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Enzyme Research
Volume 2011 (2011), Article ID 376015, 10 pages
http://dx.doi.org/10.4061/2011/376015
Research Article

Laccase-Based CLEAs: Chitosan as a Novel Cross-Linking Agent

1Environmental Engineering Laboratory, Department of Civil Engineering, University of Sherbrooke, 2 500 Boulevard de l'Université, Sherbrooke, QC, Canada J1K 2R1
2Department of Chemical and Biotechnological Engineering, University of Sherbrooke, 2 500 Boulevard de l'Université, Sherbrooke, QC, Canada J1K 2R1
3Étienne-Le Bel Centre de Recherche Clinique, Centre Hospitalier Universitaire de Sherbrooke, 3001, 12e Avenue Nord, Sherbrooke, QC, Canada J1H 5N4

Received 15 April 2011; Accepted 18 May 2011

Academic Editor: J. Guisan

Copyright © 2011 Alexandre Arsenault et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. S. K. Ahuja, G. M. Ferreira, and A. R. Moreira, “Utilization of enzymes for environmental applications,” Critical Reviews in Biotechnology, vol. 24, no. 2-3, pp. 125–154, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. E. Torres, I. Bustos-Jaimes, and S. Le Borgne, “Potential use of oxidative enzymes for the detoxification of organic pollutants,” Applied Catalysis B, vol. 46, no. 1, pp. 1–15, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. P. Giardina, V. Faraco, C. Pezzella, A. Piscitelli, S. Vanhulle, and G. Sannia, “Laccases: a never-ending story,” Cellular and Molecular Life Sciences, vol. 67, no. 3, pp. 369–385, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. A. Kunamneni, I. Ghazi, S. Camarero, A. Ballesteros, F. J. Plou, and M. Alcalde, “Decolorization of synthetic dyes by laccase immobilized on epoxy-activated carriers,” Process Biochemistry, vol. 43, no. 2, pp. 169–178, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. H. Cabana, J. P. Jones, and S. N. Agathos, “Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals,” Journal of Biotechnology, vol. 132, no. 1, pp. 23–31, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. D. Wesenberg, I. Kyriakides, and S. N. Agathos, “White-rot fungi and their enzymes for the treatment of industrial dye effluents,” Biotechnology Advances, vol. 22, no. 1-2, pp. 161–187, 2003. View at Publisher · View at Google Scholar · View at Scopus
  7. V. Elisashvili, M. Penninckx, and E. et Kachlishvili, “White-rot basidiomycetes: lignocellulolytic enzymes production in bioconversion of plant raw materials,” International Biodeterioration and Biodegradation, 2006. View at Google Scholar
  8. L. Lu, M. Zhao, and Y. Wang, “Immobilization of laccase by alginate-chitosan microcapsules and its use in dye decolorization,” World Journal of Microbiology and Biotechnology, vol. 23, no. 2, pp. 159–166, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. N. Durán, M. A. Rosa, A. D'Annibale, and L. Gianfreda, “Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: a review,” Enzyme and Microbial Technology, vol. 31, no. 7, pp. 907–931, 2002. View at Publisher · View at Google Scholar · View at Scopus
  10. R. A. Sheldon, “Cross-linked enzyme aggregates (CLEA®s): stable and recyclable biocatalysts,” Biochemical Society Transactions, vol. 35, no. 6, pp. 1583–1587, 2007. View at Publisher · View at Google Scholar · View at Scopus
  11. H. Cabana, C. Alexandre, S. N. Agathos, and J. P. Jones, “Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals,” Bioresource Technology, vol. 100, no. 14, pp. 3447–3458, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. I. Matijošyte, I. W. C. E. Arends, S. de Vries, and R. A. Sheldon, “Preparation and use of cross-linked enzyme aggregates (CLEAs) of laccases,” Journal of Molecular Catalysis B: Enzymatic, vol. 62, no. 2, pp. 142–148, 2010. View at Publisher · View at Google Scholar · View at Scopus
  13. T. Takigawa and Y. Endo, “Effects of glutaraldehyde exposure on human health,” Journal of Occupational Health, vol. 48, no. 2, pp. 75–87, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. D. F. Raikow, P. F. Landrum, and D. F. Reid, “Aquatic invertebrate resting egg sensitivity to glutaraldehyde and sodium hypochlorite,” Environmental Toxicology and Chemistry, vol. 26, no. 8, pp. 1770–1773, 2007. View at Publisher · View at Google Scholar
  15. E. Emmanuel, K. Hanna, C. Bazin, G. Keck, B. Clément, and Y. Perrodin, “Fate of glutaraldehyde in hospital wastewater and combined effects of glutaraldehyde and surfactants on aquatic organisms,” Environment International, vol. 31, no. 3, pp. 399–406, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. B. Krajewska, “Application of chitin- and chitosan-based materials for enzyme immobilizations: a review,” Enzyme and Microbial Technology, vol. 35, no. 2-3, pp. 126–139, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. A. Ghanem and A. Ghaly, “Immobilization of Glucose Oxidase in Chitosan Gel Beads,” Journal of Applied Polymer Science, vol. 91, no. 2, pp. 861–866, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. G. Delanoy, Q. Li, and J. Yu, “Activity and stability of laccase in conjugation with chitosan,” International Journal of Biological Macromolecules, vol. 35, no. 1-2, pp. 89–95, 2005. View at Publisher · View at Google Scholar · View at Scopus
  19. R. Vazquez-Duhalt, R. Tinoco, P. D'Antonio, L. D. Timmie Topoleski, and G. F. Payne, “Enzyme conjugation to the polysaccharide chitosan: smart biocatalysts and biocatalytic hydrogels,” Bioconjugate Chemistry, vol. 12, no. 2, pp. 301–306, 2001. View at Publisher · View at Google Scholar · View at Scopus
  20. R. Bourbonnais and M. G. Paice, “Oxidation of non-phenolic substrates. An expended role for laccase in lignin biodegradation,” FEBS Letters, vol. 267, no. 1, pp. 99–102, 1990. View at Publisher · View at Google Scholar · View at Scopus
  21. C. Aymard and A. Belarbi, “Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism,” Enzyme and Microbial Technology, vol. 27, no. 8, pp. 612–618, 2000. View at Publisher · View at Google Scholar · View at Scopus
  22. American Public Health Association (APHA), American Water Works Association (AWWA), and Water Environment Federation (WEF), Edited by A. E. Greenberg, L.S. Clesceri, A.D. Eaton, American Public Health Association (APHA), American Water Works Association (AWWA), Water Environment Federation (WEF), Baltimore, Md, USA.
  23. J. Zhang, Z. Xu, H. Chen, and Y. Zong, “Removal of 2,4-dichlorophenol by chitosan-immobilized laccase from Coriolus versicolor,” Biochemical Engineering Journal, vol. 45, no. 1, pp. 54–59, 2009. View at Publisher · View at Google Scholar · View at Scopus
  24. Hermanson G. T, Ed., Bioconjugate Techniques, Academic Press, San Diego, Calif, USA, 1996.
  25. L. V. Bindhu and E. T. Abraham, “Immobilization of horseradish peroxidase on chitosan for use in nonaqueous media,” Journal of Applied Polymer Science, vol. 88, no. 6, pp. 1456–1464, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. A. D'Annibale, S. Rita Stazi, V. Vinciguerra, E. Di Mattia, and G. Giovannozzi Sermanni, “Characterization of immobilized laccase from Lentinula edodes and its use in olive-mill wastewater treatment,” Process Biochemistry, vol. 34, no. 6-7, pp. 697–706, 1999. View at Publisher · View at Google Scholar · View at Scopus
  27. H. Cabana, A. Ahamed, and R. Leduc, “Conjugation of laccase from the white rot fungus Trametes versicolor to chitosan and its utilization for the elimination of triclosan,” Bioresource Technology, vol. 102, no. 2, pp. 1656–1662, 2011. View at Publisher · View at Google Scholar
  28. S. R. Couto and J. L. Toca, “Inhibitors of laccases: a review,” Current Enzyme Inhibition, vol. 2, no. 4, pp. 343–352, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. G. Battistuzzi, G. Di Rocco, A. Leonardi, and M. Sola, “1H NMR of native and azide-inhibited laccase from Rhus vernicifera,” Journal of Inorganic Biochemistry, vol. 96, no. 4, pp. 503–506, 2003. View at Publisher · View at Google Scholar · View at Scopus
  30. B. Ghorbel, A. Sellami-Kamoun, and M. Nasri, “Stability studies of protease from Bacillus cereus BG1,” Enzyme and Microbial Technology, vol. 32, no. 5, pp. 513–518, 2003. View at Publisher · View at Google Scholar · View at Scopus
  31. M. Auriol, Y. Filali-Meknassi, R. D. Tyagi, and C. D. Adams, “Laccase-catalyzed conversion of natural and synthetic hormones from a municipal wastewater,” Water Research, vol. 41, no. 15, pp. 3281–3288, 2007. View at Publisher · View at Google Scholar · View at Scopus
  32. M. Auriol, Y. Filali-Meknassi, C. D. Adams, R. D. Tyagi, T. N. Noguerol, and B. Piña, “Removal of estrogenic activity of natural and synthetic hormones from a municipal wastewater: efficiency of horseradish peroxidase and laccase from Trametes versicolor,” Chemosphere, vol. 70, no. 3, pp. 445–452, 2008. View at Publisher · View at Google Scholar · View at Scopus
  33. R. Schoevaart, M. W. Wolbers, M. Golubovic et al., “Preparation, optimization, and structures, of cross-linked enzyme aggregates (CLEAs),” Biotechnology and Bioengineering, vol. 87, no. 6, pp. 754–762, 2004. View at Publisher · View at Google Scholar · View at Scopus