Evaluation of redox mediators for amperometric biosensors: Ru-complex modified carbon-paste/enzyme electrodes
Autor: | Ekaterina V. Ivanova, Wolfgang Schuhmann, Alexander D. Ryabov, Viktorya S. Sergeeva, Joshua Oni, Christian Kurzawa |
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Rok vydání: | 2003 |
Předmět: |
Molecular Structure
Glucose Dehydrogenases Biophysics Alcohol Dehydrogenase General Medicine Biosensing Techniques Combinatorial chemistry Reference electrode Redox Carbon Ruthenium Carbon paste electrode chemistry.chemical_compound Electron transfer Bipyridine chemistry Glucose dehydrogenase Nafion Electrochemistry Organic chemistry Physical and Theoretical Chemistry Biosensor Electrodes Oxidation-Reduction |
Zdroj: | Bioelectrochemistry (Amsterdam, Netherlands). 60(1-2) |
ISSN: | 1567-5394 |
Popis: | The properties of reagentless amperometric biosensors are mainly governed by the interaction of the used redox enzyme and the redox mediators used to facilitate the electron-transfer reaction. Both the used redox mediators and the redox enzymes differ concerning their hydrophilicity and their properties within the matrix of a carbon-paste electrode. Since there is no general procedure which is applicable for any enzyme in combination with any redox mediator, optimisation is necessary for each possible combination. Three approaches for the development of biosensors were investigated using carbon-paste electrodes enriched with redox mediator as a base in all sensor architectures. A class of redox mediators with the common formula Ru(LL)(2)(X)(2) (where LL are 1,10-phenantroline or 2,2'-bipyridine type ligands, and X is an acido ligand) was investigated. In the first approach, enzymes were integrated into the carbon paste; in the second, the enzymes were adsorbed on the surface of the mediator-containing carbon-paste electrode and held in place by a Nafion film; and in the third approach, enzymes were entrapped in polymer films, which were electrochemically deposited onto the electrode's surface. The properties of the obtained biosensors strongly depend on the sensor architecture and the specific features of the used enzyme. Thus, our investigation using three different sensor architectures can provide valuable information about the possible interaction between a specific enzyme and a redox mediators with specific properties. |
Databáze: | OpenAIRE |
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