Analytical and Bioanalytical Chemistry

, Volume 402, Issue 1, pp 405–412

The aromatic peroxygenase from Marasmius rutola—a new enzyme for biosensor applications

Authors

  • Aysu Yarman
    • Fraunhofer Institute for Biomedical Engineering IBMT
  • Glenn Gröbe
    • Department of BiotechnologyLausitz University of Applied Sciences
  • Bettina Neumann
    • Fraunhofer Institute for Biomedical Engineering IBMT
  • Mathias Kinne
    • Unit of Environmental BiotechnologyInternational Graduate School of Zittau
  • Nenad Gajovic-Eichelmann
    • Fraunhofer Institute for Biomedical Engineering IBMT
  • Ulla Wollenberger
    • Institute of Biochemistry and BiologyUniversity of Potsdam Karl-Liebknecht-Str. 24–25
  • Martin Hofrichter
    • Unit of Environmental BiotechnologyInternational Graduate School of Zittau
  • René Ullrich
    • Unit of Environmental BiotechnologyInternational Graduate School of Zittau
  • Katrin Scheibner
    • Department of BiotechnologyLausitz University of Applied Sciences
    • Fraunhofer Institute for Biomedical Engineering IBMT
    • Institute of Biochemistry and BiologyUniversity of Potsdam Karl-Liebknecht-Str. 24–25
Original Paper

DOI: 10.1007/s00216-011-5497-y

Cite this article as:
Yarman, A., Gröbe, G., Neumann, B. et al. Anal Bioanal Chem (2012) 402: 405. doi:10.1007/s00216-011-5497-y

Abstract

The aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of −278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe2+/Fe3+ redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensors and their further development are discussed.

Keywords

Unspecific peroxygenaseCytochrome P450BiosensorsPhenolic substances

Copyright information

© Springer-Verlag 2011