A new approach to enhance the sensitivity of a tyrosinase based biosensor for the amperometric phenol detection at -0.2 V vs. Ag/AgCl (0.1 M KCl) has been described. The procedure consists of the cooperative functioning of tyrosinase and horseradish peroxidase in the presence of H,O,. Monoenzyme and
Peroxidase-glucose oxidase-poly(amphiphilic pyrrole) bioelectrode for selectively mediated amperometric detection of glucose
✍ Scribed by Ionel C. Popescu; Serge Cosnier; Pierre Labbé
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 733 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1040-0397
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✦ Synopsis
Monoenzyme (HRP) and bilayedmonolayer bienzyme (HRP-GOX) bioelectrodes were realized by the oxidative electropolymerization of amphiphilic pyrrole monomer 1 enzyme(s) mixtures, previously adsorbed on the surface of a glassy carbon electrode. Cyclic voltammetry measurements, canied out on poly 1-HRP modified electrodes yhowed that the electrocatalytical reduction of H202, in the presence of K,Fe(CN), as mediator, occurs at applied potentials well placed in the optimal potential range for amperometric detection. An optimization study concerning the mediator concentration, the amount of the immobilized enzyme(s), the electrode material and the matrix structure (mono-or bilayer) was performed in order to obtain the glucose biosensor. At an a plied potential of -0.1 V (vs. SCE), batch amperometric response to Hz02 for the HRP modified electrodes gave a sensitivity of ca. 280 mA M-'cm-' (up to 0.65 mM). For monolayer biosensor the sensitivity to glucose was ca. 170 mAM-' cm-' (up to 1.9 mM). The interference of ascorbate, urate and acetaminophen was found almost negligible.
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