In order to prepare a biosensor for the determination of uric acid, electropolymerization of pyrrole on Pt surface was carried out with an electrochemical cell containing pyrrole, ferrocene (as a electron mediator) and tetrabutylammonium tetrafluoroborat in acetonitrile by cyclic voltammetry between 0.0 and 1.0 V (vs. Ag/AgCl) at a scan rate of 50 mV/s upon Pt electrode. Uricase was immobilized by a glutaraldehyde/gelatine croslinking procedure on to polypyrrole film after the electropolymerization processes. The response of the biosensor against uric acid was measured after 330 seconds following the application of a constant potential of +0.7 V (vs. Ag/AgCl). The resulting biosensor exhibits excellent electrocatalysis for the uric acid. The amperometric determination is based on the electrochemical detection of H₂O₂, which is generated in enzymatic reaction of uric acid. The sensor responds to uric acid with a detection limit of 5.0 × 10⁻⁷ M. The sensor remains relatively stable for 5 weeks. Interference effect were investigated on the amperometric response of the biosensor. Determination of uric acid was carried out in the biological fluids by biosensor.

A new amperometric biosensor was developed for determining hypoxanthine in fish meat. Xanthine oxidase with pyrrole and polyvinylsulphonate was immobilized on the surface of a platinum electrode by electropolymerization. The determination of xanthine-hypoxanthine was performed by means of oxidation of uric acid liberated during the enzyme reaction on the surface of the enzyme electrode at + 0.30V (SCE). The effects of pH, substrate concentration, and temperature on the response of the xanthine-hypoxanthine biosensor were investigated. The linear working range of the enzyme electrode was 1.0 × 10⁻⁷ –1.0 × 10⁻³ M of the hypoxanthine concentration, and the detection limit was 1.0 × 10⁻⁷M. The apparent K_m(app) and I_max of the immobilized xanthine oxidase were found to be 0.0154 mM and 1.203 μA/mM, respectively. The best pH and temperature value for xanthine oxidase were selected as 7.75 and 25°C, respectively. The sensor was used for the determination of hypoxhantine in fish meat. Results show that the fish degraded very rapidly after seven days and the hypoxanthine amount was found to increase over days of storage.

In this paper, a novel amperometric cholesterol biosensor with immobilization of cholesterol oxidase on electrochemically polymerized polypyrrole–polyvinylsulphonate (PPy–PVS) films has been accomplished via the entrapment technique on the surface of a platinum electrode. Electropolymerization of pyrrole and polyvinylsulphonate on the Pt surface was carried out by cyclic voltammetry between -1.0 and +2.0 V (vs. Ag/AgCl) at a scan rate of 100 mV upon the Pt electrode with an electrochemical cell containing pyrrole and polyvinylsulphonate. The amperometric determination is based on the electrochemical detection of H₂O₂ generated in the enzymatic reaction of cholesterol. Determination of cholesterol was carried out by the oxidation of enzymatically produced H₂O₂ at 0.4 V vs. Ag/AgCl. The effects of pH and temperature were investigated and optimum parameters were found to be 7.25 and 35 °C, respectively. The storage stability and operational stability of the enzyme electrode were also studied. The results show that 32% of the response current was retained after 19 activity assays. The prepared cholesterol biosensor retained 43% of initial activity after 45 days when stored in 0.1 M phosphate buffer solution at 4 °C.

In this study, a new amperometric biosensor for the determination of hypoxanthine was developed. To this aim, polypyrrole-polyvinyl sulphonate films were prepared on the platinum electrode by the electropolymerization of pyrrole in the presence of polyvinyl sulphonate. Xanthine oxidase and uricase enzymes were immobilized in polypyrrole-polyvinyl sulphonate via the entrapment method. Optimum conditions of enzyme electrode were determined. Hypoxanthine detection is based on the oxidation of hydrogen peroxide at +400 mV produced by the enzymatic reaction on the enzyme electrode surface. The linear working range of biosensor for hypoxanthine was determined. The effects of pH and temperature on the response of the hypoxanthine biosensor were investigated. Optimum pH and temperature were measured as 8 and 30°C, respectively. Operational and storage stability of the biosensor were determined. After 20 assays, the biosensor sustained 74.5% of its initial performance. After 33 days, the biosensor lost 36% of its initial performance. The performance of the biosensor was tested in real samples.