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A novel amperometric enzyme inhibition biosensor based on xanthine oxidase immobilised onto glassy carbon electrodes for bisphenol A determination

A novel and simple biosensor for the determination of bisphenol A (BPA) based on xanthine oxidase (XOD) enzymatic inhibition has been developed. The biosensor was prepared from xanthine oxidase immobilised by crosslinking with glutaraldehyde, with hypoxanthine as enzyme substrate, and was successful...

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Bibliographic Details
Published in:Talanta (Oxford) 2018-07, Vol.184, p.388-393
Main Authors: Ben Messaoud, Najib, Ghica, Mariana Emilia, Dridi, Cherif, Ben Ali, Mounir, Brett, Christopher M.A.
Format: Article
Language:English
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Summary:A novel and simple biosensor for the determination of bisphenol A (BPA) based on xanthine oxidase (XOD) enzymatic inhibition has been developed. The biosensor was prepared from xanthine oxidase immobilised by crosslinking with glutaraldehyde, with hypoxanthine as enzyme substrate, and was successfully applied to the determination of BPA using fixed potential amperometry. Biosensor performance was optimised with respect to the applied potential, influence of pH of the electrolyte solution, XOD loading and the substrate concentration. The enzyme inhibition mechanism was evaluated from Cornish-Bowden plus Dixon plots and was found to be reversible and competitive with an apparent inhibition constant of 8.15 nM. Under optimised conditions, the determination of BPA can be achieved in the linear range up to 41 nM with a detection limit of 1.0 nM, which is equal to the lowest reported in the literature, with very good repeatability and reproducibility. The selectivity of the biosensor was evaluated by performing an interference study and found to be excellent; and stability was investigated. It was successfully applied to the detection of BPA in mineral water and in river water. [Display omitted] •A novel electrochemical enzyme inhibition biosensor for bisphenol A was developed.•The biosensor uses xanthine oxidase enzyme and hypoxanthine enzyme substrate.•A very low detection limit of 1 nM was achieved.•The enzyme inhibition mechanism is reversible and competitive.•Application to analysis of mineral and river waters is demonstrated.
ISSN:0039-9140
1873-3573
DOI:10.1016/j.talanta.2018.03.031