Comparative Studies on the Blue and Yellow Laccases

Pankaj Kumar Chaurasia¹, Shashi Lata Bharati¹ and Sunil Kumar Singh^1,

¹Department of Chemistry, Gorakhpur University, Gorakhpur (U. P.), India

Cite this paper:
Pankaj Kumar Chaurasia, Shashi Lata Bharati and Sunil Kumar Singh. Comparative Studies on the Blue and Yellow Laccases. Research in Plant Sciences. 2013; 1(2):32-37. doi: 10.12691/plant-1-2-5

Abstract

In the modern time enzymatic works have achieved a sound attention due to their successful involvements in several types of tedious syntheses without generating any type of environmentally harmful pollutants. It has also been proved that laccases have such types of capabilities to perform several environmentally safe roles in food, paper-pulp, textile, cosmetics, nanotechnology, sugar industries, synthetic organic and drugs chemistry. In most cases, laccase mediator systems play very important roles and in such cases, reactions were difficult or impossible without mediators but the studies of yellow laccases and their capabilities to oxidize phenolic lignin model compounds without help of any mediator systems have good future with several possibilities in industrial and medicinal areas. In the above respects, this review represents the concise and compact comparative studies on blue and yellow laccases with their different important properties.

Keywords:
blue laccase yellow laccase mediators lignin model compounds

This work is licensed under a Creative Commons Attribution 4.0 International License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

Figures

References:

[1]	Reishammer, B. and Malstrom B.G. Blue copper containing oxidases in copper proteins and copper enzymes (R. Lontie ed) CRC Press Inc., Boca Raton Flovida, 3. 1-35. 1984.
[2]	Solomon, E.L., Sundaram, U.M. and Machonkin, T.E. Multicopper oxidases and oxygenases, Chem. Rev., 96. 2563-2605. 1996.
[3]	Messerschmidt, A. Special structure of ascorbate oxidase, laccase and related proteins implication for catalytic mechanism, In: Multicopper Oxidase ed. Messerschmidt A, World Scientific, Singapore, 23-80. 1997.
[4]	Yadav, M. and Yadav, K.D.S. “Structural and functional aspects of lignolytic enzymes, In:“Lignocellulose Biotechnology: Future Prospects” Kuhad R.C. and Singh A. eds. I. K. Internal Publishing House, Pvt. Ltd. New Delhi, 63-88. 2007.
[5]	Dwivedi, U.N., Singh, P., Pandey, V.P. and Kumar, A. Structure – function relationship among bacteria fungal and plant laccases: a review. J. Mol. Catal. B. Enzymatic, 68.117-128. 2011.
[6]	Bao, W., Mally, D.M.O., Whetten, R. and Sederoff, R.R. A laccase associated with lignification of ioblolly pine xylem, Science, 260. 672-674. 1973.
[7]	Huang, H.W., Zoppellero, G. and Sakurai, T. Spectroscopic and kinetic studies on oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus Vernicifera laccase, J. Biol. Chem. 274, 3271-3272. 1999.
[8]	Messerschmidt, A. and Huber, R. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin-Modelling and structural relationships, Europ. J. Biochem., 187(2). 341-352. 1990.
[9]	Mayer, A.M. and Staples, R.C. Laccase: new functions for an old enzyme, Phytochem. 60. 551-565. 2002.
[10]	Giardina, P., Cannio, R., Martirani, L., Marzullo, L., Palmieri, G. and Sannia, G. Cloning and sequencing of a laccase gene from the lignin degrading basidiomycete Pleurotus ostreotus, Appl. Environ. Microbiol. 61. 2408-2413. 1995.
[11]	Jonsoon, L.K. Sjostrom, K., Haggstrom, I. and Nymom, P.O., Characterization of a laccase gene from white rot fungus Trametes versicolor and structural feature of basidiomycete laccases, Chem. Biophys. Acta., 12(51). 210-215. 1995.
[12]	Yaver, D.S., F., Xu, Golightly, E.J., Brown, K.M., Brown, S.H., Rey, M.W., Schneider, Halkier, T., Mondorf, K. and Dalboge, H. Purification, characterization, molecular cloning and expression of two laccase genes from the white rot basidiomycete Trametes villosa, Appl. Environ. Microbiol., 62. 834-841. 1996.
[13]	Eggert, C., Lafayette, P.R., Temp, U., Karl-Erik, L.E. and Dean, J.F.D. Molecular analysis of a laccase gene from the white rot fungus Pycnoporus cinnabarius, Appl. Environ. Microbiol., 64. 1766-1772. 1998.
[14]	Yaver, D.S., Overjero, M.D.C., Xu, F., Nelson, B. A., Brown, K.M., Halkier, T., Bernauer, S., Brown, S.H. and Kauppinen, S. Molecular characterization of laccase gene from the basidiomycete Coprinus cinereus and heterologous expression of the laccase LCC 1, Appl. Environ. Microbial., 65. 4943-4948. 1999.
[15]	Germann, U. A., Muller, G., Hunziker, P. E. and Lerch, K. Characterization of two allelic forms of Neurospora crassa laccase, J. Biol. Chem., 263. 885-896. 1988.
[16]	Aramayo, R. and Timberlake, W.E. Sequence and molecular structure of the Aspergillus nidulaus YA (laccase I) gene, Nucleic Acids Res., 18. 3415. 1990.
[17]	Fernandez-Larrea, J. and Stahl, U. Isolation and characterization of a laccase gene from Podospora anserine, Mol. Gen. Genet., 252. 539-551. 1996.
[18]	Berka, R.M., Schneider, P., Golightly, E.J., Brown, S.H., Madden, M., Brown, K.M., Halkier, T., Mondrof, K. and Xu, F. Characterization of the gene encoding an extracellular laccase of Mycelio phtorathermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzea, Appl. Environ. Microbiol., 63. 3151-3157. 1997.
[19]	Enguita, F. J. Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis, J. Biol. Chem., 279. 23472-23476. 2004.
[20]	Givaudan, A., Effose, A., Faure, D., Potier, P., Bouillant, M. L. and Bally, R. Polyphenol oxidase from Azospirillum lipoferum, FEMS Microbiol. Lett., 108. 205-210. 1993.
[21]	Sanchez-Amat, A., Lucas-Elio, A.P., Fernandez, E., Garcia-Borron, J. C. and Solamo, F. Molecular cloning and functional characterization of a unique multipotent polyphenol oxidase from Marinomonas mediterranea, Biochem. Biophys. Acta., 1547. 104-116. 2001.
[22]	Thomas, B.R., Yonekura, M., Morgan, T.D., Czapla, T.H., Hopins, T.L. and Kramer, K.J. A trypsin solubilised laccase from phrate pupal integument of the tobacco hornworm, Manduca sexta insect, Biochem., 19. 611-622. 1989.
[23]	Parkinson, N. and Smith, I., Weaver, R. and Edwards, J.P. A new form of arthropod phenol oxidase is abundant in venom of the parasitoid wasp Punpla hypochondrica, Insect Biochem. Mol. Biol., 31. 57-63. 2001.
[24]	Wandrey, C. and Liese, A., Kihumbn, D. and Kumar A. Industrial biocatalysis: Past, present and future, Org. Proc. Res. Dev., 4(4). 285-290. 2000.
[25]	Feng, Xu. Application of oxidoreductase: Recent progress, Ind. Biotechnol., 1(1). 38-50. 2005.
[26]	Couto, S.R. and Harrera, J.L.T. Industrial and biotechnological applications of laccases: A review, Biotechnol. Adv., 24. 500-513. 2006.
[27]	Bourbonnais, R.E. and Paice, M.G. Oxidation of non-phenolic substrates: an extended role for laccase in lignin biodegradation, FEBS Lett., 267. 99-102. 1990.
[28]	Morozova, O.V., Shumakovich, G.P., Shleev, S.V. and Yaropolov, Ya. I. Laccase mediator systems and their applications-A review, Appl. Biochem. Microbiol., 43. 523-535. 2007.
[29]	Quinatanar, L., Yoon, J., Aznar C.P., Palmer, A.E., Andersson, K.K., Britt, R.D. and Solomon, E.I. Spectroscopic and electronic structure studies of the trinuclear Cu cluster active site of the multicopper oxidase laccase: nature of its co-ordination unsaturation, J. Am. Chem. Soc., 127. 13832-13885. 2005.
[30]	Leontievsky, A.A., Vares, T., Lankinen, P., Shergill, J.K., Pozdnyakova, N.N., Myasoedova, N.M., Kalkkinen, N., Golovleva, L.A., Cammack, R., Thurston, C.F. and Hataka, A. Blue and yellow laccases of lignolytic fungi, FEBS Microbiol Letts., 156. 9-14. 1997.
[31]	Leontievsky, A., Myasoedova, N., Pozdnyakova, N. and Golovleva, L. Yellow laccase of Panus tigrinus oxidizes non-phenolic substrates without electron transfer mediators, FEBS Lett., 413. 446-448. 1997.
[32]	Chaurasia, P.K., Yadav, R.S.S. and Yadava, S. Purification and characterization of laccase secreted by Phellinus linteus MTCC-1175 and its role in the selective oxidation of aromatic methyl group, Appl. Biochem. Microbiol., 49(6). 592–599. 2013.
[33]	Chaurasia, P.K., Yadav, R.S.S. and Yadava, S. Purification and characterization of laccase from Coriolopsis floccosa MTCC-1177 and its use in the selective oxidation of aromatic methyl group to aldehyde without mediators, J. Chem. Sci., JCSC-D-12-00832 (Accepted) (2013).
[34]	Bourbonnais, R., Paice, M.G., Freiermuth, B., Bodie, E. and Borneman, S. Reactivities of various mediators and laccases with kraft pulp and lignin model compounds, Appl. Environ. Microbiol., 63(12). 4627-4632. 1997.
[35]	Banci, L., Ciofi-Baffoni, S. and Tien, M. Lignin and Mn peroxidase-catalyzed oxidation of phenolic lignin oligomers, Biochem., 38(10). 3205-10. 1999.
[36]	Hildén, L., Johansson, G. Pettersson, G. Li, J., Ljungquist, P. and Henriksson, G. Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation? FEBS Lett., 477(1-2). 79-83. 2000.
[37]	Chaurasia, P.K., Yadav, R.S.S. and Yadava, S. A review on mechanism of laccase action, Res. Rev. Biosci., 7(2). 66-71. 2013.
[38]	[38a] Bourbonnais, R. and Paice, M.G. Modeling multicylinder paper drying-validation of a new simulation program, Tappi. Journal, 79(4). 199. 1996. [38b] Kunamneni, A., Ballesteros, A., Plou, F.J. and Alcalde, M. Fungal laccase – a versatile enzyme for biotechnological applications., Communicating Curr. Res. Educational Topics and Trends in Appl. Microbiol. A. Méndez-Vilas (Ed.), pp. 233–244, Formatex, Badajoz, Spain, 2007
[39]	Chaurasia, P.K., Yadav, R.S.S. and Yadava, S. Application of crude laccase of Xylaria polymorpha MTCC-1100 in selective oxidation of aromatic methyl group to aldehyde group, Biochem.: An Indian Journal, 6(7). 237-242. 2012.
[40]	Chaurasia, P.K., Yadav R.S.S., Yadava S. Selective biotransformation of aromatic methyl groups to aldehyde groups using crude laccase of Pleurotus ostreatus MTCC-1803, Int. J. Res. Chem. Environ., 3(1). 188-97. 2013.