AK (2019) Agriculturally and industrially important fungi: current developments and potential biotechnological applications. In: Yadav AN, Singh S, Mishra S, Gupta A (eds) Recent advancement in white biotechnology through fungi, Volume 2: perspective for value-added products and environments. Springer International Publishing, Cham, pp 1–64. https://doi.org/10.1007/978-3-030-14846-1_1
Koyani RD, Vazquez-Duhalt R (2016) Laccase encapsulation in chitosan nanoparticles enhances the protein stability against microbial degradation. Environ Sci Pollut Res Int 23:18850–18857. https://doi.org/10.1007/s11356-016-7072-8
Kues U (2015) Fungal enzymes for environmental management. Curr Opin Biotechnol 33:268–278. https://doi.org/10.1016/j.copbio.2015.03.006
Laurichesse S, Avérous L (2014) Chemical modification of lignins: towards biobased polymers. Prog Polym Sci 39:1266–1290. https://doi.org/10.1016/j.progpolymsci.2013.11.004
Lee AH, Kang CM, Lee YM, Lee H, Yun CW, Kim GH, Kim JJ (2016) Heterologous expression of a new manganese-dependent peroxidase gene from Peniophora incarnata KUC8836 and its ability to remove anthracene in Saccharomyces cerevisiae. J Biosci Bioeng 122:716–721. https://doi.org/10.1016/j.jbiosc.2016.06.006
Levin L, Forchiassin F, Viale A (2005) Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements. Process Biochem 40:1381–1387. https://doi.org/10.1016/j.procbio.2004.06.005
Liang H, Lin F, Zhang Z, Liu B, Jiang S, Yuan Q, Liu J (2017) Multicopper laccase mimicking nanozymes with nucleotides as ligands. ACS Appl Mater Interfaces 9:1352–1360. https://doi.org/10.1021/acsami.6b15124
Lima RN, Porto AL (2016) Recent advances in marine enzymes for biotechnological processes. Adv Food Nutr Res 78:153–192. https://doi.org/10.1016/bs.afnr.2016.06.005
Loi M, Fanelli F, Zucca P, Liuzzi VC, Quintieri L, Cimmarusti MT, Monaci L, Haidukowski M, Logrieco AF, Sanjust E, Mule G (2016) Aflatoxin B(1) and M(1) degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators. Toxins 8. https://doi.org/10.3390/toxins8090245
Lucero Camacho-Morales R, Garcia-Fontana C, Fernandez-Irigoyen J, Santamaria E, Gonzalez-Lopez J, Manzanera M, Aranda E (2018) Anthracene drives sub-cellular proteome-wide alterations in the degradative system of Penicillium oxalicum. Ecotoxicol Environ Saf 159:127–135. https://doi.org/10.1016/j.ecoenv.2018.04.051
Ma X, Zhang L, Xia M, Li S, Zhang X, Zhang Y (2017) Mimicking the active sites of organophosphorus hydrolase on the backbone of graphene oxide to destroy nerve agent simulants. ACS Appl Mater Interfaces 9:21089–21093. https://doi.org/10.1021/acsami.7b07770
Macellaro G, Pezzella C (2014) Fungal laccases degradation of endocrine disrupting compounds. Biomed Res Int 2014:614038. https://doi.org/10.1155/2014/614038
Margot J, Bennati-Granier C, Maillard J, Blanquez P, Barry DA, Holliger C (2013) Bacterial versus fungal laccase: potential for micropollutant degradation. AMB Express 3:63. https://doi.org/10.1186/2191-0855-3-63
Mate DM, Alcalde M (2015) Laccase engineering: from rational design to directed evolution. Biotechnol Adv 33:25–40. https://doi.org/10.1016/j.biotechadv.2014.12.007
Miele A, Giardina P, Sannia G, Faraco V (2010) Random mutants of a Pleurotus ostreatus laccase as new biocatalysts for industrial effluents bioremediation. J Appl Microbiol 108:998–1006. https://doi.org/10.1111/j.1365-2672.2009.04505.x
Minussi RC, Pastore GM, Duran N (2007) Laccase induction in fungi and laccase/N-OH mediator systems applied in paper mill effluent. Bioresour Technol 98:158–164. https://doi.org/10.1016/j.biortech.2005.11.008
Morel M, Meux E, Mathieu Y, Thuillier A, Chibani K, Harvengt L, Jacquot JP, Gelhaye E (2013) Xenomic networks variability and adaptation traits in wood decaying fungi. Microb Biotechnol 6:248–263. https://doi.org/10.1111/1751-7915.12015
Mougin C, Boukcim H, Jolivalt C (2009) Soil bioremediation strategies based on the use of fungal enzymes. In: Singh A, Kuhad RC, Ward OP (eds) Advances in applied bioremediation. Springer, Berlin/Heidelberg, pp 123–149. https://doi.org/10.1007/978-3-540-89621-0_7
Naranjo-Briceno L, Pernia B, Guerra M, Demey JR, De Sisto A, Inojosa Y, Gonzalez M, Fusella E, Freites M, Yegres F (2013) Potential role of oxidative exoenzymes of the extremophilic fungus Pestalotiopsis palmarum BM-04 in biotransformation of extra-heavy crude oil. Microb Biotechnol 6:720–730. https://doi.org/10.1111/1751-7915.12067
Nicell JA, Wright H (1997) A model of peroxidase activity with inhibition by hydrogen peroxide. Enzym Microb Technol 21:302–310. https://doi.org/10.1016/S0141-0229(97)00001-X
Olicon-Hernandez DR, Gonzalez-Lopez J, Aranda E (2017) Overview on the biochemical potential of filamentous fungi to degrade pharmaceutical compounds. Front Microbiol 8:1792. https://doi.org/10.3389/fmicb.2017.01792
Piontek K, Smith AT, Blodig W (2001) Lignin peroxidase structure and function. Biochem Soc Trans 29:111–116. https://doi.org/10.1042/bst0290111
Pointing SB (2001) Feasibility of bioremediation by white-rot fungi. Appl Microbiol Biotechnol 57:20–33. https://doi.org/10.1007/s002530100745
Pozdnyakova NN (2012) Involvement of the ligninolytic system of white-rot and litter-decomposing fungi in the degradation of polycyclic aromatic hydrocarbons. Biotechnol Res Int 2012:243217. https://doi.org/10.1155/2012/243217
Pozdnyakova N, Dubrovskaya E, Chernyshova M, Makarov O, Golubev S, Balandina S, Turkovskaya O (2018a) The degradation of three-ringed polycyclic aromatic hydrocarbons by wood-inhabiting fungus Pleurotus ostreatus and soil-inhabiting fungus Agaricus bisporus. Fungal Biol 122:363–372. https://doi.org/10.1016/j.funbio.2018.02.007
Pozdnyakova NN, Balandina SA, Dubrovskaya EV, Golubev CN, Turkovskaya OV (2018b) Ligninolytic basidiomycetes as promising organisms for the mycoremediation of PAH-contaminated environments. IOP Conf Ser Earth Environ Sci 107:012071. https://doi.org/10.1088/1755-1315/107/1/012071
Qin X, Zhang J, Zhang X, 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. https://doi.org/10.1371/journal.pone.0113282
Rana KL, Kour D, Sheikh I, Dhiman A, Yadav N, Yadav AN, Rastegari AA, Singh K, Saxena AK (2019a) Endophytic fungi: biodiversity, ecological significance, and potential industrial applications. In: Yadav AN, Mishra S, Singh S, Gupta A (eds) Recent advancement in white biotechnology through fungi: Volume 1: diversity and enzymes perspectives. Springer International Publishing, Cham, pp 1–62. https://doi.org/10.1007/978-3-030-10480-1_1
Rana KL, Kour D, Sheikh I, Yadav N, Yadav AN, Kumar V, Singh BP, Dhaliwal HS, Saxena AK (2019b) Biodiversity of endophytic fungi from diverse niches and their biotechnological applications. In: Singh BP (ed) Advances in endophytic fungal research: present status and future challenges. Springer International Publishing, Cham, pp 105–144. https://doi.org/10.1007/978-3-030-03589-1_6
Rao MA, Scelza R, Scotti R, Gianfreda L (2010) Role of enzymes in the remediation of polluted environments. J Soil Sci Plant Nutr 10:333–353. https://doi.org/10.4067/S0718-95162010000100008
Rastegari AA, Yadav AN, Gupta A (2019) Prospects of renewable bioprocessing in future energy systems. Springer International Publishing, Cham
Rayu S, Karpouzas DG, Singh BK (2012) Emerging technologies in bioremediation: constraints and opportunities. Biodegradation 23:917–926. https://doi.org/10.1007/s10532-012-9576-3
Salony, Mishra S, Bisaria VS (2006) Production and characterization of laccase from Cyathus bulleri and its use in decolourization of recalcitrant textile dyes. Appl Microbiol Biotechnol 71:646–653. https://doi.org/10.1007/s00253-005-0206-4
Schlosser D, Hofer C (2002) Laccase-catalyzed oxidation of Mn(2+) in the presence of natural Mn(3+) chelators as a novel source of extracellular H(2)O(2) production and its impact on manganese peroxidase. Appl Environ Microbiol 68:3514–3521. https://doi.org/10.1128/AEM.68.7.3514-3521.2002
Sharma B, Dangi AK, Shukla P (2018) Contemporary enzyme based technologies for bioremediation: a review. J Environ Manag 210:10–22. https://doi.org/10.1016/j.jenvman.2017.12.075
Shedbalkar U, Dhanve R, Jadhav J (2008) Biodegradation of triphenylmethane dye cotton blue by Penicillium ochrochloron MTCC 517. J Hazard Mater 157:472–479. https://doi.org/10.1016/j.jhazmat.2008.01.023
Shrivastava R, Christian V, Vyas BRM (2005) Enzymatic decolorization of sulfonphthalein dyes. Enzym Microb Technol 36:333–337. https://doi.org/10.1016/j.enzmictec.2004.09.004
Sirisha VL, Jain A, Jain A (2016) Chapter nine - Enzyme immobilization: an overview on methods, support material, and applications of immobilized enzymes. In: Kim S-K, Toldrá F (eds) Advances in food and nutrition research, vol 79. Academic Press, pp 179–211. https://doi.org/10.1016/bs.afnr.2016.07.004
Su J, Fu JJ, Wang Q, Silva C, Cavaco-Paulo A (2018) Laccase: a green catalyst for the biosynthesis of poly-phenols. Crit Rev Biotechnol 38:294–307. https://doi.org/10.1080/07388551.2017.1354353
Suresh PS, Kumar A, Kumar R, Singh VP (2008) An in silico [correction of insilico] approach to bioremediation: laccase as a case study. J Mol Graph Model 26:845–849. https://doi.org/10.1016/j.jmgm.2007.05.005
Syed K, Yadav JS (2012) P450 monooxygenases (P450ome) of the model white rot fungus Phanerochaete chrysosporium. Crit Rev Microbiol 38:339–363. https://doi.org/10.3109/1040841X.2012.682050
Syed K, Porollo A, Lam YW, Yadav JS (2011) A fungal P450 (CYP5136A3) capable of oxidizing polycyclic aromatic hydrocarbons and endocrine disrupting alkylphenols: role of Trp(129) and Leu(324). PLoS One 6:e28286. https://doi.org/10.1371/journal.pone.0028286
Theerachat M, Emond S, Cambon E, Bordes F, Marty A, Nicaud JM, Chulalaksananukul W, Guieysse D, Remaud-Simeon M, Morel S (2012) Engineering and production of laccase from Trametes versicolor in the yeast Yarrowia lipolytica. Bioresour Technol 125:267–274. https://doi.org/10.1016/j.biortech.2012.07.117
Tongpim S, Pickard MA (1999) Cometabolic oxidation of phenanthrene to phenanthrene trans-9,10-dihydrodiol by Mycobacterium strain S1 growing on anthracene in the presence of phenanthrene. Can J Microbiol 45:369–376. https://doi.org/10.1139/cjm-45-5-369
Torres-Duarte C, Roman R, Tinoco R, Vazquez-Duhalt R (2009) Halogenated pesticide transformation by a laccase–mediator system. Chemosphere 77:687–692. https://doi.org/10.1016/j.chemosphere.2009.07.039
Torres-Farrada G, Manzano Leon AM, Rineau F, Ledo Alonso LL, Sanchez-Lopez MI, Thijs S, Colpaert J, Ramos-Leal M, Guerra G, Vangronsveld J (2017) Diversity of ligninolytic enzymes and their genes in strains of the Genus Ganoderma: applicable for biodegradation of xenobiotic compounds? Front Microbiol 8:898. https://doi.org/10.3389/fmicb.2017.00898
Tsutsumi Y, Haneda T, Nishida T (2001) Removal of estrogenic activities of bisphenol A and nonylphenol by oxidative enzymes from lignin-degrading basidiomycetes. Chemosphere 42:271–276. https://doi.org/10.1016/S0045-6535(00)00081-3
Valderrama B, Ayala M, Vazquez-Duhalt R (2002) Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes. Chem Biol 9:555–565 . Pii S1074-5521(02)00149-7. https://doi.org/10.1016/S1074-5521(02)00149-7
Van den Brink HM, van Gorcom RF, van den Hondel CA, Punt PJ (1998) Cytochrome P450 enzyme systems in fungi. Fungal Genet Biol 23:1–17. https://doi.org/10.1006/fgbi.1997.1021
Verma P, Madamwar D (2002) Production of ligninolytic enzymes for dye decolorization by cocultivation of white-rot fungi Pleurotus ostreatus and phanerochaete chrysosporium under solid-state fermentation. Appl Biochem Biotechnol 102-103:109–118. https://doi.org/10.1385/ABAB:102-103:1-6:109
Viswanath B, Rajesh B, Janardhan A, Kumar AP, Narasimha G (2014) Fungal laccases and their applications in bioremediation. Enzyme Res 2014:163242. https://doi.org/10.1155/2014/163242
Wang M, Abad D, Kickhoefer VA, Rome LH, Mahendra S (2015) Vault nanoparticles packaged with enzymes as an efficient pollutant biodegradation technology. ACS Nano 9:10931–10940. https://doi.org/10.1021/acsnano.5b04073
Watanabe K (2001) Microorganisms relevant to bioremediation. Curr Opin Biotechnol 12:237–241. https://doi.org/10.1016/S0958-1669(00)00205-6
Wong KS, Cheung MK, Au CH, Kwan HS (2013a) A novel Lentinula edodes laccase and its comparative enzymology suggests guaiacol-based laccase engineering for bioremediation. PLoS One 8:1–12. https://doi.org/10.1371/journal.pone.0066426.t001
Wong KS, Cheung MK, Au CH, Kwan HS (2013b) A novel Lentinula edodes laccase and its comparative enzymology suggest guaiacol-based laccase engineering for bioremediation. PLoS One 8:e66426. https://doi.org/10.1371/journal.pone.0066426
Wu Y, Teng Y, Li Z, Liao X, Luo Y (2008) Potential role of polycyclic aromatic hydrocarbons (PAHs) oxidation by fungal laccase in the remediation of an aged contaminated soil. Soil Biol Biochem 40:789–796. https://doi.org/10.1016/j.soilbio.2007.10.013
Wu J, Xiao D, Zhao H, He H, Peng J, Wang C, Zhang C, He J (2015) A nanocomposite consisting of graphene oxide and Fe3O4 magnetic nanoparticles for the extraction of flavonoids from tea, wine and urine samples. Mikrochim Acta 182:2299–2306. https://doi.org/10.1007/s00604-015-1575-8
Xu F (1996) Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 35:7608–7614. https://doi.org/10.1021/bi952971a
Yadav AN, Sachan SG, Verma P, Kaushik R, Saxena AK (2016) Cold active hydrolytic enzymes production by psychrotrophic Bacilli isolated from three sub-glacial lakes of NW Indian Himalayas. J Basic Microbiol 56:294–307
Yadav A, Verma P, Kumar R, Kumar V, Kumar K (2017) Current applications and future prospects of eco-friendly microbes. EU Voice 3:21–22
Yadav AN, Verma P, Kumar V, Sangwan P, Mishra S, Panjiar N, Gupta VK, Saxena AK (2018) Biodiversity of the genus Penicillium in different habitats. In: Gupta VK, Rodriguez-Couto S (eds) New and future developments in microbial biotechnology and bioengineering, Penicillium system properties and applications. Elsevier, Amsterdam, pp 3–18. https://doi.org/10.1016/B978-0-444-63501-3.00001-6
Yadav AN, Mishra S, Singh S, Gupta A (2019a) Recent advancement in white biotechnology through fungi Volume 1: diversity and enzymes perspectives. Springer International Publishing, Cham
Yadav AN, Mishra S, Singh S, Gupta A (2019b) Recent advancement in white biotechnology through fungi. Volume 2: perspective for value-added products and environments. Springer International Publishing, Cham
Yang J, Li W, Ng TB, Deng X, Lin J, Ye X (2017) Laccases: production, expression regulation, and applications in pharmaceutical biodegradation. Front Microbiol 6. https://doi.org/10.3389/fmicb.2017.00832
Zhang C, Li M, Chen X, Li M (2015) Edible fungus degrade bisphenol A with no harmful effect on its fatty acid composition. Ecotoxicol Environ Saf 118:126–132. https://doi.org/10.1016/j.ecoenv.2015.04.020
Zhang H, Zhang S, He F, Qin X, Zhang X, Yang Y (2016) Characterization of a manganese peroxidase from white-rot fungus Trametes sp.48424 with strong ability of degrading different types of dyes and polycyclic aromatic hydrocarbons. J Hazard Mater 320:265–277. https://doi.org/10.1016/j.jhazmat.2016.07.065
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Baker, P., Tiroumalechetty, A., Mohan, R. (2019). Fungal Enzymes for Bioremediation of Xenobiotic Compounds. In: Yadav, A., Singh, S., Mishra, S., Gupta, A. (eds) Recent Advancement in White Biotechnology Through Fungi. Fungal Biology. Springer, Cham. https://doi.org/10.1007/978-3-030-25506-0_19
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