Laccase immobilization and insolubilization: from fundamentals to applications for the elimination of emerging contaminants in wastewater treatment

References

• Abadulla E, Tzanov T, Costa S, Robra KH, Cavaco-Paulo A, Gübitz GM. 2000. Decolorization and detoxification of textile dyes with a laccase from Trametes hirsuta. Appl Environ Microbiol 66: 3357–3362.
   PubMed Web of Science ®Google Scholar
• Ahn MY, Dec J, Kim JE, Bollag JM. 2002. Treatment of 2,4-dichlorophenol polluted soil with free and immobilized laccase. J Environ Qual 31: 1509–1515.
   PubMed Web of Science ®Google Scholar
• Andréasson LE, Reinhammar B. 1979. The mechanism of electron transfer in laccase-catalysed reactions. Biochim Biophys Acta 568: 145–156.
   Google Scholar
• Arboleda C, Cabana H, De Pril E, Jones JP, Jimenez GA, Mejia AI, Agathos SN, Penninckx MJ. 2012. Elimination of bisphenol A and triclosan using the enzymatic system of autochthonous Colombian forest fungi. ISRN Biotechnol 2013: 968241.
   Google Scholar
• Arsenault A, Cabana H, Jones JP. 2011. Laccase-Based CLEAs: Chitosan as a Novel Cross-Linking Agent. Enzyme Res 2011: 376015.
   Google Scholar
• Auriol M, Filali-Meknassi Y, Adams CD, Tyagi RD. 2006. Natural and synthetic hormone removal using the horseradish peroxidase enzyme: temperature and pH effects. Water Res 40: 2847–2856.
   PubMed Web of Science ®Google Scholar
• Auriol M, Filali-Meknassi Y, Adams CD, Tyagi RD, Noguerol TN, Piña B. 2008. Removal of estrogenic activity of natural and synthetic hormones from a municipal wastewater: efficiency of horseradish peroxidase and laccase from Trametes versicolor. Chemosphere 70: 445–452.
   PubMed Web of Science ®Google Scholar
• Auriol M, Filali-Meknassi Y, Tyagi RD, Adams CD. 2007. Laccase-catalyzed conversion of natural and synthetic hormones from a municipal wastewater. Water Res 41: 3281–3288.
   PubMed Web of Science ®Google Scholar
• Aust SD, Benson JT. 1993. The fungus among us: use of white rot fungi to biodegrade environmental pollutants. Environ Health Perspect 101: 232–233.
   PubMedGoogle Scholar
• Aytar BS, Bakir U. 2008. Preparation of cross-linked tyrosinase aggregates. Process Biochemi 43:125–131.
   Web of Science ®Google Scholar
• Baldrian P. 2006. Fungal laccases - occurrence and properties. FEMS Microbiol Rev 30: 215–242.
   PubMed Web of Science ®Google Scholar
• Bayramoglu G, Yilmaz M, Yakup Arica M. 2010. Preparation and characterization of epoxy-functionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes. Bioprocess Biosyst Eng 33: 439–448.
   PubMed Web of Science ®Google Scholar
• Belfroid AC, Van der Horst A, Vethaak AD, Schäfer AJ, Rijs GB, Wegener J, Cofino WP. 1999. Analysis and occurrence of estrogenic hormones and their glucuronides in surface water and waste water in The Netherlands. Sci Total Environ 225: 101–108.
   PubMed Web of Science ®Google Scholar
• Berka RM, Schneider P, Golightly EJ, Brown SH, Madden M, Brown KM, Halkier T, Mondorf K, Xu F. 1997. Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae. Appl Environ Microbiol 63: 3151–3157.
   PubMed Web of Science ®Google Scholar
• Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, Mougin C. 2002. Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 41: 7325–7333.
   PubMed Web of Science ®Google Scholar
• Bhatnagar A, Sillanpää M. 2009. Applications of chitin- and chitosan-derivatives for the detoxification of water and wastewater–a short review. Adv Colloid Interface Sci 152: 26–38.
   PubMed Web of Science ®Google Scholar
• Bollag JM, Shuttleworth KL, Anderson DH. 1988. Laccase-mediated detoxification of phenolic compounds. Appl Environ Microbiol 54: 3086–3091.
   PubMed Web of Science ®Google Scholar
• Bollag JM. 1992. Decontaminating soil with enzymes. Environ Sci Technol 26:1876–1881.
   Web of Science ®Google Scholar
• Bollag JM, Leonowicz A. 1984. Comparative studies of extracellular fungal laccases. Appl Environ Microbiol 48: 849–854.
   PubMed Web of Science ®Google Scholar
• Bolong N, Ismail AF, Salim MR, Matsuura T. 2009. A review of the effects of emerging contaminants in wastewater and options for their removal. Desalination 238:229–246.
   Google Scholar
• Bourbonnais R, Leech D, Paice MG. 1998. Electrochemical analysis of the interactions of laccase mediators with lignin model compounds. Biochim Biophys Acta 1379: 381–390.
   PubMed Web of Science ®Google Scholar
• Bourbonnais R, Paice MG. 1990. Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation. FEBS Lett 267: 99–102.
   PubMed Web of Science ®Google Scholar
• Bourbonnais R, Paice MG, Freiermuth B, Bodie E, Borneman S. 1997. Reactivities of various mediators and laccases with kraft pulp and lignin model compounds. Appl Environ Microbiol 63: 4627–4632.
   PubMed Web of Science ®Google Scholar
• Bruggink A, Schoevaart R, Kieboom T. 2003. Concepts of nature in organic synthesis: cascade catalysis and multistep conversions in concert. Org Process Res Develop 7:622–640.
   Web of Science ®Google Scholar
• Cabana H, Ahamed A, Leduc R. 2011. Conjugation of laccase from the white rot fungus Trametes versicolor to chitosan and its utilization for the elimination of triclosan. Bioresour Technol 102: 1656–1662.
   PubMed Web of Science ®Google Scholar
• Cabana H, Jiwan JL, Rozenberg R, Elisashvili V, Penninckx M, Agathos SN, Jones JP. 2007a. Elimination of endocrine disrupting chemicals nonylphenol and bisphenol A and personal care product ingredient triclosan using enzyme preparation from the white rot fungus Coriolopsis polyzona. Chemosphere 67: 770–778.
   PubMed Web of Science ®Google Scholar
• Cabana H, Jones JP, Agathos SN. 2007b. Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. J Biotechnol 132: 23–31.
   PubMed Web of Science ®Google Scholar
• Cabana H, Jones JP, Agathos SN. 2009a. Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine-disrupting chemicals. Biotechnol Bioeng 102: 1582–1592.
   PubMed Web of Science ®Google Scholar
• Cabana H, Alexandre C, Agathos SN, Jones JP. 2009b. Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals. Bioresour Technol 100: 3447–3458.
   PubMed Web of Science ®Google Scholar
• Cabral JMS, Kennedy JF. 1991. Covalent and coordination immobilization of proteins. In: Taylor RF, ed. Protein immobilization: fundamentals and applications. New York: Marcel Dekker, pp 73–138.
   Google Scholar
• Call HP, Mucke I. 1997. History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lignozym(R)-process). J Biotechnol 53:163–202.
   Web of Science ®Google Scholar
• Campbell MK, Farrell SO. 2006. Biochemistry. 5th edn. USA: Thomson Brooks/Cole.
   Google Scholar
• Cao L. 2005. Immobilised enzymes: science or art? Curr Opin Chem Biol 9: 217–226.
   PubMed Web of Science ®Google Scholar
• Cao L, Langen L, Sheldon RA. 2003. Immobilised enzymes: carrier-bound or carrier-free? Curr Opin Biotechnol 14: 387–394.
   PubMed Web of Science ®Google Scholar
• Claus H, Faber G, König H. 2002. Redox-mediated decolorization of synthetic dyes by fungal laccases. Appl Microbiol Biotechnol 59: 672–678.
   PubMed Web of Science ®Google Scholar
• Couto SR, Herrera JLT. 2006. Industrial and biotechnological applications of laccases: A review. Biotechnol Adv 24:500–513.
   PubMed Web of Science ®Google Scholar
• Couto SR, Toca JL. 2006. Inhibitors of laccases: A review. Current Enzyme Inhibition 2:343–352.
   Google Scholar
• Dalal S, Kapoor M, Gupta MN. 2007. Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions. J Mol Catal B: Enz 44:128–132.
   Google Scholar
• D’Annibale A, Stazi SR, Vinciguerra V, Di Mattia E, Sermanni GG. 1999. Characterization of immobilized laccase from Lentinula edodes and its use in olive-mill wastewater treatment. Process Biochem (Barking, London, England), 34:697–706.
   Web of Science ®Google Scholar
• D’Annibale A, Stazi SR, Vinciguerra V, Giovannozzi Sermanni G. 2000. Oxirane-immobilized Lentinula edodes laccase: stability and phenolics removal efficiency in olive mill wastewater. J Biotechnol 77: 265–273.
   PubMed Web of Science ®Google Scholar
• Dimich-Ward H, Wymer ML, Chan-Yeung M. 2004. Respiratory health survey of respiratory therapists. Chest 126: 1048–1053.
   Google Scholar
• Ducros V, Brzozowski AM, Wilson KS, Brown SH, Ostergaard P, Schneider P, Yaver DS, Pedersen AH, Davies GJ. 1998. Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution. Nat Struct Biol 5: 310–316.
   PubMedGoogle Scholar
• Duran N, Rosa MA, D’Annibale A, Gianfreda L. 2002. Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: a review. Enzyme Microb Technol 31:907–931.
   Web of Science ®Google Scholar
• Emmanuel E, Hanna K, Bazin C, Keck G, Clément B, Perrodin Y. 2005. Fate of glutaraldehyde in hospital wastewater and combined effects of glutaraldehyde and surfactants on aquatic organisms. Environ Int 31: 399–406.
   PubMed Web of Science ®Google Scholar
• Epton R, McLaren JV, Thomas TH. 1971. Enzyme insolubilization with cross-linked polyacryloylaminoacetaldehyde dimethylacetal. Biochem J 123: 21P–22P.
   Google Scholar
• Fernández-Lorente G, Palomo JM, Mateo C, Munilla R, Ortiz C, Cabrera Z, Guisán JM, Fernandez-Lafuente R. 2006. Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance. Biomacromolecules 7: 2610–2615.
   PubMed Web of Science ®Google Scholar
• Ferraroni M, Myasoedova NM, Schmatchenko V, Leontievsky AA, Golovleva LA, Scozzafava A, Briganti F. 2007. Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases. BMC Struct Biol 7: 60.
   PubMed Web of Science ®Google Scholar
• Fraenkel-Conrat H, Mecham DK. 1949. The reaction of formaldehyde with proteins; demonstration of intermolecular cross-linking by means of osmotic pressure measurements. J Biol Chem 177: 477–486.
   PubMed Web of Science ®Google Scholar
• Fukuda T, Uchida H, Suzuki M, Miyamoto H, Morinaga H, Nawata H, Uwajima T. 2004. Transformation products of bisphenol A by a recombinant Trametes villosa laccase and their estrogenic activity. J Chem Technol Biotechnol 79:1212–1218.
   Google Scholar
• Fukuda T, Uchida H, Takashima Y, Uwajima T, Kawabata T, Suzuki M. 2001. Degradation of bisphenol A by purified laccase from Trametes villosa. Biochem Biophys Res Commun 284: 704–706.
   PubMed Web of Science ®Google Scholar
• Gaitan IJ, Medina SC, González JC, Rodríguez A, Espejo AJ, Osma JF, Sarria V, Alméciga-Díaz CJ, Sánchez OF. 2011. Evaluation of toxicity and degradation of a chlorophenol mixture by the laccase produced by Trametes pubescens. Bioresour Technol 102: 3632–3635.
   PubMed Web of Science ®Google Scholar
• Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D’Ambrosio C, Scaloni A, Rizzi M. 2004. The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair. J Mol Biol 342: 1519–1531.
   PubMed Web of Science ®Google Scholar
• Garcia HA, Hoffman CM, Kinney KA, Lawler DF. 2011. Laccase-catalyzed oxidation of oxybenzone in municipal wastewater primary effluent. Water Res 45: 1921–1932.
   PubMed Web of Science ®Google Scholar
• Giardina P, Faraco V, Pezzella C, Piscitelli A, Vanhulle S, Sannia G. 2010. Laccases: a never-ending story. Cell Mol Life Sci 67: 369–385.
   PubMed Web of Science ®Google Scholar
• Gigi O, Marbach I, Mayer AM. 1981. Properties of gallic acid-induced extracellular laccase of Botrytis cinerea. Phytochemistry 20:1211–1213.
   Web of Science ®Google Scholar
• Gilles MA, Hudson AQ, Borders CL Jr. 1990. Stability of water-soluble carbodiimides in aqueous solution. Anal Biochem 184: 244–248.
   PubMed Web of Science ®Google Scholar
• Hadorn H, Nitschmann HH. 1944. Die Umsetzung des Caseins mit Formaldehyd. V. Über das verhalten der ε-aminogruppen des lysins und der peptidgruppen. Helvetica Chimica Acta 27:299–312.
   Google Scholar
• Habeeb AJ, Hiramoto R. 1968. Reaction of proteins with glutaraldehyde. Arch Biochem Biophys 126: 16–26.
   PubMed Web of Science ®Google Scholar
• Hakulinen N, Kiiskinen LL, Kruus K, Saloheimo M, Paananen A, Koivula A, Rouvinen J. 2002. Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nat Struct Biol 9: 601–605.
   PubMedGoogle Scholar
• Hanefeld U, Gardossi L, Magner E. 2009. Understanding enzyme immobilisation. Chem Soc Rev 38: 453–468.
   PubMed Web of Science ®Google Scholar
• Harms H, Schlosser D, Wick LY. 2011. Untapped potential: exploiting fungi in bioremediation of hazardous chemicals. Nat Rev Microbiol 9: 177–192.
   PubMed Web of Science ®Google Scholar
• Hegedus I, Nagy E. 2009. Improvement of chymotrypsin enzyme stability as single enzyme nanoparticles. Chem Eng Sci 64:1053–1060.
   Web of Science ®Google Scholar
• Heinz Fraenkel-Conrat, Olcott HS. 1948. The reaction of formaldehyde with proteins. V. Cross-linking between Amino and Primary Amide or Guanidyl Groups. J Am Chem Soc 70:2673–2684.
   Google Scholar
• Hermanson GT. 1996. Bioconjugate techniques. San Diego: Academic Press.
   Google Scholar
• Hilal N, Nigmatullin R, Alpatova A. 2004. Immobilization of cross-linked lipase aggregates within microporous polymeric membranes. J Memb Sci 238:131–141.
   Web of Science ®Google Scholar
• Honda T, Miyazaki M, Nakamura H, Maeda H. 2006. Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface. Adv Synth Catal 348:2163–2171.
   Google Scholar
• Honda T, Miyazaki M, Nakamura H, Maeda H. 2005. Immobilization of enzymes on a microchannel surface through cross-linking polymerization. Chem Commun (Camb): 5062–5064.
   Google Scholar
• Johannes C, Majcherczyk A. 2000. Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems. Appl Environ Microbiol 66: 524–528.
   PubMed Web of Science ®Google Scholar
• Kalkan NA, Aksoy S, Aksoy EA, Hasirci N. 2012. Preparation of chitosan-coated magnetite nanoparticles and application for immobilization of laccase. J Appl Poly Sci 123:707–716.
   Web of Science ®Google Scholar
• Kallio JP, Gasparetti C, Andberg M, Boer H, Koivula A, Kruus K, Rouvinen J, Hakulinen N. 2011. Crystal structure of an ascomycete fungal laccase from Thielavia arenaria–common structural features of asco-laccases. FEBS J 278: 2283–2295.
   PubMed Web of Science ®Google Scholar
• Khosravi A, Vossoughi M, Shahrokhian S, Alemzadeh I. 2012. Nano reengineering of horseradish peroxidase with dendritic macromolecules for stability enhancement. Enzyme Microb Technol 50: 10–16.
   Google Scholar
• Kim J, Grate JW. 2005. Single enzyme nanoparticles. 05AIChE: 2005 AIChE Annual Meeting and Fall Showcase, 30 October 2005 through 4 November 2005, Cincinnati, OH, pp. 14286.
   Google Scholar
• Kim J, Grate JW. 2003. Single-enzyme nanoparticles armored by a nanometer-scale organic/inorganic network. Nano Letters 3:1219–1222.
   Web of Science ®Google Scholar
• Kim J, Grate JW, Wang P. 2006. Nanostructures for enzyme stabilization. Chem Eng Sci 61:1017–1026.
   Web of Science ®Google Scholar
• Kim YJ, Nicell JA. 2006. Laccase-catalyzed oxidation of bisphenol A with the aid of additives. Process Biochem, 41:1029–1037.
   Web of Science ®Google Scholar
• Kimura K, Amy G, Drewes JE, Heberer T, Kim T, Watanabe Y. 2003. Rejection of organic micropollutants (disinfection by-products, endocrine disrupting compounds, and pharmaceutically active compounds) by NF/RO membranes. J Memb Sci 227:113–121.
   Web of Science ®Google Scholar
• Kiso Y, Muroshige K, Oguchi T, Yamada T, Hirose M, Ohara T, Shintani T. 2010. Effect of molecular shape on rejection of uncharged organic compounds by nanofiltration membranes and on calculated pore radii. J Memb Sci 358:101–113.
   Web of Science ®Google Scholar
• Krajewska B. 2004. Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. Enz Microbial Technol 35:126–139.
   Web of Science ®Google Scholar
• Kunamneni A, Plou FJ, Ballesteros A, Alcalde M. 2008. Laccases and their applications: a patent review. Recent Pat Biotechnol 2: 10–24.
   PubMedGoogle Scholar
• Kurzer F, Douraghi-Zadeh K. 1967. Advances in the chemistry of carbodiimides. Chem Rev 67: 107–152.
   PubMed Web of Science ®Google Scholar
• Kusakabe K, Miyagawa D, Gu Y, Maeda H, Morooka S. 2001. Development of self-heating microreactor for catalytic reactions. J Chem Eng Jpn 34:441–443.
   Google Scholar
• Lee JM, Edwards HHL, Pereira CA, Samii SI. 1996. Crosslinking of tissue-derived biomaterials in 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC). J Mater Sci Mater Med 7:531–541.
   Web of Science ®Google Scholar
• Leonowicz A, Sarkar JM, Bollag J. 1988. Improvement in stability of an immobilized fungal laccase. Appl Microbiol Biotechnol 29:129–135.
   Web of Science ®Google Scholar
• Leung HW. 2001. Ecotoxicology of glutaraldehyde: review of environmental fate and effects studies. Ecotoxicol Environ Saf 49: 26–39.
   PubMed Web of Science ®Google Scholar
• Li K, Xu F, Eriksson KE. 1999. Comparison of fungal laccases and redox mediators in oxidation of a nonphenolic lignin model compound. Appl Environ Microbiol 65: 2654–2660.
   PubMed Web of Science ®Google Scholar
• Liu G, Shi Z, Kuriger T, Hanton LR, Simpson J, Moratti SC, Robinson BH, Athanasiadis T, Valentine R, Wormald PJ, Robinson S. 2009a. Synthesis and characterization of chitosan/dextran-based hydrogels for surgical use. Macromolecular Symposia 279:151–157.
   Google Scholar
• Liu ZH, Kanjo Y, Mizutani S. 2009b. Removal mechanisms for endocrine disrupting compounds (EDCs) in wastewater treatment - physical means, biodegradation, and chemical advanced oxidation: a review. Sci Total Environ 407: 731–748.
   PubMed Web of Science ®Google Scholar
• Lopez JL, Matson SL. 1997. A multiphase/extractive enzyme membrane reactor for production of diltiazem chiral intermediate. J Memb Sci 125:189–211.
   Web of Science ®Google Scholar
• López-Alonso JP, Diez-García F, Font J, Ribó M, Vilanova M, Scholtz JM, González C, Vottariello F, Gotte G, Libonati M, Laurents DV. 2009. Carbodiimide EDC induces cross-links that stabilize RNase A C-dimer against dissociation: EDC adducts can affect protein net charge, conformation, and activity. Bioconjug Chem 20: 1459–1473.
   PubMed Web of Science ®Google Scholar
• Madhavi V, Lele SS. 2009. Laccase: Properties and Applications. BioResources 4:1694–1717.
   Web of Science ®Google Scholar
• Majeau JA, Brar SK, Tyagi RD. 2010. Laccases for removal of recalcitrant and emerging pollutants. Bioresour Technol 101: 2331–2350.
   PubMed Web of Science ®Google Scholar
• Majeti NVRK. 2000. A review of chitin and chitosan applications. React Funct Poly 46:1–27.
   Web of Science ®Google Scholar
• Marbach I, Harel E, Mayer AM. 1984. Molecular properties of extracellular Botrytis cinerea laccase. Phytochemistry 23:2713–2717.
   Web of Science ®Google Scholar
• Mateo C, Palomo JM, van Langen LM, van Rantwijk F, Sheldon RA. 2004. A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates. Biotechnol Bioeng 86: 273–276.
   PubMed Web of Science ®Google Scholar
• Mateo C, Palomo JM, Fernandez-Lorente G, Guisan JM, Fernandez-Lafuente R. 2007. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enz Microbial Technol 40:1451–1463.
   Web of Science ®Google Scholar
• Mateo C, Palomo JM, Van Langen LM, Van Rantwijk F, Sheldon RA. 2004. A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates. Biotechnol Bioeng 86:273–276.
   PubMed Web of Science ®Google Scholar
• MatijošyteI, Arends IWCE, de Vries S, Sheldon RA. 2010. Preparation and use of cross-linked enzyme aggregates (CLEAs) of laccases. J Mol Cataly B: Enz 62:142–148.
   Google Scholar
• Messerschmidt A. 1997. Multi-copper Oxidases, World Scientific, Singapore.
   Google Scholar
• Messerschmidt A, Huber R. 1990. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur J Biochem 187: 341–352.
   PubMedGoogle Scholar
• Migneault I, Dartiguenave C, Bertrand MJ, Waldron KC. 2004. Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. BioTechniques 37: 790–6, 798.
   PubMedGoogle Scholar
• Minuth W, Klischies M, Esser K. 1978. The phenoloxidases of the ascomycete Podospora anserina. Structural differences between laccases of high and low molecular weight. Eur J Biochem 90: 73–82.
   PubMedGoogle Scholar
• Muñoz C, Guillén F, Martínez AT, Martínez MJ. 1997. Laccase isoenzymes of Pleurotus eryngii: characterization, catalytic properties, and participation in activation of molecular oxygen and Mn2+ oxidation. Appl Environ Microbiol 63: 2166–2174.
   PubMed Web of Science ®Google Scholar
• Nakajima N, Ikada Y. 1995. Mechanism of amide formation by carbodiimide for bioconjugation in aqueous media. Bioconjug Chem 6: 123–130.
   PubMed Web of Science ®Google Scholar
• Nghiem LD, Schäfer AI. 2002. Adsorption and transport of trace contaminant estrone in NF/RO membranes. Environ Eng Sci 19:441–451.
   Web of Science ®Google Scholar
• Nicolucci C, Rossi S, Menale C, Godjevargova T, Ivanov Y, Bianco M, Mita L, Bencivenga U, Mita DG, Diano N. 2011. Biodegradation of bisphenols with immobilized laccase or tyrosinase on polyacrylonitrile beads. Biodegradation 22: 673–683.
   PubMed Web of Science ®Google Scholar
• Osma JF, Toca-Herrera JL, Rodríguez-Couto S. 2011. Cost analysis in laccase production. J Environ Manage 92: 2907–2912.
   PubMed Web of Science ®Google Scholar
• Park SN, Park JC, Kim HO, Song MJ, Suh H. 2002. Characterization of porous collagen/hyaluronic acid scaffold modified by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide cross-linking. Biomaterials 23: 1205–1212.
   PubMed Web of Science ®Google Scholar
• Piontek K, Antorini M, Choinowski T. 2002. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers. J Biol Chem 277: 37663–37669.
   PubMed Web of Science ®Google Scholar
• Plakas KV, Karabelas AJ. 2011. A systematic study on triazine retention by fouled with humic substances NF/ULPRO membranes. Sep PurifiTechnol 80:246–261.
   Google Scholar
• Quiocho FA, Richards FM. 1964. Intermolecular cross linking of a protein in the crystalline state: carboxypeptidase-A. Proc Natl Acad Sci USA 52: 833–839.
   PubMed Web of Science ®Google Scholar
• Reiss R, Ihssen J, Thöny-Meyer L. 2011. Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum. BMC Biotechnol 11: 9.
   PubMed Web of Science ®Google Scholar
• Ricotta A, Unz RF, Bollag J. 1996. Role of a laccase in the degradation of pentachlorophenol. Bull Environ Contam Toxicol 57: 560–567.
   Web of Science ®Google Scholar
• Roessl U, Nahálka J, Nidetzky B. 2010. Carrier-free immobilized enzymes for biocatalysis. Biotechnol Lett 32: 341–350.
   PubMed Web of Science ®Google Scholar
• Roy JJ, Abraham TE, Abhijith KS, Kumar PV, Thakur MS. 2005. Biosensor for the determination of phenols based on cross-linked enzyme crystals (CLEC) of laccase. Biosens Bioelectron 21: 206–211.
   PubMed Web of Science ®Google Scholar
• Roy-Arcand L, Archibald FS. 1991. Direct dechlorination of chlorophenolic compounds by laccases from Trametes (Coriolus) versicolor. Enzyme and Microbial Technology 13:194–203.
   Web of Science ®Google Scholar
• Sangeetha K, Abraham TE. 2008. Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications. Int J Biol Macromol 43: 314–319.
   PubMed Web of Science ®Google Scholar
• Sano LL, Krueger AM, Landrum PF. 2005. Chronic toxicity of glutaraldehyde: differential sensitivity of three freshwater organisms. Aquat Toxicol 71: 283–296.
   PubMed Web of Science ®Google Scholar
• Schäfer AI, Akanyeti I, Semião AJ. 2011. Micropollutant sorption to membrane polymers: a review of mechanisms for estrogens. Adv Colloid Interface Sci 164: 100–117.
   PubMed Web of Science ®Google Scholar
• Schoevaart R, Kieboom T. 2002a. Combined catalytic conversion involving an enzyme, a homogeneous and a heterogeneous catalyst: One-pot preparation of 4-deoxy-D-glucose derivatives from D-galactose. Tetrahedron Lett 43:3399–3400.
   Web of Science ®Google Scholar
• Schoevaart R, Kieboom T. 2002b. Galactose dialdehyde as potential protein cross-linker: proof of principle. Carbohydr Res 337: 899–904.
   Google Scholar
• Schoevaart R, Kieboom T. 2001. Galactose dialdehyde: the forgotten candidate for a protein cross-linker? Carbohydr Res 334: 1–6.
   PubMed Web of Science ®Google Scholar
• Schoevaart R, Siebum A, van Rantwijk F, Sheldon RA, Kieboom T. 2005. Glutaraldehyde cross-link analogues from carbohydrates. Starch 57:161.
   Google Scholar
• Schoevaart R, Wolbers MW, Golubovic M, Ottens M, Kieboom AP, van Rantwijk F, van der Wielen LA, Sheldon RA. 2004. Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs). Biotechnol Bioeng 87: 754–762.
   PubMed Web of Science ®Google Scholar
• Schoevaart WRK, Van Langen LM, Van Den Dool RTM, Boumans JWL. 2006. Method for preparation of crosslinked enzyme aggregates using aldehydes and amines. US Patent 2008/0296231 A1.
   Google Scholar
• Servos MR, Bennie DT, Burnison BK, Jurkovic A, McInnis R, Neheli T, Schnell A, Seto P, Smyth SA, Ternes TA. 2005. Distribution of estrogens, 17beta-estradiol and estrone, in Canadian municipal wastewater treatment plants. Sci Total Environ 336: 155–170.
   PubMed Web of Science ®Google Scholar
• Sheldon RA. 2011. Cross-linked enzyme aggregates as industrial biocatalysts. Org Process Res Develop 15:213–223.
   Web of Science ®Google Scholar
• Sheldon RA. 2007. Enzyme immobilization: The quest for optimum performance. Adv Syn Catal 349:1289–1307.
   Web of Science ®Google Scholar
• Solomon EI, Sundaram UM, Machonkin TE. 1996. Multicopper Oxidases and Oxygenases. Chem Rev 96: 2563–2606.
   Google Scholar
• Sorgedrager MJ, Verdoes D, van der Meer H, Sheldon RA. 2008. Cross-linked enzyme aggregates in a membrane slurry reactor continuous production of 6-APA by enzymatic hydrolysis of penicillin. Chimica Oggi/Chemistry Today 24:23–25.
   Google Scholar
• Srinivasan C, Dsouza TM, Boominathan K, Reddy CA. 1995. Demonstration of Laccase in the White Rot Basidiomycete Phanerochaete chrysosporium BKM-F1767. Appl Environ Microbiol 61: 4274–4277.
   PubMed Web of Science ®Google Scholar
• Strong PJ, Claus H. 2011. Laccase: A review of its past and its future in bioremediation. Crit Rev Environ Sci Technol 41:373–434.
   Web of Science ®Google Scholar
• Taboada-Puig R, Junghanns C, Demarche P, Moreira MT, Feijoo G, Lema JM, Agathos SN. 2011. Combined cross-linked enzyme aggregates from versatile peroxidase and glucose oxidase: production, partial characterization and application for the elimination of endocrine disruptors. Bioresour Technol 102: 6593–6599.
   PubMed Web of Science ®Google Scholar
• Takigawa T, Endo Y. 2006. Effects of glutaraldehyde exposure on human health. J Occup Health 48: 75–87.
   PubMed Web of Science ®Google Scholar
• Tanaka T, Tonosaki T, Nose M, Tomidokoro N, Kadomura N, Fujii T, Taniguchi M. 2001. Treatment of model soils contaminated with phenolic endocrine-disrupting chemicals with laccase from Trametes sp. in a rotating reactor. J Biosci Bioeng 92: 312–316.
   PubMed Web of Science ®Google Scholar
• ten Have R, Teunissen PJ. 2001. Oxidative mechanisms involved in lignin degradation by white-rot fungi. Chem Rev 101: 3397–3413.
   PubMed Web of Science ®Google Scholar
• Twyman RM. 2005. Enzymes: Immobilized enzymes. In: Encyclopedia of Analytical Science, 2nd edn. London, UK: Elsevier Science, pp 523–529.
   Google Scholar
• Wells A, Teria M, Eve T. 2006. Green oxidations with laccase-mediator systems. Biochem Soc Trans 34: 304–308.
   PubMed Web of Science ®Google Scholar
• Williams A, Ibrahim IT. 1981. Carbodiimide chemistry: Recent advances. Chem Rev 81:589–636.
   Web of Science ®Google Scholar
• Wong SS. 1991. Chemistry of protein conjugation and cross linking. 1 edition edn. Boca Raton, Florida, USA: CRC Press.
   Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Yadav R, Labhsetwar N, Kotwal S, Rayalu S. 2011a. Single enzyme nanoparticle for biomimetic CO2 sequestration. J Nanoparticle Res 13:263–271.
   Google Scholar
• Yadav R, Satyanarayanan T, Kotwal S, Rayalu S. 2011b. Enhanced carbonation reaction using chitosan-based carbonic anhydrase nanoparticles. Current Sci 100:520–524.
   Google Scholar
• Yang WY, Min DY, Wen SX, Jin L, Rong L, Tetsuo M, Bo C. 2006. Immobilization and characterization of laccase from Chinese Rhus vernicifera on modified chitosan. Process Biochem 41:1378–1382.
   Google Scholar
• Yaropolov AI, Skorobogat’ko OV, Vartanov SS, Varfolomeyev SD. 1994. Laccase - Properties, catalytic mechanism, and applicability. Appl Biochem Biotechnol 49:257–280.
   Web of Science ®Google Scholar
• Yoshida H. 1883. Chemistry of Lacquer (Urushi) part I. Chemical Society of Tokio 43:472–486.
   Google Scholar
• Yoshitake A, Katayama Y, Nakamura M, Iimura Y, Kawai S, Morohoshi N. 1993. N-linked carbohydrate chains protect laccase III from proteolysis in Coriolus versicolor. J Gen Microbiol 139:179–185.
   Google Scholar
• Zhang J, Xu Z, Chen H, Zong Y. 2009. Removal of 2,4-dichlorophenol by chitosan-immobilized laccase from Coriolus versicolor. Biochem Eng J 45:54–59.
   Web of Science ®Google Scholar
• Zouari N, Romette J, Thomas D. 1987. Purification and properties of two laccase isoenzymes produced by Botrytis cinerea. Appl Biochem Biotechnol 15:213–225.
   Google Scholar