Advertisement

Applied Biochemistry and Biotechnology

, Volume 55, Issue 3, pp 207–218 | Cite as

Superactivity of peroxidase solubilized in reversed micellar systems

  • L. Setti
  • P. Fevereiro
  • E. P. Melo
  • P. G. Pifferi
  • J. M. S. Cabral
  • M. R. Aires-Barros
Original Articles

Abstract

Vaccinium mirtyllus peroxidase solubilized in reversed micelles was used for the oxidation of guaiacol. Some relevant parameters for the enzymatic activity, such as pH,w o (molar ratio water/surfactant), surfactant type and concentration, and cosurfactant concentration, were investigated. The peroxidase showed higher activities in reversed micelles than in aqueous solution. The stability of the peroxidase in reversed micelles was also studied, namely, the effect ofw o and temperature on enzyme deactivation. The peroxidase displayed higher stabilities in CTAB/hexanol in isooctane reversed micelles, with halflife times higher than 500 h.

Index Entries

Vaccinium mirtyllus peroxidase reversed micelles superactivity stability 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Ryu, K. and Dordick, J. S. (1992),Biochemistry 31, 2588–2598.CrossRefGoogle Scholar
  2. 2.
    Tanrog, A., Dorris, M. L., and Guziec, F. S. (1992),Anal. Biochem. 205, 271–277.CrossRefGoogle Scholar
  3. 3.
    Halliwell, B. and de Rycker, J. (1988),Photochem. Photobiol. 28, 757–763.CrossRefGoogle Scholar
  4. 4.
    Ryu, K. and Dordick, J. S. (1992),Biochemistry 31(9), 2588–2598.CrossRefGoogle Scholar
  5. 5.
    Singer, S. J. (1962),Adv. Protein. Chem. 17, 1–68.CrossRefGoogle Scholar
  6. 6.
    Martinek, K., Levashov, A. V., Khmelnitski, Yu. L., Klyachko, N. L., and Berezin, I. V. (1982),Science (Washington, DC)218, 889–891.CrossRefGoogle Scholar
  7. 7.
    Klyachko, N. L., Levashov, A. V., and Martinek, K. (1984),Mol. Biol. 18, 1019–1032.Google Scholar
  8. 8.
    Martinek, K., Khmelnitski, Yu. L., Levashov, A. V., and Berezin, I. V. (1982),Dokl. Akad. NanK. SSSR 263, 737–741.Google Scholar
  9. 9.
    Barbaric, S. and Luisi, P. L. (1981),J. Am. Chem. Soc. 103, 4239–4244.CrossRefGoogle Scholar
  10. 10.
    Martinek, K., Levashov, A. V., Klyachko, N. L., Pautin, V. I., and Berezin, I. V. (1981),Biochem. Biophys. Acta 657, 277–294.Google Scholar
  11. 11.
    Belonogova, O. V., Likhtenshtein, G. I., Levashov, A. V., Khmelnitski, Y. L., Klyachko, N. L., and Martinek, K. (1983),Biokhimiya (Moskow)48, 379–386.Google Scholar
  12. 12.
    Shield, J. W., Ferguson, H. D., Bommarius, A. S., and Hatton, T. A. (1986),Ind. Eng. Chem. Fundam. 25(4), 603–612.CrossRefGoogle Scholar
  13. 13.
    Melo, N., Gomes, A., Cabral, J. M. S., and Fevereiro, P. (1995),Plant Sci. 106, 177–184.CrossRefGoogle Scholar
  14. 14.
    Chance, B. and Machly, A. C. (1964),Methods Enzymol. 2, 764–775.CrossRefGoogle Scholar
  15. 15.
    Martinek, K., Klyachko, N. L., Kabanov, A. V., Khmelnitsky, Yu. L., and Levashov, A. V. (1989),Biochim. Biophys. Acta 981, 161–172.CrossRefGoogle Scholar
  16. 16.
    Martinek, K., Klyachko, N. L., Levashov, A. V., and Berezin, I. V. (1983),Dokl. Akad. Nauk. SSSR 269(2), 491–493.Google Scholar
  17. 17.
    Levashov, A. V., Khmelnitsky, Yu. L., Klyachko, N. L. et al. (1982),J. Colloid. Interface Sci. 88(2), 444–457.CrossRefGoogle Scholar
  18. 18.
    Clementi, F. and Palade, C. E. (1969),J. Cell. Biol 41, 33–58.CrossRefGoogle Scholar
  19. 19.
    Welinder, K. G. (1985),Eur. J. Biochem. 151, 497–550.CrossRefGoogle Scholar
  20. 20.
    Leung, R. and Shah, D. O. (1987),J. Coll. Interf. Sci. 120, 330–344.CrossRefGoogle Scholar
  21. 21.
    Henley, J. P. and Sadana, A. (1985),Enzyme Microb. Technol. 7, 50–60.CrossRefGoogle Scholar

Copyright information

© Humana Press Inc 1995

Authors and Affiliations

  • L. Setti
    • 1
  • P. Fevereiro
    • 2
  • E. P. Melo
    • 3
  • P. G. Pifferi
    • 1
  • J. M. S. Cabral
    • 3
  • M. R. Aires-Barros
    • 3
  1. 1.Dipartimento di Chimica Industriale e dei MaterialiBolognaItaly
  2. 2.Instituto de Tecnologia e Química BiológicaUniversidade Nova LisboaOeirasPortugal
  3. 3.Laboratório de Engenharia BioquímicaInstituto Superior TécnicoLisboaPortugal

Personalised recommendations