A tyrosinase biosensor based on ordered mesoporous carbon-Au/L-lysine/Au nanoparticles for simultaneous determination of hydroquinone and catechol.

TitleA tyrosinase biosensor based on ordered mesoporous carbon-Au/L-lysine/Au nanoparticles for simultaneous determination of hydroquinone and catechol.
Publication TypeJournal Article
Year of Publication2013
AuthorsTang L, Zhou Y, Zeng G, Li Z, Liu Y, Zhang Y, Chen G, Yang G, Lei X, Wu M
JournalThe Analyst
Volume138
Issue12
Pagination3552-60
Date Published2013 Jun 21
Abstract

A novel biosensor was developed based on tyrosinase immobilization with ordered mesoporous carbon-Au (OMC-Au), L-lysine membrane and Au nanoparticles on a glassy carbon electrode (GCE). It was applied for the simultaneous determination of dihydroxybenzene isomers using differential pulse voltammetry (DPV). The tyrosinase/OMC-Au/L-lysine/Au film was characterized by scanning electron microscopy (SEM) and impedance spectra. Under optimized conditions, the DPV study results for two isomers, hydroquinone (HQ, 1,4-dihydroxybenzene) and catechol (CC, 1,2-dihydroxybenzene) showed low peak potentials, and the peak-to-peak difference was about 135.85 mV, which ensured the anti-interference ability of the biosensor and made simultaneous detection of dihydroxybenzene isomers possible in real samples. DPV peak currents increased linearly with concentration over the range of 4.0 × 10(-7) to 8.0 × 10(-5) M, and the detection limits of hydroquinone and catechol were 5 × 10(-8) M and 2.5 × 10(-8) M (S/N = 3), respectively. The tyrosinase biosensor exhibited good repeatability and stability. In addition, the response mechanism of enzyme catalysed redox on the OMC-Au/L-lysine/Au film modified electrode based on electrochemical study was discussed. The proposed method could be extended for the development of other enzyme-based biosensors.

DOI10.1039/c3an36928e
Alternate JournalAnalyst