Cruz JC, García J, Ayala M

Language: English
References: 25
Page: 5-12
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ABSTRACT

In this work we report the oxidation of volatile organosulfur compounds (VOC) catalyzed by the enzyme chloroperoxidase from Caldariomyces fumago. VOC are regarded as atmospheric pollutants due to their unpleasant odor and low detection threshold. Diethyl sulfide, dimethyl disulfide, propanethiol, butanethiol and hexanethiol were found to be substrates for the enzyme in a liquid medium reaction at pH 6, under peroxidatic conditions. Product analysis showed that sulfides were oxidized to their respective sulfoxides whereas thiols were oxidized to the corresponding disulfides. The identified products showed significantly lower vapor pressure than the parental compounds; thus, the products are not considered atmospheric pollutants. A 70-mL two-phase reactor was assembled in order to determine the efficiency of the enzymatic treatment. The liquid phase, consisting of 15% organic solvent and 85% buffer, was contacted with the gaseous phase, consisting of a substrate-enriched air stream. Using dimethyl disulfide as model substrate, we found that only enzymatic oxidation occurred in this system; by controlling the enzyme and peroxide concentration, we found that the substrate is transferred to the aqueous phase where 1 mol of enzyme converted approximately 12,400 mol of substrate, thus highlighting the potential of enzymatic treatment of malodorous gaseous streams.

REFERENCES

1. Casella, L., Monzani, E. & Nicolis, S. Potential applications of peroxidases in the fine chemical industries, in Biocatalysis based on heme peroxidases (eds. Torres, E. & Ayala, M.) 111-153 (Springer-Verlag; 2010).

2. Márquez-Rocha, F.J., Pica-Granados, Y., Sandoval-Villasana, A.M. & Vázquez-Duhalt, R. Determination of genotoxicity using a chloroperoxidase-mediated model of PAH-DNA adduct formation. Bull. Environ. Contam. Toxicol. 59, 788-795 (1997).

3. Ayala, M. & Vázquez-Duhalt, R. Enzymatic catalysis on petroleum products in Petroleum biotechnology (eds. Vázquez-Duhalt, R. & Quintero-Ramírez, R.) 67-111 (Amsterdam, Elsevier Science, 2004).

4. Torres, R., Bustos-Jaimes, I. & Le Borgne, S. Potential use of oxidative enzymes for the detoxification of organic pollutants. Appl. Catal. Environ. 46, 1-15 (2003).

5. Torres, C. & Vázquez-Duhalt, R. Applications and prospective of peroxidase biocatalysis in the environmental field in Biocatalysis based on heme peroxidases (eds. Torres, E. & Ayala, M.) 179-206 (Springer-Verlag, 2010).

6. Hofrichter, M. & Ullrich, R. Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance. Appl. Microbiol. Biotechnol. 71, 276-288 (2006).

7. Allenmark, G.A. & Andersson, M.A. Chloroperoxidase-induced asymmetric sulfoxidation of some conformationally restricted sulfides. Chirality 10, 246-252 (1998).

8. Colonna, S., Gaggero, N., Carrea, G. & Pasta, P. A new enzymatic enantioselective synthesis of dialkyl sulfoxides catalysed by monooxygenases. Chem. Commun. 439-440 (1997).

9. Vargas, R.R., Bechara, E.J.H., Marzorati, L. & Wladislaw, B. Asymmetric sulfoxidation of a [beta]-carbonyl sulfide series by chloroperoxidase. Tetrahedron: Asymmetry 10, 3219-3227 (1999).

10. Pasta, P., Carrea, G., Colonna, S. & Gaggero, N. Effects of chloride on the kinetics and stereochemistry of chloroperoxidase catalyzed oxidation of sulfides. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1209, 203-208 (1994).

11. Ayala, M., Robledo, N.R., López-Munguía, A. & Vázquez- Duhalt, R. Substrate specificity and ionization potential in chloroperoxidase-catalyzed oxidation of diesel fuel. Environ. Sci. Technol. 34, 2804-2809 (2000).

12. Ayala, M., Tinoco, R., Hernández, V., Bremauntz, P. & Vázquez- Duhalt, R. Biocatalytic oxidation of fuel as an alternative to biodesulfurization. Fuel Process. Technol. 57, 101-111 (1998).

13. Schiffman, S.S. & Williams, C.M. Science of odor as a potential health issue. J. Environ. Qual. 34, 129-138 (2005).

14. Andersson, F., Annika, T.S., Karlsson, A., Svensson, B.H. & Ejlertsson, J.R. Occurrence and abatement of volatile sulfur compounds during biogas production. J. Air Waste Manage. Assoc. 54, 855-861 (2004).

15. Smet, E., Lens, P. & Van Langenhove, H. Treatment of waste gases contaminated with odorous sulfur compounds. Crit. Rev. Environ. Sci. Technol. 28, 89-117 (1998).

16. Pickard, M.A., Kadima, T.A. & Carmichael, R.D. Chloroperoxidase, a peroxidase with potential. J. Ind. Microbiol. Biotechnol. 7, 235-241 (1991).

17. Radzicka, A. & Wolfenden, R. A proficient enzyme. Science 267, 90-93 (1995).

18. Brown, R.L. & Stein, S.E. Boiling point data in NIST Chemistry WebBook, NIST Standard Reference Database Number 69 (eds. Linstrom, P.J. & Mallards, W.G.) National Institute of Standards and Technology http://webbook nist.gov (last seen on 2012).

19. Goto, Y., Matsui, T., Ozaki, S.I., Watanabe, Y. & Fukuzumi, S. Mechanisms of sulfoxidation catalyzed by high-valent intermediates of heme enzymes: electron-transfer vs oxygentransfer mechanism. J. Am. Chem. Soc. 121, 9497-9502 (1999).

20. Kobayashi, S., Nakano, M., Kimura, T. & Schaap, A.P. On the mechanism of the peroxidase-catalyzed oxygen-transfer reaction. Biochemistry 26, 5019-5022 (1987).

21. Silverstein, R.M.& Hager, L.P. Chloroperoxidase-catalyzed oxidation of thiols and disulfides to sulfenyl chlorides. Biochemistry 13, 5069-5073 (1974).

22. Burner, U. & Obinger, C. Transient-state and steady-state kinetics of the oxidation of aliphatic and aromatic thiols by horseradish peroxidase. FEBS Lett. 411, 269-274 (1997).

23. Burner, U., Jantschko, W. & Obinger, C. Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. FEBS Lett. 443, 290-296 (1994).

24. Valderrama, B., Ayala, M. & Vázquez-Duhalt, R. Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes. Chem. Biol. 9, 555-565 (2000).

25. Ayala, M., Batista, C.V. & Vázquez-Duhalt, R. Heme destruction, the main molecular event during the peroxide-mediated inactivation of chloroperoxidase from Caldariomyces fumago. J. Biol. Inorg. Chem. 16, 63-68 (2011).