L-Dopa synthesis catalyzed by tyrosinase immobilized in poly(ethyleneoxide) conducting polymers

Yildiz H. B., Caliskan S., Kamaci M., Caliskan A., Yilmaz H.

International Journal of Biological Macromolecules, vol.56, pp.34-40, 2013 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 56
  • Publication Date: 2013
  • Doi Number: 10.1016/j.ijbiomac.2013.01.031
  • Journal Name: International Journal of Biological Macromolecules
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.34-40
  • Keywords: Biocatalysis, Conducting polymers, Electropolymerization, Enzyme immobilization, L-Dopa synthesis
  • Ankara Haci Bayram Veli University Affiliated: No

Abstract

1-3,4-Dihydroxy phenylalanine called as l-Dopa is a precursor of dopamine and an important neural message transmitter and it has been a preferred drug for the treatment of Parkinson's disease. In this study, with regards to the synthesis of l-Dopa two types of biosensors were designed by immobilizing tyrosinase on conducting polymers: thiophene capped poly(ethyleneoxide)/polypyrrole (PEO-co-PPy) and 3-methylthienyl methacrylate-co-p-vinylbenzyloxy poly(ethyleneoxide)/polypyrrole (CP-co-PPy). PEO-co-PPy and CP-co-PPy were synthesized electrochemically and tyrosinase immobilized by entrapment during electropolymerization. l-Tyrosine was used as the substrate for l-Dopa synthesis. The kinetic parameters of the designed biosensors, maximum reaction rate of the enzyme (Vmax) and Michaelis Menten constant (Km) were determined. Vmax were found as 0.007μmol/(minelectrode) for PEO-co-PPy matrix and 0.012μmol/(minelectrode) for CP-co-PPy matrix. Km values were determined as 3.4 and 9.2mM for PEO-co-PPy and CP-co-PPy matrices, respectively. Optimum temperature and pH, operational and shelf life stabilities of immobilized enzyme were also examined. © 2013 Elsevier B.V.