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Degradation of sulfonated azo dyes by the purified lignin peroxidase from Brevibacillus laterosporus MTCC 2298

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Abstract

Lignin peroxidase (EC 1.11.1.14) was purified from the Brevibacillus laterosporus MTCC 2298 by ion exchange chromatography. The Km value of the purified lignin peroxidase (using n-propanol as substrate) was 1.6 mM. The MW of purified enzyme determined with the help of MW-standard markers was approximately 205 kDa. Purity of the enzyme was confirmed by native polyacrylamide gel electrophoresis (PAGE) and the activity staining using a substrate L-DOPA. Sulfonated azo dyes such as Methyl orange and Blue-2B were degraded by the purified lignin peroxidase. Degradation of the dyes was confirmed by HPLC, GC-MS, and FTIR spectroscopy. The mainly elected products of Methyl orange were 4-substituted hexanoic acid (m/z = 207), 4-cyclohexenone lactone cation (m/z = 191), and 4-isopropanal-2, 5-cyclohexa-dienone (m/z = 149) and for Blue-2B were 4-(2-hexenoic acid)-2, 5-cyclohexa-diene-one (m/z = 207; M − 1 = 206) and dehydro-acetic acid derivative (m/z = 223).

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References

  1. Banat, I. M., P. Nigam, D. Singh, and R. Marchant (1996) Microbial decolorization of textile-dye-containing effluents: a review. Bioresour. Technol. 58: 217–227.

    Article  CAS  Google Scholar 

  2. Coughlin, M. F., B. K. Kinkle, and P. L. Bishop (1999) Degradation of azo dyes containing aminonaphthol by Sphingomonas sp. strain 1CX. J. Ind. Microbiol. Biotechnol. 23: 341–346.

    Article  CAS  Google Scholar 

  3. Nachiyar, C. V. and G. S. Rajkumar (2003) Degradation of a tannery and textile dye, Navitan Fast Blue S5R by Pseudomonas aeruginosa. World J. Microbiol. Biotechnol. 19: 609–614.

    Article  CAS  Google Scholar 

  4. Dua, M., A. Singh, N. Sethunathan, and A. K. Johri (2002) Biotechnology and bioremediation: successes and limitations. Appl. Microbiol. Biotechnol. 59: 143–152.

    Article  CAS  Google Scholar 

  5. Huang, Q., J. Walter, and J. R. Weber (2002) Peroxidase-catalyzed oxidative coupling of phenols in the presence of geosorbents: Effects of sorbent chemical characteristics, American Chemical Society, Environmental Chemistry Awards Symposia, 224th ACS National Meeting, Boston, MA, USA.

  6. Pasti-Grigsby, M. B., A. Paszczynski, S. Goszczynski, D. L. Crawford, and R. L. Crawford (1992) Influence of aromatic substitution patterns on azo dye degradability by Streptomyces spp. and Phanerochaete chrysosporium. Appl. Environ. Microbiol. 58: 3605–3613.

    CAS  Google Scholar 

  7. Martinez, A. T., M. Speranza, F. J. Ruiz-Duenas, P. Ferreira, S. Camarero, F. Guillen, M. J. Martinez, A. Gutierrez, and J. C. del Rio (2005) Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin. Int. Microbiol. 8: 195–204.

    CAS  Google Scholar 

  8. Linke, D., H. Zorn, B. Gerken, H. Parlar, and R. G. Berger (2007) Laccase isolation by foam fractionation: New prospects of an old process. Enzyme Microb. Technol. 40: 273–277.

    Article  CAS  Google Scholar 

  9. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193: 265–275.

    CAS  Google Scholar 

  10. Shanmugam, V., M. Kumari, and K. D. Yadav (1999) n-Propanol as a substrate for assaying the ligninperoxidase activity of Phanerochaete chrysosporium. Indian J. Biochem. Biophys. 36: 39–43.

    CAS  Google Scholar 

  11. Ramachandra, M., D. L. Crawford, and G. Hertel (1988) Characterization of an extracellular lignin peroxidase of the lignocellulolytic actinomycete Streptomyces viridosporus. Appl. Environ. Microbiol. 54: 3057–3063.

    CAS  Google Scholar 

  12. Hossain, S. M. and N. Anantharaman (2006) Activity enhancement of ligninolytic enzymes of Trametes versi-color with bagasse powder. Afr. J. Biotechnol. 5: 189–194.

    CAS  Google Scholar 

  13. Tuisel, H., R. Sinclair, J. A. Bumpus, W. Ashbaugh, B. J. Brock, and S. D. Aust (1990) Lignin peroxidase H2 from Phanerochaete chrysosporium: purification, characterization and stability to temperature and pH. Arch. Biochem. Biophys. 279: 158–166.

    Article  CAS  Google Scholar 

  14. Fakoussa, R. M. and M. Hofrichter (1999) Biotechnology and microbiology of coal degradation. Appl. Microbiol. Biotechnol. 52: 25–40.

    Article  CAS  Google Scholar 

  15. Kumari, M., R. S. Yadav, and K. D. Yadav (2002) Secretion of ligninperoxidase by Penicillium citrinum, Fusarium oxysporum and Aspergillus terreus. Indian J. Exp. Biol. 40: 802–806.

    CAS  Google Scholar 

  16. Tien, M., T. K. Kirk, C. Bull, and J. A. Fee (1986) Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by ligninase of Phanerochaete chrysosporium burds. J. Biol. Chem. 261: 1687–1693.

    CAS  Google Scholar 

  17. Pclczar, M. J., E. C. S. Chen, and N. R. Kring (2004) Microbiology. 5th ed., Tata McGraw-Hill Publishing Co. Ltd., New Delhi, India.

    Google Scholar 

  18. Tien, M. and T. K. Kirk (1984) Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase. Proc. Natl. Acad. Sci. USA 81: 2280–2284.

    Article  CAS  Google Scholar 

  19. Andrawis, A., K. A. Johnson, and M. Tien (1988) Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium. J. Biol. Chem. 263: 1195–1198.

    CAS  Google Scholar 

  20. Hu, Z. C., R. A. Korus, C. R. Venkataramu, and R. L. Crawford (1993) Deactivation kinetics of lignin peroxidase from Phanerochaete chrysosporium. Enzyme Microb. Technol. 15: 567–574.

    Article  CAS  Google Scholar 

  21. Yang, J. S., H. L. Yuan, H. X. Wang, and W. X. Chen (2005) Purification and characterization of lignin peroxidases from Penicillium decumbens P6. World J. Microbiol. Biotechnol. 21: 435–440.

    Article  CAS  Google Scholar 

  22. Ward, G., Y. Hadar, I. Bilkis, and C. G. Dosoretz (2003) Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes. J. Biol. Chem. 278: 39726–39734.

    Article  CAS  Google Scholar 

  23. Ruiz-Duenas, F. J., S. Camarero, M. Perez-Boada, M. J. Martinez, and A. T. Martinez (2001) A new versatile peroxidase from Pleurotus. Biochem. Soc. Trans. 29: 116–122.

    Article  CAS  Google Scholar 

  24. Goodwin, D. C., S. D. Aust, and T. A. Grover (1995) Evidence for veratryl alcohol as a redox mediator in lignin peroxidase-catalyzed oxidation. Biochemistry 34: 5060–5065.

    Article  CAS  Google Scholar 

  25. Collins, P. J., J. A. Field, P. Teunissen, and A. D. W. Dobson (1997) Stabilization of lignin peroxidases in white rot fungi by tryptophan. Appl. Environ. Microbiol. 63: 2543–2548.

    CAS  Google Scholar 

  26. Goszczynski, S., A. Paszczynski, M. B. Pasti-Grigsby, R. L. Crawford, and D. L. Crawford (1994) New pathway for degradation of sulfonated azo dyes by microbial peroxidases of Phanerochaete chrysosporium and Streptomyces chromofuscus. J. Bacteriol. 176: 1339–1347.

    CAS  Google Scholar 

  27. Bumpus, J. A. and B. J. Brock (1988) Biodegradation of crystal violet by the white rot fungus Phanerochaete chrysosporium. Appl. Environ. Microbiol. 54: 1143–1150.

    CAS  Google Scholar 

  28. Vazquez-Duhalt, R., D. W. S. Westlake, and P. M. Fedorak (1994) Lignin peroxidase oxidation of aromatic compounds in systems containing organic solvents. Appl. Environ. Microbiol. 60: 459–466.

    CAS  Google Scholar 

  29. Baciocchi, E., M. F. Gerini, P. J. Harvey, O. Lanzalunga, and S. Mancinelli (2000) Oxidation of aromatic sulfides by lignin peroxidase from Phanerochaete chrysosporium. Eur. J. Biochem. 267: 2705–2710.

    Article  CAS  Google Scholar 

  30. Chivukula, M. and V. Renganathan (1995) Phenolic azo dye oxidation by laccase from Pyricularia oryzae. Appl. Environ. Microbiol. 61: 4374–4377.

    CAS  Google Scholar 

  31. Reddy, G. V. B., M. D. S. Gelpke, and M. H. Gold (1998) Degradation of 2,4,6-trichlorophenol by Phanerochaete chrysosporium: Involvement of reductive dechlorination. J. Bacteriol. 180: 5159–5164.

    CAS  Google Scholar 

  32. Spain, J. C. and D. T. Gibson (1991) Pathway for biodegradation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 57: 812–819.

    CAS  Google Scholar 

  33. Martins, M. A. M., I. C. Ferreira, I. M. Santos, M. J. Queiroz, and N. Lima (2001) Biodegradation of bioaccessible textile azo dyes by Phanerochaete chrysosporium. J. Biotechnol. 89: 91–98.

    Article  CAS  Google Scholar 

  34. Soares, G. M. B., M. T. P. Amorim, R. Hrdina, and M. Costa-Ferreira (2002) Studies on the biotransformation of novel disazo dyes by laccase. Process Biochem. 37: 581–587.

    Article  CAS  Google Scholar 

  35. Baciocchi, E., M. F. Gerini, O. Lanzalunga, A. Lapi, S. Mancinelli, and P. Mencarelli (2000) Oxidative N-demethylation of N,N-dimethylanilines catalyzed by lignin peroxidase: a mechanistic insight by a kinetic deuterium isotope effect study. Chem. Commun. 5: 393–394.

    Article  Google Scholar 

  36. Baciocchi, E., M. F. Gerini, O. Lanzalunga, A. Lapi, M. G. Lo Piparo, and S. Mancinelli (2001) Isotope-effect profiles in the oxidative N-demethylation of N,N-dimethylanilines catalyzed by lignin peroxidase and a chemical model. Eur. J. Org. Chem. 12: 2305–2310.

    Article  Google Scholar 

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Correspondence to Sushama S. Gomare.

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Gomare, S.S., Jadhav, J.P. & Govindwar, S.P. Degradation of sulfonated azo dyes by the purified lignin peroxidase from Brevibacillus laterosporus MTCC 2298. Biotechnol Bioproc E 13, 136–143 (2008). https://doi.org/10.1007/s12257-008-0008-5

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