Applied Microbiology and Biotechnology

, Volume 42, Issue 5, pp 675–681 | Cite as

Kinetics of chemically modified lignin peroxidase and enzymatic oxidation of aromatic nitrogen-containing compounds

  • R. Vazquez-Duhalt
  • D. W. S. Westlake
  • P. M. Fedorak
Biotechnology Original Paper

Abstract

Lignin peroxidase from the white-rot fungus Phanerochaete chrysosporium was chemically modified by reductive alkylation with benzyl, naphthyl and anthracyl moieties, thereby increasing its superficial hydrophobicity. The three chemical modifications altered the kinetic behaviour of the enzyme in 10% acetonitrile with four different substrates: carbazole, pinacyanol, pyrene and veratryl alcohol. Benzyl modification of lignin peroxidase increased the catalytic efficiency (kcat/Km,app) 2.7 times for carbazole oxidation. Thirteen N-containing compounds, including pyrroles, pyridines, and aromatic amines, were tested to determine whether they could be oxidized by lignin peroxidase in 10% acetonitrile. All the pyrrole analogues and all the amines tested were oxidized, but none of the pyridine analogous reacted. Some products were isolated and analyzed by high-resolution mass spectrometry. Most were dimers or polymers and, in some cases, these contained oxygen atoms. The possibility of bitumen and petroleum modifications using this enzyme is discussed.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Barr DP, Shah MM, Grover TA, Aust SD (1992) Production of hydroxyl radical by lignin peroxidase from Phanerochaete chrysosporium. Arch Biochem Biophys 298:480–485Google Scholar
  2. Dordick JS (1989) Enzymatic catalysis in monophasic organic solvents. Enzyme Microb Technol 11:194–211Google Scholar
  3. Farrel RL, Murtagh KE, Tien M, Mozuch MD, Kirk TK (1989) Physical and enzymatic properties of lignin peroxidase isoenzymes from Phanerochaete chrysosporium. Enzyme Microb Technol 11:322–328Google Scholar
  4. Fedorak PM, Semple KM, Vazquez-Duhalt R, Westlake DWS (1993) Chloroperoxidase-mediated modifications of petroporphyrins and asphaltenes. Enzyme Microb Technol 15: 429–437Google Scholar
  5. Fields R (1972) The rapid determination of amino groups. Methods Enzymol 25:464–468Google Scholar
  6. Fu CM, Schaffer AM (1985) Effect of nitrogen compounds on cracking catalysis. Ind Eng Chem Prod Res Dev 24:68–75Google Scholar
  7. Girgis MJ, Gates BC (1991) Reactivities, reaction networks, and kinetics in high pressure catalytic hydro-processing. Ind Eng Chem Res 30:2021–2058Google Scholar
  8. Hammel KE, Kalyanaraman B, Kirk TK (1986) Oxidation of polycyclic aromatic hydrocarbons and dibenzo[p]dioxins by Phanerochaete chrysosporium ligninase. J Biol Chem 261:16948–16952Google Scholar
  9. Hammel KE, Jensen KA, Mozuch MD, Landucci LL, Tien M, Pease EA (1993) Ligninolysis by purified lignin peroxidase J Biol Chem 268:12274–12281Google Scholar
  10. Ho TC (1988) Hydrodenitrogenation catalysis. Catal Rev Sci Eng 30:117–160Google Scholar
  11. Ho TC, Katritzky AR, Cato SJ (1992) Effect of nitrogen compounds on cracking catalysis. Ind Eng Chem Res 31:1587–1597Google Scholar
  12. Ito Y, Fujii H, Imanishi Y (1992) Lipase modification by various synthetic polymers for use in chloroform. Biotechnol Lett 14:1149–1152Google Scholar
  13. Jokuty PL, Gray MR (1991) Resistant nitrogen compounds in hydrogenated gas oil from Athabasca bitumen. Energy Fuels 5:791–795Google Scholar
  14. Jokuty PL, Gray MR (1992) Nitrogen bases resistant to hydrodenitrogenation: evidence against using quinoline as a model compound. Ind Eng Chem Res 31:1445–1449Google Scholar
  15. Kedderis GL, Rickert DE, Pandey RN, Hollenberg PF (1986) 18O studies of the peroxidase-catalyzed oxidation of N-methylcarbazole. J Biol Chem 261:15910–15914Google Scholar
  16. Levin RD, Lias SG (1982) Ionization potentials and appearance measurements 1971–1981. US National Standards Reference Data Series no. 71. U.S. National Bureau of Standards, Washington, DCGoogle Scholar
  17. Lin S, Carison RM (1984) Susceptibility of environmentally important heterocycles to chemical disinfection: reactions with aqueous chlorine, chlorine dioxide, and chloramine. Environ Sci Technol 18:743–748PubMedGoogle Scholar
  18. McKay JF, Weber JM, Latham DR (1976) Characterization of nitrogen bases in high-boiling petroleum distillates. Anal Chem 48:891–898Google Scholar
  19. Mitra-Kirtley S, Mullins OC, Elp J van, George SJ, Chen J, Cramer SP (1993) Determination of the chemical structures in petroleum asphaltenes using XANES spectroscopy. J Am Chem Soc 115:252–258Google Scholar
  20. Payzant JD, Hogg AM, Montgomery DS, Strausz OP (1985) A field ionization mass spectrometry study of the maltene fraction of Athabasca bitumen. Part III. The polars. AOSTRA J Res 1:203–210Google Scholar
  21. Rosenstock HM, Draxl K, Steiner BW, Herron JT (1977) Energetics of gaseous ions. J Phys Chem Ref Data 6 [Suppl 1]:I34-I690Google Scholar
  22. Sanglard D, Leisola MSA, Fiechter A (1986) Role of extracellular ligninases in biodegradation of benzo(a)pyrene by Phanerochaete chrysosporium. Enzyme Microb Technol 8:209–211Google Scholar
  23. Strausz OP, Mojelsky TW, Lown EM (1992) The molecular structure of asphaltene: an unfolding story. Fuel 71:1355–1363Google Scholar
  24. Takahashi K, Ajima A, Yoshimoto T, Inada Y (1984) Polyethylene glycol-modified catalase exhibits unexpectedly high activity in benzene. Biochem Biophys Res Commun 125:761–766Google Scholar
  25. Terabe S, Konaka R (1969) Electron spin resonance studies on oxidation with nickel peroxide. Spin trapping of free-radical intermediates. J Am Chem Soc 91:5655–5657Google Scholar
  26. Tien M, Kirk TK (1984) Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase. Proc Natl Acad Sci USA 81:2280–2284Google Scholar
  27. Tien M, Kirk TK, Bull C, Fee JA (1966) Steady-state and transient-state kinetics studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligininase of Phanerochaete chrysosporium Burds. J Biol Chem 261:1687–1693Google Scholar
  28. Vazquez-Duhalt R, Fedorak PM, Westlake DWS (1992) Role of enzyme hydrophobicity in biocatalysis in organic solvents. Enzyme Microb Technol 14:837–841Google Scholar
  29. Vazquez-Duhalt R, Westlake DWS, Fedorak PM (1993a) Cytochrome c as a biocatalyst for the oxidation of thiophenes and organosulfides. Enzyme Microb Technol 15:494–499Google Scholar
  30. Vazquez-Duhalt R, Semple KM, Westlake DWS, Fedorak PM (1993b) Effect of water-miscible organic solvents on the catalytic activity of cytochrome c. Enzyme Microb Technol 15: 936–943Google Scholar
  31. Vazquez-Duhalt R, Westlake DWS, Fedorak PM (1994) Lignin peroxidase oxidation of aromatic compounds in systems containing organic solvent. Appl Environ Microbiol 60:459–466Google Scholar

Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • R. Vazquez-Duhalt
    • 1
  • D. W. S. Westlake
    • 1
  • P. M. Fedorak
    • 1
  1. 1.Department of MicrobiologyUniversity of AlbertaEdmontonCanada

Personalised recommendations