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Updated: May 14, 2026

Genetic Incorporation of Biosynthesized L-dihydroxyphenylalanine (DOPA) and Its Application to Protein Conjugation
Published on: August 24, 2018
L-Dopa synthesis catalyzed by tyrosinase immobilized in poly(ethyleneoxide) conducting polymers
Huseyin Bekir Yildiz1, Salim Caliskan, Musa Kamaci
1Department of Chemistry, Karamanoglu Mehmetbey University, 70100 Karaman, Turkey. yildizhb@kmu.edu.tr
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 0.007 μmol/(minelectrode) for PEO-co-PPy matrix and 0.012 μmol/(minelectrode) for CP-co-PPy matrix. Km values were determined as 3.4 and 9.2 mM 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.
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