4.6 Article

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

Journal

ANALYST
Volume 138, Issue 12, Pages 3552-3560

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c3an36928e

Keywords

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Funding

  1. Program for the Outstanding Young Talents of China
  2. National Natural Science Foundation of China [51222805]
  3. Program for New Century Excellent Talents in University from the Ministry of Education of China [NCET-11-0129]
  4. Fundamental Research Funds for the Central Universities, Hunan University
  5. Foundation for the Author of Excellent Doctoral Dissertation of Hunan Province
  6. Hunan Provincial Innovation Foundation For Postgraduate [CX2009B080]

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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 x 10(-7) to 8.0 x 10(-5) M, and the detection limits of hydroquinone and catechol were 5 x 10(-8) M and 2.5 x 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.

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