The development of a peroxidase biosensor for monitoring phenol and related aromatic compounds
✍ Scribed by T. Ruzgas; J. Emnéus; L. Gorton; G. Marko-Varga
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 825 KB
- Volume
- 311
- Category
- Article
- ISSN
- 0003-2670
No coin nor oath required. For personal study only.
✦ Synopsis
The possibility of horseradish peroxidase (HRP) modified solid graphite and carbon paste electrodes to perform as biosensors for the determination of phenol and related compounds was studied. Phenoxy radicals, formed during the enzymatic oxidation of phenolic compounds in the presence of hydrogen peroxide, are reduced electrochemically. The reduction current is proportional to their concentration in the solution. From the hydrodynamic voltammograrns, calibration curves and performance stability it was concluded that the reduction of phenoxy radicals is more efficient at the solid graphite electrodes in comparison with the carbon paste based sensor. The potentials, at which electrochemical reduction of phenoxy radicals appears, depend on the electron donating properties of the substituent in the phenol molecule. It was found that, in the presence of lo-20 /.LM of H,O, in the solution, the responses of HRP-modified solid graphite electrode to p-cresol are rate limited by the enzymatic reaction. The electrode was most stable when the buffer solution contained 5% of methanol. Among 20 phenolic compounds tested, phenol, catechol, resorcinol, p-cresol, 4-chlorophenol, 2,4-dichlorophenol, 4-chloro-3-methylphenol, vanillin and 2-amino-4-chlorophenol can be determined. The greatest sensitivity was obtained for 2-amino-4-chlorophenol(85 nA cm-* PM-'1.
📜 SIMILAR VOLUMES
Once activated by hydrogen peroxide, horse-focused on the use of HRP because the enzyme is less radish peroxidase (HRP) catalyzes the oxidation of aquecostly to produce, inactivates less rapidly, or acts on a ous aromatic compounds to produce high molecular wider variety of substrates than other oxi
Bulk-modified epoxy-graphite tyrosinase biosensors were fabricated by four different procedures. The influence of these fabrication procedures on the analytical performance of the enzyme electrode in an amperometric wall-jet flow cell has been studied. The bioprobe performance is assessed by cyclic