Review Article (Open access)

Int. J. Life. Sci. Scienti. Res., 1(2): 71-73, November 2015

Laccase sources and their applications in environmental pollution

Sarvesh Kumar Mishra*, Shailendra Kumar Srivastava and Krishna Ash

Department of Microbiology and Microbial Technology, AAIDU, Allahabad, U.P, India

*Address for Correspondence: Sarvesh Kumar Mishra, Research Scholar, Department of Microbiology and Microbial Technology, AAIDU, Allahabad, U.P, India


ABSTRACT- Laccase are multicopper oxidases that are widely distributed among plants, insects, fungi and bacteria. Pollution increased with the time day by day, laccase is an oxido-reductase which play a significant role in remediation. These enzyme catalyze and one-electron oxidation of a wide variety of organic and inorganic substrate including mono-, di-, and poly-phenols, amino-phenols, metho-oxyphenols, aromatic amines, and ascorbate, with the concomitant four electron reduction of oxygen to water. Present study on their use in several industrial application, includes dye decolorization, detoxification of environmental pollutants and revalorization of waste and waste water etc. this review helps to understand the properties of these improvement enzymes for efficient utilization for its biotechnological and environmental applications. Now we provide a brief discussion of this interesting group of enzymes, increase knowledge of which will promote laccase based industrial process in future.

Keywords: Laccase, Biodegradation, Bioremediation and Dye decolorization.

Laccases (benzenediol: oxygen oxidoreductase, EC exist widely in nature and belongs to small group of enzymes called the blue copper protein or copper oxidases (Sivakumar et al. 2010). These are multicopper oxidases that are widely distributed among plants, insects, fungi and bacteria. These proteins are characterized by containing copper atoms. One copper is placed at the T1 site, where the reducing substrate binds and other three copper are clustered in which molecular oxygen binds. Laccases have received much attention of researchers in last decades due to their ability to oxidize both phenolic and non-phenolic lignin related compounds as well as highly recalcitrant environmental pollutants so it makes these biocatalysts very useful for their application in several biotechnological processes.

occurrence- Laccase is most widely distributed in a panoramic view of higher plant, insect, fungi and bacteria (Diamantidis et al. 2000).

Plant: Laccase in plants have been identified in tree (Mango, Pine etc), cabbages, turnip, beets, apples, asparagus, potatoes, pears and various vegetables (Levine 1965). Recently laccase has been expressed in the embryo of maize (Zea mays).

Insect:  The insect laccase is a long amino-terminal sequence characterized by unique domain consisting of several conserved cystine, aromatic and charged residues. Laccase are found in dozen of insects of genera that include Bombyx, Calliphora, Diploptera, Drosophilla, Lucilia, Manduca, Musca, Oryctes, Papilio, Phormia, Rhodnius, Sarcophaga, Schistocerca and Tenebrio (Xu 1999). Recently, two isoforms of laccase 2 gene have been found to catalyze larval, pupal and adult cuticle tanning in Tribolium castaneum (Arakane et al., 2005; Sharma and Kuhad 2008).

Fungi: Fungal laccase have higher redox potential than bacterial or plant. Most of the laccase described in literature was isolated from higher fungi. Laccase have been isolated from ascomycetes, deuteromycetes and basidiomycetes fungi (Assavaning et al. 1992). Laccase from Monicillium indicum was the first laccase to be characterized from an ascomycetes showing peroxidative activity (Thakkar et al. 1992). In fungi, ascomycetes and deuteromycetes have not been a focus for lignin degradation studies as much as the white-rot basidiomycetes . Most common laccase producers are the wood rotting fungi Trametes versicolor, Trametes hirsute, Trametes ochracea, Trametes villosa, Trametes gallica, Cerena maxima, Coriolposis polyzona, Lentinus tigrinus, Pleurotus erynngii, Pleurotus osteatus etc. (Morozoa et al. 2007).

Bacteria: Bacterial laccase was first reported in Azospirrilum lipoferum (Givaudan et al. 1993), it play a role in cell pigmentation, oxidation of phenolic compounds (Faure et al. 1994, 1995). Other name as E. coli, Bacillus subtilis, S. lavendulae, S.cyaneus, Marinomonas mediterranea, Aquifex aceolicus, Bacillus sp., Bacillus halodurans, Leptotrix discophora SS1, Oceano bacilusiheynesis (cotA), Alpha-proteobacterium SD21, Gama-proteobacterium JB, Pseudomonas fluorescens GB-1, Pseudomonas maltophila, Xanthomonas campesteris (copA), Pseudomonas putida GB-1 (cumA), Pseudomonas syringae pv tomato(copA), Pseudomonas aerophillum (pae1888), Streptomyces antibioticus, Streptomyces griseus (epoA), Thermus thermophillus (HB27) and Streptomyces psammoticus MTCC7334 etc. (Sharma et al., 2007)


Laccase in Environmental Pollutant- The goal of present work is to study and thoroughly compare the properties of laccase. Laccase is also used in bioremediation agent to clean up herbicides, pesticides and certain explosive in soil. Laccase is important because it oxidizes both the toxic and nontoxic substrates. It is utilized in textile industry, food processing industry, wood processing industry, pharmaceutical industry, and chemical industry. This enzyme is very specific, ecologically sustainable and a proficient catalyst.

A few laccases are at present in market for textile, food and other industries, and more candidates are being actively developed for future commercialization. A vast amount of industrial applications for laccases have been proposed and they include pulp and paper, textile, organic synthesis, environmental, food, pharmaceuticals and nano-biotechnology. Being specific, energy-saving and biodegradable, laccase-based biocatalysts fit well with the development of highly efficient, sustainable and eco-friendly industries.

Laccase in the Paper Industry- Making paper from wood requires separation of the wood fibres from each other and then reforming them into a sheet. In wood, lignin glues the fibres together. These fibres can be separated either by degradation and removal of lignin (chemical pulping), or by physically tearing the fibres apart (mechanical pulping). Chemical and mechanical pulps have different market niches. Many paper products contain both pulp types, in variable proportions depending on the required properties. Mechanical pulp is cheaper than chemical pulp because of its high yield (up to 95 % by weight of the starting material, in contrast to the yield from chemical pulping of wood is usually less than 50%), and capital cost. However the high lignin content of the mechanical pulp fibres detracts from the quality of the paper; because the fibres have little flexibility, they do not bond together, the paper has lower strength, and there is a tendency of the pulp to yellow on exposure to sunlight. In addition, mechanical pulping requires a lot of electrical energy, which in turn increases the cost.

Laccase in the Dye Decolourization- The treatment of industrial effluents containing aromatic compounds is necessary prior to final discharge to the environment (Khalifia et al., 2010). Nowadays, environmental regulations in most countries require that wastewater must be decolorized before its discharge (Molianen et al., 2010) to reduce environmental problem related to the effluent (Tavares et al., 2009). A newly isolate deuteromycetes fungus pestalotiopsis sp. has high potential producer of industrially important laccase and decolorization of azo dye (Hao et al., 2007). Laccases from the white-rot fungi Cerrena unicolor and Trametes hirsuta for their ability to decolorize simulated textile baths (Molianen et al., 2010).

Laccase in Waste Detoxification and Decontamination- Laccase has been used to oxidatively detoxify or remove various aromatic xenobiotics and pollutants found in industrial waste and contaminated soil or water. Laccase catalysis could result in direct degradation or polymerization/ immobilization. Reported example of direct dechlorination, cleavage of aromatic rings, mineralization of polycyclic aromatic hydrocarbons, decolorization of pulp or cotton mill effluent and bleaching of textile dyes. The process includes polymerization among pollutants themselves or copolymerization with other nontoxic substances (such as humic materials). Polymerized pollutants often become insoluble or immobilized, thus facilitating easy removal by such means as adsorption, sedimentation or filtration (Xu 1999).    

Laccase in Bioremediation and Biodegradation- Keum and li obtained laccase from T. versicolour and Pleurotus ostreatus for degradation of PCB as well as phenol. T. versicolour is used for the the bioremediation of atrazine in soil (Shraddha et al., 2011). T. villosa remediates the soil by degrading 2, 4- DCP (2, 4-dichlorophenol). Cerrena unicolor has the capability of reducing lignin content from sugarcane bagasse (D’sauza et al., 2009). Decolorization and detoxification of a textile industry effluent by laccase from Trametes trogii (Imran et al., 2012). Large amount of polyphenol is present in the beer factory wastewater which is present in dark brown in colour and degrade by the white-rot fungus Coriolopsis gallica (Yague et al., 2000). Laccase produced from Trametes sp. bioremediate the distillery wastewater generated from the sugarcane molasses fermentation with high content of organic matter (Gonzalez et al., 2000)

Laccase is ubiquitious in nature, being produced by various sources like plants, insect, fungi and also bacteria. The function of enzyme differs from organism to organism. Laccase play an important role in the carbon cycle and could help in degrading a wide range of xenoaromatics. They have many industrial applications because of their innate ability of oxidation of phenolic and nonphenolic compounds. Laccase enzyme has the property to act on a range of substrate and to detoxify a range of pollutants. They decolourize and detoxify the industrial effluents and help in wastewater treatment. They act on both phenolic and nonphenolic lignin related compounds as well as highly recalcitrant environmental pollutants which help researchers to put them in various biotechnological applications. 


1.      Arakane Y, Muthukrishnan S, Beeman RW, Kanost MR, Kramer KJ. Laccase 2 is the phenoloxidase gene required for beetle cuticle tanning. PNAS. 2005, 102: 11337-11342.

2.      Assavanig, A., Amornktticharoen, B., Ekpaisal, N., Meevootisom, V., and Flegel, T. W., “Isolation, characterization and function of laccase of Trichoderma,” Applied Microbiology Biotechnology, 1992, 38: 198-202.

3.      Diamantidis, G., Effosse, A., Potier, P., and Bally, R. “Purification and characterization of the first bacterial laccase in rhizospheric bacteria,” Azospirillum lipoferum, Soil Biology and Biochemistry, 2000, 32: 919-927.

4.      D'Souza-Ticlo, Sharma D., Raghukumar C. A Thermostable metaltolerant laccase with bioremediation potential from a marinederived fungus. Marine biotechnology., 2009, Vol.11, no.6, pp.725- 737.

5.      Faure D, Bouillant ML, Bally R. Isolation of Azospirillum lipoferum 4T Tn5 mutants affected in melanization and laccase activity. Appl Environ Microbiol.,1994, 60, 3413–3415.

6.      Givaudan A, Effosse A, Faure D, Potier P, Bouillant ML, Bally R . Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere : evidence for laccase activity in non-motile strains of Azospirillum lipoferum. FEMS Microbiol. Lett., 1993, 108: 205-210.

7.      Gonzalez T., Terron M.C., Yague S., Zapico E., Galletti G.C., Gonzalez A.E. Pyrolysis/gas chromatography/mass spectrometry monitoring of fungal-biotreated distillery waste water using trametes sp. I- 62(CECT20197). Rapid communications in mass spectrometry., 2000, Vol.14, no.15, pp.1417-1424.

8.      Hao J., Song F., Huang F., Yang C., Zhanng Z., Zheng Y., Tian X. .Production of laccase by a newly isolated deuteromycete fungus Pestalotiopsis sp. and its decolorization of azo dye. J. Ind. microbiol biotechnol., 2007, 34 (3):233-4017171552 cit: 4.

9.      Imran M., Asad J.M., Hadri H.S. and Mehmood S. . Production and industrial applications of laccase enzyme. Journal of cell and molecular biology, 2012, 10(1): 1-11, 2012.

10.  Khlifia R, Belbahria L, Woodwarda S, Ellouza M,Dhouiba A, Sayadia S, Mechichia T. Decolourization and detoxification of textile industry wastewater by the laccase-mediator system. J Hazard Mater., 2010, 75: 802–80.

11.  Levine, W.G. “Laccase, A review,” In : The Biochemistry of copper, Academic Press Inc., New York, 1965, pp. 371-385.

12.  Moilanen U, Osma JF, Winquist E, Leisola M,Couto SR. Decolorization of simulated textile dye baths by crude laccases from Trametes hirsute and Cerrena unicolor. Eng Life Sci., 2010,10 (3): 1–6.

13.  Morozova OV, Shumakovich GP, Gorbacheva MA, Shleev SV, Yaropolov AI. “Blue” Laccases. J .Biochem., 2007, 72(10): 1136-1150.

14.  Sadhasivam S, Savitha S, Swaminathan K, Lin FH.Production, purification and characterization of mid-redox potential laccase from a newly isolated Trichoderma harzianum WL1. Process biochem., 2008, 43: 736-742.

15.  Sharma KK and Kuhad RC. Laccase: enzyme revisited and function redefined. Ind J.Microbiol., 2008, 48: 309–316.

16.  Sharma P, Goel R, Caplash N. Bacterial laccases. World J Microbiol Biotechnol., 2007, 23: 823-832.

17.  Shraddha, Shekher R., Sehgal S., Kamthania M., Kumar A. Laccase: Microbial sources, Production, and potential Biotechnological applications. Enzyme Research, 2011; pp.11.

18.  Sivakumar R., Rajendran R., Balakumar C., Tamilvendan M. Isolation, Screening and Optimization of production medium for thermostable Laccase Production from Ganoderma sp. International journal of engineering science and technology , 2010, vol.2 (12), 7133-7141.

19.  Tavares APM, Cristovao RO, Gamelas JAF,Loureiro JM, Boaventuraa RAR, Macedoa EA. Sequential decolourization of reactive textile dyes by laccase mediator system. J Chem Technol Biotechnol., 2009, 84: 442–446, 2009.

20.  Thakker, G. D., Evans, C. S., and Rao, K. K., “Purification and characterization of laccase from Monocillium indicum,” Appl. Microbial Biotechnol., 1992, 37: 321-323.

21.  Xu. F., “Laccase,” In Flickinger, M. C. & Drew, S. W. (eds.), Encyclopedia of Bioprocess Technology: Fermentation, Biocatalysis, Bioseparation, John Wiley and Sons Inc., New York 1999, pp. 1545-1554.

22.  Yague S., Terron M.C., Gonzalez T. Biotreatment of tannin-rich beer-factory wastewater with white-rot basidiomycete coriolopsis gallica monitored by pyrolysis/gas chromatography/mass spectrometry. Rapid communications in mass spectrometry, 2000; 14(10): 905-910.