Abstract
This particular chapter spotlights the growing environmental concerns and hazardous consequences of numerous organic contaminants so-called emerging contaminants (ECs). These ECs are being detected, though in different quantities, in different environmental matrices and wastewater treatment systems. With ever-increasing awareness, people are now more concerned about the wide-spread distribution of pharmaceutically related active compounds in water matrices. In turn, the free flow of ECs in water matrices poses notable adverse effects on human, aquatic animals, and naturally occurring plants, even at very small concentrations. Due to inadequacies and ineffectiveness of, in practice, physical and chemical-based remediation processes, robust treatment approaches, such as microorganisms and their novel enzyme-based degradation/removal of ECs, are of supreme interest. This chapter focuses on various pharmaceutically related ECs and their efficient mitigation from water matrices. Following a brief introduction, the focus is given to two main treatment approaches, i.e., (1) remediation of pharmaceutically active compounds by crude (pristine) and purified enzymes (i.e., lignin peroxidase, manganese peroxidase, soybean peroxidase, horseradish peroxidase, and laccases) and (2) immobilized enzyme-assisted degradation of pharmaceutically active compounds.
Keywords
- Biocatalysis
- Biological risks
- Enzymes
- Hazardous compounds
- Toxicity
- Wastewater treatment
This is a preview of subscription content, access via your institution.
Buying options






References
Pylypchuk IV, Daniel G, Kessler VG, Seisenbaeva GA (2020) Removal of diclofenac, paracetamol, and carbamazepine from model aqueous solutions by magnetic Sol–Gel encapsulated horseradish peroxidase and lignin peroxidase composites. Nano 10(2):282
Ali N, Khan A, Bilal M, Malik S, Badshah S, Iqbal H (2020) Chitosan-based bio-composite modified with Thiocarbamate moiety for decontamination of cations from the aqueous media. Molecules 25(1):226
Ali N, Said A, Ali F, Raziq F, Ali Z, Bilal M et al (2020) Photocatalytic degradation of congo red dye from aqueous environment using cobalt ferrite nanostructures: development, characterization, and photocatalytic performance. Water Air Soil Pollut 231(2):50
Ebele AJ, Abdallah MAE, Harrad S (2017) Pharmaceuticals and personal care products (PPCPs) in the freshwater aquatic environment. Emerg Contam 3(1):1–16
Khan A, Ali N, Bilal M, Malik S, Badshah S, Iqbal H (2019) Engineering functionalized chitosan-based sorbent material: characterization and sorption of toxic elements. Appl Sci 9(23):5138
Petrović M, Gonzalez S, Barceló D (2003) Analysis and removal of emerging contaminants in wastewater and drinking water. TrAC Trends Anal Chem 22(10):685–696
Tixier C, Singer HP, Oellers S, Müller SR (2003) Occurrence and fate of carbamazepine, clofibric acid, diclofenac, ibuprofen, ketoprofen, and naproxen in surface waters. Environ Sci Technol 37(6):1061–1068
Aldekoa J, Medici C, Osorio V, Pérez S, Marcé R, Barceló D, Francés F (2013) Modelling the emerging pollutant diclofenac with the GREAT-ER model: application to the Llobregat River basin. J Hazard Mater 263:207–213
Buser HR, Poiger T, Müller MD (1998) Occurrence and fate of the pharmaceutical drug diclofenac in surface waters: rapid photodegradation in a lake. Environ Sci Technol 32(22):3449–3456
Hallgren P, Wallberg P (2015) Background report on pharmaceutical concentrations and effects in the Baltic Sea. In: Policy area hazards of the EU strategy for the Baltic Sea Region. Swedish Environmental Protection Agency, Stockholm
Belhaj D, Baccar R, Jaabiri I, Bouzid J, Kallel M, Ayadi H, Zhou JL (2015) Fate of selected estrogenic hormones in an urban sewage treatment plant in Tunisia (North Africa). Sci Total Environ 505:154–160
Morsi R, Bilal M, Iqbal HMN, Ashraf SS (2020) Laccases and peroxidases: the smart, greener and futuristic biocatalytic tools to mitigate recalcitrant emerging pollutants. Sci Total Environ:136572
Bilal M, Adeel M, Rasheed T, Zhao Y, Iqbal HMN (2019) Emerging contaminants of high concern and their enzyme-assisted biodegradation – a review. Environ Int 124:336–353
Bilal M, Jing Z, Zhao Y, Iqbal HM (2019) Immobilization of fungal laccase on glutaraldehyde cross-linked chitosan beads and its bio-catalytic potential to degrade bisphenol A. Biocatal Agric Biotechnol 19:101174
Bilal M, Ashraf SS, Barceló D, Iqbal HM (2019) Biocatalytic degradation/redefining “removal” fate of pharmaceutically active compounds and antibiotics in the aquatic environment. Sci Total Environ 691:1190–1211
Bilal M, Rasheed T, Iqbal HMN, Yan Y (2018) Peroxidases-assisted removal of environmentally-related hazardous pollutants with reference to the reaction mechanisms of industrial dyes. Sci Total Environ 644:1–13
Glumoff T, Harvey P, Molinari S, Goble M, Frank G, Palmer JM et al (1990) Lignin peroxidase from Phanerochaete chrysosporium molecular and kinetic characterization of isozymes. Eur J Biochem 187:515–520
Furukawa T, Bello FO, Horsfall L (2014) Microbial enzyme systems for lignin degradation and their transcriptional regulation. Front Biol 9:448–471
Wen X, Jia Y, Li J (2009) Degradation of tetracycline and oxytetracycline by crude lignin peroxidase prepared from Phanerochaete chrysosporium–a white rot fungus. Chemosphere 75(8):1003–1007
Zhang Y, Geißen SU (2010) In vitro degradation of carbamazepine and diclofenac by crude lignin peroxidase. J Hazard Mater 176(1–3):1089–1092
Ivancich A, Mazza G, Desbois A (2001) Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes. Biochemistry 40:6860–6866
Zhang Y, Geißen SU (2012) Elimination of carbamazepine in a non-sterile fungal bioreactor. Bioresour Technol 112:221–227
Heinfling A, Ruiz-Dueñas FJ, Martı́nez MJ, Bergbauer M, Szewzyk U, Martı́nez AT (1998) A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta. FEBS Lett 428(3):141–146
Glenn JK, Gold MH (1985) Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidiomycete, Phanerochaete chrysosporium. Arch Biochem Biophys 242(2):329–341
Paszczyński A, Huynh VB, Crawford R (1985) Enzymatic activities of an extracellular, manganese-dependent peroxidase from Phanerochaete chrysosporium. FEMS Microbiol Lett 29(1–2):37–41
Bilal M, Asgher M, Parra-Saldivar R, Hu H, Wang W, Zhang X, Iqbal HM (2017) Immobilized ligninolytic enzymes: an innovative and environmental responsive technology to tackle dye-based industrial pollutants–a review. Sci Total Environ 576:646–659
Kellner H, Luis P, Pecyna MJ, Barbi F, Kapturska D, Krüger D et al (2014) Widespread occurrence of expressed fungal secretory peroxidases in forest soils. PLoS One 9(4):e95557
Champagne PP, Ramsay JA (2005) Contribution of manganese peroxidase and laccase to dye decoloration by Trametes versicolor. Appl Microbiol Biotechnol 69(3):276
Maciel MJM, Ribeiro HCT (2010) Industrial and biotechnological applications of ligninolytic enzymes of the basidiomycota: a review. Electron J Biotechnol 13(6):14–15
Sundaramoorthy M, Kishi K, Gold MH, Poulos TL (1994) The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution. J Biol Chem 269(52):32759–32767
Hildén K, Mäkelä MR, Steffen KT, Hofrichter M, Hatakka A, Archer DB, Lundell TK (2014) Biochemical and molecular characterization of an atypical manganese peroxidase of the litter-decomposing fungus Agrocybe praecox. Fungal Genet Biol 72:131–136
Li L, Liu B, Yang J, Zhang Q, He C, Jia R (2019) Catalytic properties of a short manganese peroxidase from Irpex lacteus F17 and the role of Glu166 in the Mn2+-independent activity. Int J Biol Macromol 136:859–869
Wong DW (2009) Structure and action mechanism of ligninolytic enzymes. Appl Biochem Biotechnol 157(2):174–209
Lueangjaroenkit P, Teerapatsakul C, Sakka K, Sakka M, Kimura T, Kunitake E, Chitradon L (2019) Two manganese peroxidases and a laccase of Trametes polyzona KU-RNW027 with novel properties for dye and pharmaceutical product degradation in redox mediator-free system. Mycobiology 47:217–229
Wen X, Jia Y, Li J (2010) Enzymatic degradation of tetracycline and oxytetracycline by crude manganese peroxidase prepared from Phanerochaete chrysosporium. J Hazard Mater 177(1–3):924–928
Bódalo A, Gomez JL, Gomez E, Bastida J, Maximo MF (2006) Comparison of commercial peroxidases for removing phenol from water solutions. Chemosphere 63(4):626–632
Fernandes M, Souza DH, Henriques RO, Alves MV, Skoronski E, Junior AF (2020) Obtaining soybean peroxidase from soybean hulls and its application for detoxification of 2, 4-dichlorophenol contaminated water. J Environ Chem Eng 8:103786
Alneyadi A, Shah I, AbuQamar S, Ashraf S (2017) Differential degradation and detoxification of an aromatic pollutant by two different peroxidases. Biomol Ther 7(1):31
Alneyadi AH, Ashraf SS (2016) Differential enzymatic degradation of thiazole pollutants by two different peroxidases–a comparative study. Chem Eng J 303:529–538
Almaqdi KA, Morsi R, Alhayuti B, Alharthi F, Ashraf SS (2019) LC-MSMS based screening of emerging pollutant degradation by different peroxidases. BMC Biotechnol 19(1):83
Arnoldsson K, Andersson PL, Haglund P (2012) Formation of environmentally relevant brominated dioxins from 2,4,6,-tribromophenol via bromoperoxidase-catalyzed dimerization. Environ Sci Technol 46(13):7239–7244
Baumer JD, Valério A, de Souza SMGU, Erzinger GS, Furigo Jr A, de Souza AAU (2018) Toxicity of enzymatically decolored textile dyes solution by horseradish peroxidase. J Hazard Mater 360:82–88
Zhou H, Yang D, Qiu X, Wu X, Li Y (2013) A novel and efficient polymerization of lignosulfonates by horseradish peroxidase/H2O2 incubation. Appl Microbiol Biotechnol 97(24):10309–10320
Colosi LM, Pinto RA, Huang Q, Weber WJJ (2009) Peroxidase-mediated degradation of perfluorooctanoic acid. Environ Toxicol Chem Int J 28(2):264–271
Ling KQ, Li WS, Sayre LM (2008) Oxidations of N-(3-indoleethyl) cyclic aliphatic amines by horseradish peroxidase: the indole ring binds to the enzyme and mediates electron-transfer amine oxidation. J Am Chem Soc 130(3):933–944
Yang L, Shi Y, Li J, Fang L, Luan T (2018) Transformation of aqueous sulfonamides under horseradish peroxidase and characterization of sulfur dioxide extrusion products from sulfadiazine. Chemosphere 200:164–172
Xu R, Si Y, Li F, Zhang B (2015) Enzymatic removal of paracetamol from aqueous phase: horseradish peroxidase immobilized on nanofibrous membranes. Environ Sci Pollut Res 22(5):3838–3846
Berry TD, Filley TR, Blanchette RA (2014) Oxidative enzymatic response of white-rot fungi to single-walled carbon nanotubes. Environ Pollut 193:197–204
Giardina P, Faraco V, Pezzella C, Piscitelli A, Vanhulle S, Sannia G (2010) Laccases: a never-ending story. Cell Mol Life Sci 67(3):369–385
Asgher M, Noreen S, Bilal M (2017) Enhancing catalytic functionality of Trametes versicolor IBL-04 laccase by immobilization on chitosan microspheres. Chem Eng Res Des 119:1–11
Asgher M, Noreen S, Bilal M (2017) Enhancement of catalytic, reusability, and long-term stability features of Trametes versicolor IBL-04 laccase immobilized on different polymers. Int J Biol Macromol 95:54–62
Moreno AD, Ibarra D, Eugenio ME, Tomás-Pejó E (2019) Laccases as versatile enzymes: from industrial uses to novel applications. J Chem Technol Biotechnol 95:481. https://doi.org/10.1002/jctb.6224
Unuofin JO, Okoh AI, Nwodo UU (2019) Aptitude of oxidative enzymes for treatment of wastewater pollutants: a laccase perspective. Molecules (Basel, Switzerland) 24(11):2064
Guardado ALP, Belleville MP, Alanis MDJR, Saldivar RP, Sanchez-Marcano J (2019) Effect of redox mediators in pharmaceuticals degradation by laccase: a comparative study. Process Biochem 78:123–131
Litwińska K, Bischoff F, Matthes F, Bode R, Rutten T, Kunze G (2019) Characterization of recombinant laccase from Trametes versicolor synthesized by Arxula adeninivorans and its application in the degradation of pharmaceuticals. AMB Express 9(1):102
Alharbi SK, Nghiem LD, Van De Merwe JP, Leusch FD, Asif MB, Hai FI, Price WE (2019) Degradation of diclofenac, trimethoprim, carbamazepine, and sulfamethoxazole by laccase from Trametes versicolor: transformation products and toxicity of treated effluent. Biocatal Biotransformation 37(6):399–408
Sutar RS, Rathod VK (2015) Ultrasound assisted laccase catalyzed degradation of ciprofloxacin hydrochloride. J Ind Eng Chem 31:276–282
Sutar RS, Rathod VK (2015) Ultrasound assisted enzyme catalyzed degradation of cetirizine dihydrochloride. Ultrason Sonochem 24:80–86
Suda T, Hata T, Kawai S, Okamura H, Nishida T (2012) Treatment of tetracycline antibiotics by laccase in the presence of 1-hydroxybenzotriazole. Bioresour Technol 103(1):498–501
Llorca M, Rodríguez-Mozaz S, Couillerot O, Panigoni K, de Gunzburg J, Bayer S et al (2015) Identification of new transformation products during enzymatic treatment of tetracycline and erythromycin antibiotics at laboratory scale by an on-line turbulent flow liquid-chromatography coupled to a high resolution mass spectrometer LTQ-Orbitrap. Chemosphere 119:90–98
Mugdha A, Usha M (2012) Enzymatic treatment of wastewater containing dyestuffs using different delivery systems. Sci Rev Chem Commun 2(1):31–40
Yang RL, Zhao XJ, Wu TT, Bilal M, Wang ZY, Luo HZ, Yang WJ (2019) A novel and highly regioselective biocatalytic approach to acetylation of helicid by using whole-cell biocatalysts in organic solvents. Catal Commun 128:105707
Asgher M, Shahid M, Kamal S, Iqbal HMN (2014) Recent trends and valorization of immobilization strategies and ligninolytic enzymes by industrial biotechnology. J Mol Catal B Enzym 101:56–66
Zdarta J, Meyer AS, Jesionowski T, Pinelo M (2018) Developments in support materials for immobilization of oxidoreductases: a comprehensive review. Adv Colloid Interf Sci 258:1–20
Sheldon RA, van Pelt S (2013) Enzyme immobilisation in biocatalysis: why, what and how. Chem Soc Rev 42(15):6223–6235
Ren S, Li C, Jiao X, Jia S, Jiang Y, Bilal M, Cui J (2019) Recent progress in multienzymes co-immobilization and multienzyme system applications. Chem Eng J 373:1254–1278
Bilal M, Asgher M (2015) Dye decolorization and detoxification potential of Ca-alginate beads immobilized manganese peroxidase. BMC Biotechnol 15(1):111
Touahar IE, Haroune L, Ba S, Bellenger JP, Cabana H (2014) Characterization of combined cross-linked enzyme aggregates from laccase, versatile peroxidase and glucose oxidase, and their utilization for the elimination of pharmaceuticals. Sci Total Environ 481:90–99
García-Zamora JL, León-Aguirre K, Quiroz-Morales R, Parra-Saldívar R, Gómez-Patiño MB, Arrieta-Baez D et al (2018) Chloroperoxidase-mediated halogenation of selected pharmaceutical micropollutants. Catalysts 8(1):32
Guo J, Liu X, Zhang X, Wu J, Chai C, Ma D et al (2019) Immobilized lignin peroxidase on Fe3O4@ SiO2@ polydopamine nanoparticles for degradation of organic pollutants. Int J Biol Macromol 138:433–440
Inoue S, Igarashi Y, Yoneda Y, Kawai S, Okamura H, Nishida T (2015) Elimination and detoxification of fungicide miconazole and antidepressant sertraline by manganese peroxidase-dependent lipid peroxidation system. Int Biodeterior Biodegradation 100:79–84
Forrez I, Carballa M, Verbeken K, Vanhaecke L, Ternes T, Boon N, Verstraete W (2010) Diclofenac oxidation by biogenic manganese oxides. Environ Sci Technol 44(9):3449–3454
Yang J, Lin Y, Yang X, Ng TB, Ye X, Lin J (2017) Degradation of tetracycline by immobilized laccase and the proposed transformation pathway. J Hazard Mater 322:525–531
Wen X, Zeng Z, Du C, Huang D, Zeng G, Xiao R et al (2019) Immobilized laccase on bentonite-derived mesoporous materials for removal of tetracycline. Chemosphere 222:865–871
Jahangiri E, Thomas I, Schulze A, Seiwert B, Cabana H, Schlosser D (2018) Characterisation of electron beam irradiation-immobilised laccase for application in wastewater treatment. Sci Total Environ 624:309–322
Ba S, Haroune L, Soumano L, Bellenger JP, Jones JP, Cabana H (2018) A hybrid bioreactor based on insolubilized tyrosinase and laccase catalysis and microfiltration membrane remove pharmaceuticals from wastewater. Chemosphere 201:749–755
Taheran M, Naghdi M, Brar SK, Knystautas EJ, Verma M, Surampalli RY (2017) Degradation of chlortetracycline using immobilized laccase on Polyacrylonitrile-biochar composite nanofibrous membrane. Sci Total Environ 605:315–321
Naghdi M, Taheran M, Brar SK, Kermanshahi-pour A, Verma M, Surampalli RY (2017) Immobilized laccase on oxygen functionalized nanobiochars through mineral acids treatment for removal of carbamazepine. Sci Total Environ 584:393–401
Ji C, Hou J, Wang K, Zhang Y, Chen V (2016) Biocatalytic degradation of carbamazepine with immobilized laccase-mediator membrane hybrid reactor. J Membr Sci 502:11–20
Kumar VV, Cabana H (2016) Towards high potential magnetic biocatalysts for on-demand elimination of pharmaceuticals. Bioresour Technol 200:81–89
Nguyen LN, Hai FI, Price WE, Leusch FD, Roddick F, McAdam EJ et al (2014) Continuous biotransformation of bisphenol A and diclofenac by laccase in an enzymatic membrane reactor. Int Biodeterior Biodegradation 95:25–32
Wang Q, Cui J, Li G, Zhang J, Huang F, Wei Q (2014) Laccase immobilization by chelated metal ion coordination chemistry. Polymers 6(9):2357–2370
Acknowledgments
Authors are grateful to their representative universities/institutes for providing literature facilities.
Conflict of Interests
Authors declare no conflict of interest in any capacity, including financial and competing.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2020 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Bilal, M., Iqbal, H.M.N., Barceló, D. (2020). Perspectives on the Feasibility of Using Enzymes for Pharmaceutical Removal in Wastewater. In: Rodriguez-Mozaz, S., Blánquez Cano, P., Sarrà Adroguer, M. (eds) Removal and Degradation of Pharmaceutically Active Compounds in Wastewater Treatment. The Handbook of Environmental Chemistry, vol 108. Springer, Cham. https://doi.org/10.1007/698_2020_661
Download citation
DOI: https://doi.org/10.1007/698_2020_661
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-77508-7
Online ISBN: 978-3-030-77509-4
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)