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Oxidation of crocein orange G by lignin peroxidase isoenzymes

Kinetics and Effect of H2O2

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Abstract

The ligninolytic enzyme system ofPhanerochaete chrysosporiun is able to decolorize several recalcitrant dyes. Three lignin peroxidase isoenzymes, LiP 3.85, LiP 4.15, and LiP 4.65, were purified by preparative isoelectric focusing from the carbon-limited culture medium ofP. chrysosporium. Based on amino terminal sequences, the purified isoenzymes correspond to the isoenzymes H8, H6, and H2, respectively, from theN-limited culture. The purified isoenzymes were used for decolorization of an azo dye, Crocein Orange G (COG). According to the kinetic data obtained, the oxidation of COG by lignin peroxidase appeared to follow Michaelis-Menten kinetics. Kinetic parameters for each isoenzyme were determined. The inactivating effect of ascending H2O2 concentrations on COG oxidation is shown to be exponential within the used concentration range. The best degree of decolorization of 100 μM COG was obtained when the H2O2 concentration was 150 μM. This was also the lowest H2O2 concentration for maximal decolorization of 100 μM COG, regardless of the amount of lignin peroxidase used in the reaction.

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References

  1. Zollinger, H. (1987),Color Chemistry: Syntheses, Properties, and Applications of Organic Dyes and Pigments, VCH, New York.

    Google Scholar 

  2. Pagga, U. and Brown, D. (1986),Chemosphere 15, 479–491.

    Article  CAS  Google Scholar 

  3. Shaul, G. M., Holdsworth, T. J., Dempsey, C. R., and Dostal, K. A. (1991),Chemosphere 22, 107–119.

    Article  CAS  Google Scholar 

  4. Haug, W., Schmidt, A., Nörtemann, B., Hempel, D. C., Stolz, A., and Knackmuss, H.-J. (1991),Appl. Environ. Microbiol. 57, 3144–3149.

    CAS  Google Scholar 

  5. McCann, J. and Ames, B. N. (1975),Proc. Natl. Acad. Sci. USA 73, 950–954.

    Article  Google Scholar 

  6. Zimmermann, T., Kulla, H. G., and Leisinger, T. (1982),Eur. J. Biochem. 129, 197–203.

    Article  CAS  Google Scholar 

  7. Rafii, F., Franklin, W., and Cerniglia, C. E. (1990),Appl. Environ. Microbiol. 56, 2146–2151.

    CAS  Google Scholar 

  8. Fujita, S. and Peisach, J. (1977),Biochem. Biophys. Res. Commun. 78, 328–335.

    Article  CAS  Google Scholar 

  9. Huang, M.-T., Miwa, G. T., and Lu, A. Y. H. (1979),J. Biol. Chem. 254, 3930–3935.

    CAS  Google Scholar 

  10. Hammel, K. E. and Tardone, P. J. (1988),Biochemistry 27, 6563–6568.

    Article  CAS  Google Scholar 

  11. Mileski, G. J., Bumpus, J. A., Jurek, M. A., and Aust, S. D. (1988),Appl. Environ. Microbiol. 54, 2885–2889.

    CAS  Google Scholar 

  12. Valli, K., Wariishi, H., and Gold, M. H. (1992),J. Bacteriol. 174, 2131–2137.

    CAS  Google Scholar 

  13. Valli, K., Brock, B. J., Joshi, D. K., and Gold, M. H. (1992),Appl. Environ. Microbiol. 58, 221–228.

    CAS  Google Scholar 

  14. Hammel, K. E., Gai, W. Z., Green, B., and Moen, M. A. (1992),Appl. Environ. Microbiol. 58, 1832–1838.

    CAS  Google Scholar 

  15. Cripps, C., Bumpus, J. A., and Aust, S. D. (1990),Appl. Environ. Microbiol. 56, 1114–1118.

    CAS  Google Scholar 

  16. Spadaro, J. T., Gold, M. H., and Renganathan, V. (1992),Appl. Environ. Microbiol. 58, 2397–2401.

    CAS  Google Scholar 

  17. Ollikka, P., Alhonmäki, K., Leppänen, V. M., Glumoff, T., Raijola, T., and Suominen, I. (1993),Appl. Environ. Microbiol. 59, 4010–4016.

    CAS  Google Scholar 

  18. Paszczynski, A., Pasti, M. B., Goszczynski, S., Crawford, D. L., and Crawford, R. L. (1991),Enzyme Microb. Technol. 13, 378–384.

    Article  CAS  Google Scholar 

  19. Paszczynski, A. and Crawford, R. L. (1991),Biochem. Biophys. Res. Commun. 178, 1056–1063.

    Article  CAS  Google Scholar 

  20. Goszczynski, S., Paszczynski, A., Pasti-Grigsby, M. B., Crawford, R. L., and Crawford, D. L. (1994),J. Bacteriol. 176, 1339–1347.

    CAS  Google Scholar 

  21. Chivukula, M., Spadaro, J. T., and Renganathan, V. (1995),Biochemistry 34, 7765–7772.

    Article  CAS  Google Scholar 

  22. Nelson, D. P. and Kiesow, L. A. (1972),Anal. Biochem. 49, 474–478.

    Article  CAS  Google Scholar 

  23. Kirk, T. K., Schultz, E., Connors, W. T., Lorenz, L. F., and Zeikus, J. G. (1978),Arch. Microbiol. 117, 277–285.

    Article  CAS  Google Scholar 

  24. Glumoff, T. (1991), PhD Thesis, Swiss Federal Institute of Technology, Zurich, Switzerland.

    Google Scholar 

  25. Linko, S. (1988),Enzyme Microb. Technol. 10, 410–417.

    Article  CAS  Google Scholar 

  26. Tien, M. and Kirk, T. K. (1988),Methods Enzymol. 161, 238–249.

    Article  CAS  Google Scholar 

  27. Glumoff, T., Harvey, P. J., Molinari, S., Goble, M., Frank, G., Palmer, J. M., Smit, J. D. G., and Leisola, M. S. A. (1990),Eur. J. Biochem. 187, 515–520.

    Article  CAS  Google Scholar 

  28. Laemmli, U. K. (1970),Nature 227, 680–685.

    Article  CAS  Google Scholar 

  29. Bradford, M. M. (1976),Anal. Biochem. 72, 248–254.

    Article  CAS  Google Scholar 

  30. Tien, M., Kirk, T. K., Bull, C., and Fee, J. A. (1986),J. Biol. Chem. 261, 1687–1693.

    CAS  Google Scholar 

  31. Dass, S. B. and Reddy, C. A. (1990),FEMS Microbiol. Lett. 69, 221–224.

    Article  CAS  Google Scholar 

  32. Johnson, T. M., Pease, E. A., Li, J. K., and Tien, M. (1992),Arch. Biochem. Biophys. 296, 660–666.

    Article  CAS  Google Scholar 

  33. Chung, N. and Aust, S. D. (1995),Arch. Biochem. Biophys. 316, 851–855.

    Article  CAS  Google Scholar 

  34. Tuisel, H., Sinclair, R., Bumpus, J. A., Ashbaugh, W., Brock, B. J., and Aust, S. D. (1990),Arch. Biochem. Biophys. 279, 158–166.

    Article  CAS  Google Scholar 

  35. Ollikka, P., Leppänen, V.-M., Anttila, T., and Suominen, I. (1995),Prot. Express. Purif. 6, 337–342.

    Article  CAS  Google Scholar 

  36. Cai, D. Y. and Tien, M. (1989),Biochem. Biophys. Res. Commun. 162, 464–469.

    Article  CAS  Google Scholar 

  37. Wariishi, H. and Gold, M. H. (1990),J. Biol. Chem. 265, 2070–2077.

    CAS  Google Scholar 

  38. Koduri, R. S. and Tien, M. (1995),J. Biol. Chem. 270, 22,254-22,258.

    Google Scholar 

  39. Barr, D. P. and Aust, S. D. (1994),Arch. Biochem. Biophys. 312, 511–515.

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Biochemistry, University of Turku, Vatselankatu 2, FIN-20014, Turku, Finland

    Pauli Ollikka

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  1. Pauli Ollikka
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  2. Tiina Harjunpää
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  3. Kaisa Palmu
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  4. Pekka Mäntsälä
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  5. Ilari Suominen
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Correspondence to Pauli Ollikka.

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Ollikka, P., Harjunpää, T., Palmu, K. et al. Oxidation of crocein orange G by lignin peroxidase isoenzymes. Appl Biochem Biotechnol 75, 307–321 (1998). https://doi.org/10.1007/BF02787783

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  • DOI: https://doi.org/10.1007/BF02787783

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