Abstract
Background and Source: Laccase belongs to the blue multi-copper oxidases, which are widely distributed in fungi and higher plants. It is present in Ascomycetes, Deuteromycetes, and Basidiomycetes and found abundantly in white-rot fungi.
Applications: Laccase enzymes because of their potential have acquired more importance and application in the area of textile, pulp and paper, and food industry. Recently, it is being used in developing biosensors for detection and removal of toxic pollutants, designing of biofuel cells and medical diagnostics tool. Laccase is also being used as a bioremediation agent as they have been found potent enough in cleaning up herbicides pesticides and certain explosives in soil. Because of having the ability to oxidize phenolic, non-phenolic lignin-related compounds and highly fractious environmental pollutants, laccases have drawn the attention of researchers in the last few decades. Commercially, laccases have been used to determine the difference between codeine and morphine, produce ethanol and are also being employed in de-lignify woody tissues. We have revised patents related to applicability of laccases. We have revised all the patents related to its wide applicability.
Conclusion: For fulfillment of these wide applications, one of the major concerns is to develop a system for efficient production of these enzymes at a broad scale. Research in the field of laccases has been accelerated because of its wide diversity, utility, and enzymology. This paper deals with recent trends in implementation of the laccases in all practical possibilities with the help of optimizing various parameters and techniques which are responsible for mass production of the enzyme in industries.
Keywords: Laccase, enzyme, de-lignify, bioremediation, enzymology, multi-copper oxidases.
Graphical Abstract
[1]
Rochefort D, Kouisni L, Gendron K. Physical immobilization of laccase on an electrode by means of poly (ethyleneimine) microcapsules. J Electroanal Chem 2008; 617: 53-63.
[2]
Williamson PR. Biochemical and molecular characterization of the diphenol oxidase of Cryptococcus neoformans: identification as a laccase. J Bacteriol 1994; 176: 656-64.
[4]
Levine WG. Laccase, a review. In: Peisach J, Ed. The Biochemistry of Copper. New York: Academic Press Inc. 1965; pp. 371-85.
[5]
Bertrand G. Simultaneous occurence of laccase and tyrosinase in the juice of some mushrooms. C R Hebd Seances Acad Sci 1896; 123: 463-5.
[6]
Diamantidis G, Effosse A, Potier P, et al. Purification and characterization of the first bacterial laccase in the rhizospheric bacterium Azospirillum lipoferum. Soil Biol Biochem 2000; 32: 919-27.
[7]
Martins LO, Soares CM, Pereira MM, et al. Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J Biol Chem 2002; 277: 18849-59.
[8]
Suzuki T, Endo K, Ito M, et al. A thermostable laccase from Streptomyces lavendulae REN-7: purification, characterization, nucleotide sequence, and expression. Biosci Biotechnol Biochem 2003; 67: 2167-75.
[9]
Arias ME, Arenas M, Rodríguez J, et al. Kraft pulp biobleaching and mediated oxidation of a nonphenolic substrate by laccase from Streptomyces cyaneus CECT 3335. J Appl Environ Microbiol 2003; 69: 1953-8.
[10]
Jimenez-Juarez N, Roman-Miranda R, Baeza A, et al. Alkali and halide-resistant catalysis by the multipotent oxidase from Marinomonas mediterranea. J Biotechnol 2005; 117: 73-82.
[12]
Xu F. Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 1996; 35: 7608-14.
[13]
Freeman JC, Nayar PG, Begley TP, et al. Stoichiometry and spectroscopic identity of copper centers in phenoxazinone synthase: a new addition to the blue copper oxidase family. Biochemistry 1993; 32: 4826-30.
[14]
Bourbonnais R, Paice M, Reid I, et al. Lignin oxidation by laccase isozymes from Trametes versicolor and role of the mediator 2, 2′-azinobis (3-ethylbenzthiazoline-6-sulfonate) in kraft lignin depolymerization. Appl Environ Microbiol 1995; 61: 1876-80.
[15]
Leontievsky A, Myasoedova N, Pozdnyakova N, et al. Yellow’laccase of Panus tigrinus oxidizes non‐phenolic substrates without electron‐transfer mediators. FEBS Lett 1997; 413: 446-8.
[16]
Dittmer NT, Suderman RJ, Jiang H, et al. Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae. Insect Biochem Mol 2004; 34: 29-41.
[17]
Archibald F, Bourbonnais R, Jurasek L, et al. Kraft pulp bleaching and delignification by Trametes versicolor. J Biotechnol 1997; 53: 215-36.
[18]
Duran N, Esposito E. Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: a review. Appl Catal B 2000; 28: 83-99.
[19]
Gianfreda L, Xu F, Bollag J-M. Laccases: a useful group of oxidoreductive enzymes. Bioremediat J 1999; 3: 1-26.
[22]
Li K, Xu F, Eriksson K-EL. Comparison of fungal laccases and redox mediators in oxidation of a nonphenolic lignin model compound. Appl Environ Microbiol 1999; 65: 2654-60.
[23]
Pickard MA, Hashimoto A. Stability and carbohydrate composition of chloroperoxidase from Caldariomyces fumago grown in a fructose–salts medium. Can J Microbiol 1988; 34: 998-1002.
[24]
Call H, Mücke I. History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lignozym®-process). J Biotechnol 1997; 53: 163-202.
[25]
Shleev S, Morozova O, Nikitina O, et al. Comparison of physico-chemical characteristics of four laccases from different basidiomycetes. Biochimie 2004; 86: 693-703.
[26]
Piontek K, Antorini M, Choinowski T. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers. J Biol Chem 2002; 277: 37663-9.
[27]
Rodriguez A, Falcon M, Carnicero A, et al. Laccase activities of Penicillium chrysogenum in relation to lignin degradation. Appl Microbiol Biotechnol 1996; 45: 399-403.
[28]
Lee KH, Wi SG, Singh AP, et al. Micromorphological characteristics of decayed wood and laccase produced by the brown-rot fungus Coniophora puteana. J Wood Sci 2004; 50: 281-4.
[29]
Mansur M, Suárez T, Fernández-Larrea JB, et al. Identification of a laccase gene family in the new lignin-degrading basidiomycete CECT 20197. Appl Environ Microbiol 1997; 63: 2637-46.
[30]
Stajić M, Persky L, Friesem D, et al. Effect of different carbon and nitrogen sources on laccase and peroxidases production by selected Pleurotus species. Enzyme Microb Technol 2006; 38: 65-73.
[31]
Lee Y-R, Park C-H, Lee B-H, et al. Effect of nutrients on the production of extracellular enzymes for decolorization of reactive blue 19 and reactive black 5. J Microbiol Biotechnol 2006; 16: 226-31.
[32]
Keyser P, Kirk T, Zeikus J. Ligninolytic enzyme system of Phanaerochaete chrysosporium: synthesized in the absence of lignin in response to nitrogen starvation. J Bacteriol 1978; 135: 790-7.
[33]
Leatham GF, Kirk TK. Regulation of ligninolytic activity by nutrient nitrogen in white-rot basidiomycetes. FEMS Microbiol Lett 1983; 16: 65-7.
[34]
D’Souza-Ticlo D, Verma AK, Mathew M, et al. Effect of nutrient nitrogen on laccase production, its isozyme pattern and effluent decolorization by the fungus NIOCC# 2a, isolated from mangrove wood. Indian J Mar Sci 2006; 35: 364-72.
[35]
Heinzkill M, Bech L, Halkier T, et al. Characterization of laccases and peroxidases from wood-rotting fungi (family Coprinaceae). Appl Environ Microbiol 1998; 64: 1601-6.
[36]
Elisashvili V, Penninckx M, Kachlishvili E, et al. Lentinus edodes and Pleurotus species lignocellulolytic enzymes activity in submerged and solid-state fermentation of lignocellulosic wastes of different composition. Bioresour Technol 2008; 99: 457-62.
[37]
Monteiro M, De Carvalho M. Pulp bleaching using laccase from Trametes versicolor under high temperature and alkaline conditions. Biotechnol Fuel Chemical Spring 1998; 70-72: 983-93.
[38]
Buswell JA, Cai Y, Chang S-T. Effect of nutrient nitrogen and manganese on manganese peroxidase and laccase production by Lentinula (Lentinus) edodes. FEMS Microbiol Lett 1995; 128: 81-7.
[39]
Lee I-Y, Jung K-H, Lee C-H, et al. Enhanced production of laccase in Trametes vesicolor by the addition of ethanol. Biotechnol Lett 1999; 21: 965-8.
[40]
Xavier A, Evtuguin D, Ferreira R, et al. Laccase production for lignin oxidase activity Proceedings of 8th International Conference on Biotechnology. Korea. 2017.
[41]
Eggert C, Temp U, Eriksson K-E. The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase. Appl Environ Microbiol 1996; 62: 1151-8.
[42]
Pointing S, Jones E, Vrijmoed L. Optimization of laccase production by Pycnoporus sanguineus in submerged liquid culture. Mycologia 2000; 139-44.
[43]
Zadrazil F, Gonser A, Lang E. Influence of incubation temperature on the secretion of extracellular ligninolytic enzymes of Pleurotus sp. and Dichomitus squalens into soil. Proceedings of the conference on enzymes in the environment: activity, ecology and applicants. CRC Press, 2002.
[44]
Lema J, Roca E, Sanroman A, et al. Pulsating bioreactors Multiphase Bioreactor Design. CRC Press 2001.
[45]
Blánquez P, Casas N, Font X, et al. Mechanism of textile metal dye biotransformation by Trametes versicolor. Water Res 2004; 38: 2166-72.
[46]
Blánquez P, Sarrà M, Vicent M. Study of the cellular retention time and the partial biomass renovation in a fungal decolourisation continuous process. Water Res 2006; 40: 1650-6.
[47]
Romero S, Blánquez P, Caminal G, et al. Different approaches to improving the textile dye degradation capacity of Trametes versicolor. Biochem Eng J 2006; 31: 42-7.
[48]
Blánquez P, Caminal G, Sarra M, et al. The effect of HRT on the decolourisation of the Grey Lanaset G textile dye by Trametes versicolor. Chem Eng J 2007; 126: 163-9.
[49]
Couto SR, Sanromán MA, Hofer D, et al. Stainless steel sponge: a novel carrier for the immobilisation of the white-rot fungus Trametes hirsuta for decolourization of textile dyes. Bioresour Technol 2004; 95: 67-72.
[50]
Couto SR, Sanromán M, Hofer D, et al. Production of laccase by Trametes hirsuta grown in an immersion bioreactor and its application in the docolorization of dyes from a leather factory. Eng Life Sci 2004; 4: 233-8.
[51]
Sedarati MR, Keshavarz T, Leontievsky AA, et al. Transformation of high concentrations of chlorophenols by the white-rot basidiomycete Trametes versicolor immobilized on nylon mesh. Electron J Biotechnol 2003; 6: 104-14.
[52]
Pandey A, Selvakumar P, Soccol CR, et al. Solid state fermentation for the production of industrial enzymes. Curr Sci 1999; 149-62.
[53]
Couto SR, Toca-Herrera JL. Laccase production at reactor scale by filamentous fungi. Biotechnol Adv 2007; 25: 558-69.
[54]
Lorenzo M, Moldes D, Couto SR, et al. Improving laccase production by employing different lignocellulosic wastes in submerged cultures of Trametes versicolor. Bioresour Technol 2002; 82: 109-13.
[55]
Kahraman SS, Gurdal IH. Effect of synthetic and natural culture media on laccase production by white rot fungi. Bioresour Technol 2002; 82: 215-7.
[56]
Marques De Souza CG, Zilly A, Peralta RM. Production of laccase as the sole phenoloxidase by a Brazilian strain of Pleurotus pulmonarius in solid state fermentation. J Basic Microbiol 2002; 42: 83-90.
[57]
Couto SR, Moldes D, Liébanas A, et al. Investigation of several bioreactor configurations for laccase production by Trametes versicolor operating in solid-state conditions. Biochem Eng J 2003; 15: 21-6.
[58]
Couto SR, Lopez E, Sanromán MA. Utilisation of grape seeds for laccase production in solid-state fermentors. J Food Eng 2006; 74: 263-7.
[59]
Rosales E, Couto SR, Sanromán MA. Increased laccase production by Trametes hirsuta grown on ground orange peelings. Enzyme Microb Technol 2007; 40: 1286-90.
[60]
Aramayo R, Timberlake WE. Sequence and molecular structure of the Aspergillus nidulans yA (laccase I) gene. Nucleic Acids Res 1990; 18: 3415.
[61]
Saloheimo M, Niku-Paavola M-L, Knowles JK. Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata. Microbiology 1991; 137: 1537-44.
[62]
Galhaup C, Goller S, Peterbauer CK, et al. Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ionsa. Microbiology 2002; 148: 2159-69.
[64]
Hong F, Meinander NQ, Jönsson LJ. Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris. Biotechnol Bioeng 2002; 79: 438-49.
[65]
Collins PJ, Dobson A. Regulation of laccase gene transcription in Trametes versicolor. Appl Environ Microbiol 1997; 63: 3444-50.
[66]
Sethuraman A, Akin DE, Eisele JG, et al. Effect of aromatic compounds on growth and ligninolytic enzyme production of two white rot fungi Ceriporiopsis subvermispora and Cyathus stercoreus. Can J Microbiol 1998; 44: 872-85.
[67]
Couto SR, Herrera JLT. Industrial and biotechnological applications of laccases: a review. Biotechnol Adv 2006; 24: 500-13.
[69]
Minussi RC, Rossi M, Bologna L, et al. Phenols removal in musts: strategy for wine stabilization by laccase. Mol Catal B Enzym 2007; 45: 102-7.
[70]
Servili M, De Stefano G, Piacquadio P, et al. A novel method for removing phenols from grape must. Am J Enol Vitic 2000; 51: 357-61.
[72]
Minussi RC, Pastore GM, Durán N. Potential applications of laccase in the food industry. Trends Food Sci Technol 2002; 13: 205-16.
[73]
Ribeiro DS, Henrique S, Oliveira LS, et al. Enzymes in juice processing: a review. Int J Food Sci Technol 2010; 45: 635-41.
[74]
de Souza Bezerra TM, Bassan JC, de Oliveira Santos VT, et al. Covalent immobilization of laccase in green coconut fiber and use in clarification of apple juice. Process Biochem 2015; 50: 417-23.
[75]
Lettera V, Pezzella C, Cicatiello P, et al. Efficient immobilization of a fungal laccase and its exploitation in fruit juice clarification. Food Chem 2016; 196: 1272-8.
[76]
Yagüe S, Terrón MC, González T, et al. Biotreatment of tannin‐rich beer‐factory wastewater with white‐rot basidiomycete Coriolopsis gallica monitored by pyrolysis/gas chromatography/mass spectrometry. Rapid Commun Mass Spectrom 2000; 14: 905-10.
[77]
González T, Terrón MC, Yagüe S, et al. Pyrolysis/gas chromatography/mass spectrometry monitoring of fungal‐biotreated distillery wastewater using Trametes sp. I-62 (CECT 20197). Rapid Commun Mass Spectrom 2000; 14: 1417-24.
[78]
Konstantinou IK, Albanis TA. TiO2-assisted photocatalytic degradation of azo dyes in aqueous solution: kinetic and mechanistic investigations: a review. Appl Catal B 2004; 49: 1-14.
[79]
Mishra G, Tripathy M. A critical review of the treatments for decolourization of textile effluent. Colourage 1993; 40: 35.
[80]
Banat IM, Nigam P, Singh D, et al. Microbial decolorization of textile-dyecontaining effluents: a review. Bioresour Technol 1996; 58: 217-27.
[81]
Raghukumar C. Fungi from marine habitats: an application in bioremediation. Mycol Res 2000; 104: 1222-6.
[82]
Cameron M, Timofeevski S, Aust S. Enzymology of Phanerochaete chrysosporium with respect to the degradation of recalcitrant compounds and xenobiotics. Appl Microbiol Biotechnol 2000; 54: 751-8.
[83]
Maceiras R, Rodríguez-Couto S, Sanroman A. Influence of several activators on the extracellular laccase activity and in vivo decolourization of poly R-478 by semi-solid-state cultures of Trametes versicolor. Eng Life Sci 2001; 21: 255-64.
[84]
Pointing SB, Vrijmoed L. Decolorization of azo and triphenylmethane dyes by Pycnoporus sanguineus producing laccase as the sole phenoloxidase. World J Microbiol Biotechnol 2000; 16: 317-8.
[85]
Rodriguez E, Pickard MA, Vazquez-Duhalt R. Industrial dye decolorization by laccases from ligninolytic fungi. Curr Microbiol 1999; 38: 27-32.
[86]
Yavuz M, Kaya G, Aytekin Ç. Using Ceriporiopsis subvermispora CZ-3 laccase for indigo carmine decolourization and denim bleaching. Int Biodeterior Biodegradation 2014; 88: 199-205.
[87]
Iracheta-Cárdenas MM, Rocha-Peña MA, Galán-Wong LJ, et al. A Pycnoporus sanguineus laccase for denim bleaching and its comparison with an enzymatic commercial formulation. J Environ Manage 2016; 177: 93-100.
[88]
Tzanov T, Basto C, Gübitz GM, et al. Laccases to improve the whiteness in a conventional bleaching of cotton. Macromol Mater Eng 2003; 288: 807-10.
[89]
Rodríguez-Couto S. Laccases for denim bleaching: an eco-friendly alternative. Open Text J 2012; 1: 10-2.
[90]
Sousa AC, Martins LO, Robalo MP. Laccase‐catalysed homocoupling of primary aromatic amines towards the biosynthesis of dyes. Adv Synth Catal 2013; 355: 2908-17.
[91]
Blanco CD, González MD, Monmany JMD, et al. Dyeing properties, synthesis, isolation and characterization of an in situ generated phenolic pigment, covalently bound to cotton. Enzyme Microb Technol 2009; 44: 380-5.
[92]
Kunamneni A, Plou FJ, Ballesteros A, et al. Laccases and their applications: a patent review. Recent Pat Biotechnol 2008; 2: 10-24.
[96]
Gonçalves MLF, Steiner W. Purification and characterization of laccase from a newly isolated wood-decaying fungus, USA. ACS Symp Ser 1996.
[97]
Felby C, Pedersen LS, Nielsen BR. Enhanced auto adhesion of wood fibers using phenol oxidases. Wood Res Technol 1997; 51: 281-6.
[98]
Lund M, Ragauskas A. Enzymatic modification of kraft lignin through oxidative coupling with water-soluble phenols. Appl Microbiol Biotechnol 2001; 55: 699-703.
[99]
Bourbonnais R, Paice M, Freiermuth B, et al. Reactivities of various mediators and laccases with kraft pulp and lignin model compounds. Appl Environ Microbiol 1997; 63: 4627-32.
[100]
Xu H, Bloomfield K, Lund H. Chlorine dioxide
treatment compositions and processes. WO20061
26983A1, 2015.
[101]
Bauer CG, Kühn A, Gajovic N, et al. New enzyme sensors for morphine and codeine based on morphine dehydrogenase and laccase. Fresenius J Anal Chem 1999; 364: 179-83.
[102]
Jarosz-Wilkołazka A, Ruzgas T, Gorton L. Use of laccase-modified electrode for amperometric detection of plant flavonoids. Enzyme Microb Technol 2004; 35: 238-41.
[103]
Ellouze M, Sayadi S. White-rot fungi and their enzymes as a biotechnological tool for xenobiotic bioremediation. In: Saleh HEM, Rahman ROA, Eds. Manage Hazard Waste. London: InTech 2016.
[104]
Martelé Y, Callewaert K, Naessens K, et al. Controlled patterning of biomolecules on solid surfaces. Mater Sci Eng C 2003; 23: 341-5.
[105]
Rodríguez-Delgado MM, Alemán-Nava GS, Rodríguez-Delgado JM, et al. Laccase-based biosensors for detection of phenolic compounds. TrAC Trend Anal Chem 2015; 74: 21-45.
[106]
Di Fusco M, Tortolini C, Deriu D, et al. Laccase-based biosensor for the determination of polyphenol index in wine. Talanta 2010; 81: 235-40.
[107]
MacVittie K. Conlon, Katz E. A wireless transmission system powered by an enzyme biofuel cell implanted in an orange. Bioelectrochemistry 2015; 106: 28-33.
[108]
Chen T, Barton SC, Binyamin G, et al. A miniature biofuel cell. J Am Chem Soc 2001; 123: 8630-1.
[109]
Sunagawa K, Sugimachi M, Inagaki M. Micro integrated
cardiac pacemaker and distributed cardiac pacing
system. EP1541191A1, 2011.
[110]
Sakai H, Tomita T, Takagi R, et al. Fuel cell with
sequential enzymatic reactions. US8076035B2, 2011.
[111]
Kubo W, Nomoto T, Yano T. Enzyme electrode, and
device, sensor, fuel cell and electrochemical reactor
employing the enzyme electrode. WO2006/009324, 2006.
[113]
Heller A, Mano N, Kim H-H, et al. Miniature biological
fuel cell that is operational under physiological
conditions, and associated devices and methods.
WO/2003/106966, 2003.
[114]
Wang B, Yan Y, Tian Y, et al. Heterologous expression and characterisation of a laccase from Colletotrichum lagenarium and decolourisation of different synthetic dyes. World J Microbiol Biotechnol 2016; 32: 40.
[115]
Zeng J, Zhu Q, Wu Y, et al. Oxidation of polycyclic aromatic hydrocarbons using Bacillus subtilis CotA with high laccase activity and copper independence. Chemosphere 2016; 148: 1-7.
[116]
Amitai G, Adani R, Sod-Moriah G, et al. Oxidative biodegradation of phosphorothiolates by fungal laccase. FEBS Lett 1998; 438: 195-200.
[117]
Bastos AC, Magan N. Trametes versicolor: potential for atrazine bioremediation in calcareous clay soil, under low water availability conditions. Int Biodeterior Biodegradation 2009; 63: 389-94.
[118]
Corcoran E. Sick water? The central role of wastewater management in sustainable development: a rapid response assessment. UNEP/Earthprint 2010.
[119]
Bilal M, Asgher M, Iqbal HM, et al. Bio-catalytic performance and dye-based industrial pollutants degradation potential of agarose-immobilized MnP using a Packed Bed Reactor System. Int J Biol Macromol 2017; 102: 582-90.
[120]
Bilal M, Asgher M, Iqbal HM, et al. Bio-based degradation of emerging endocrine-disrupting and dye-based pollutants using cross-linked enzyme aggregates. Environ Sci Pollut Res Int 2017; 24: 7035-41.
[121]
Bilal M, Asgher M, Parra-Saldivar R, et al. Immobilized ligninolytic enzymes: an innovative and environmental responsive technology to tackle dye-based industrial pollutants–a review. Sci Total Environ 2017; 576: 646-59.
[122]
Bilal M, Iqbal HM, Hu H, et al. Development of horseradish peroxidase-based cross-linked enzyme aggregates and their environmental exploitation for bioremediation purposes. J Environ Manage 2017; 188: 137-43.
[123]
Chatha SAS, Asgher M, Iqbal HM. Enzyme-based solutions for textile processing and dye contaminant biodegradation-a review. Environ Sci Pollut Res 2017; 24: 14005-18.
[124]
Ahmed I, Iqbal HM, Dhama K. Enzyme-based biodegradation of hazardous pollutants-An overview. J Exp Biol Agric Sci 2017; 5: 402-11.
[125]
Daughton CG, Ternes TA. Pharmaceuticals and personal care products in the environment: agents of subtle change? Environ Health Perspect 1999; 107: 907.
[126]
Rezg R, El-Fazaa S, Gharbi N, et al. Bisphenol A and human chronic diseases: current evidences, possible mechanisms, and future perspectives. Environ Int 2014; 64: 83-90.
[127]
Barrios-Estrada C, de Jesús Rostro-Alanis M, Muñoz-Gutiérrez BD, et al. Emergent contaminants: Endocrine disruptors and their laccase-assisted degradation–A review. Sci Total Environ 2018; 612: 1516-31.
[128]
Chen S-C, Chen C-H, Chern C-L, et al. p-Phenylenediamine induces p53-mediated apoptosis in Mardin–Darby canine kidney cells. Toxicol In Vitro 2006; 20: 801-7.
[129]
Huang Y-C, Hung W-C, Kang W-Y, et al. p-Phenylenediamine induced DNA damage in SV-40 immortalized human uroepithelial cells and expression of mutant p53 and COX-2 proteins. Toxicol Lett 2007; 170: 116-23.
[130]
Piscitelli A, Pezzella C, Lettera V, et al. Fungal laccases: structure, function and applications. FL: CRC Press 2013.
[132]
Brinch D, Pedersen P. Toxicological studies on laccase from Myceliophthora thermophila expressed in Aspergillus oryzae. Regul Toxicol Pharmacol 2002; 35: 296-307.
[133]
Onuki T, Nogucji M, Mitamura J. Oxidative hair dye composition containing laccase. Pat Int Appl WO 2000; 37: 789-94.
[134]
Golz-Berner K, Walzel B, Zastrow L, et al. Cosmetic
and dermatological preparation containing copperbinding
proteins for skin lightening. WO2004017931, 2004.
[135]
Lang G, Cotteret J. Dyeing composition containing a
laccase and keratinous fiber dyeing methods using
same. US6471730B1, 2002.
[136]
Lang G, Cotteret J. Keratinous fibre oxidation dyeing
compositions containing a laccase and dyeing method
using same. US6537328B1, 2003.
[137]
Plos G. Oxidation dyeing method using Nacetyclysteine
as a reducing agent and laccase as an
oxidating agent. US6840964B1, 2005.
[141]
Pereira R, Burgaud H. Producing tetraazapentamethine
compounds comprises reacting an azine compound
with an oxidizing agent, useful for dyeing
keratinic fibers, eg hair. FR2863487A, 2005.
[142]
Nakajima M, Fujita H, Kikuchi Y, et al. Cosmetic
mixture for the oxidation tinting of keratin fibres,
containing in a support material suitable for tinting
keratin fibres (a) at least one laccase-type enzyme; (b)
at least one polymer thickener selected from polymers.
US20020043731A1, 2002.
[144]
Doucet O, Golz-Berner K, Walzel B, et al. Cosmetic
or dermatological preparation with skin-lightening
proteins. WO2004/017931, 2004.
[146]
Fernández-Fernández M, Sanromán MÁ, Moldes D. Recent developments and applications of immobilized laccase. Biotechnol Adv 2013; 31: 1808-25.
[147]
Ibarra-Escutia P, Gómez JJ, Calas-Blanchard C, et al. Amperometric biosensor based on a high resolution photopolymer deposited onto a screen-printed electrode for phenolic compounds monitoring in tea infusions. Talanta 2010; 81: 1636-42.
[148]
Arroyo M. Inmovilización de enzimas. Fundamentos, métodos y aplicaciones. Ars Pharmaceutica 1998; 39: 23-39.
[149]
Bryjak J, Kruczkiewicz P, Rekuć A, et al. Laccase immobilization on copolymer of butyl acrylate and ethylene glycol dimethacrylate. Biochem Eng J 2007; 35: 325-32.
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