Print Email Facebook Twitter Electron transfer between a quinohemoprotein alcohol dehydrogenase and an electrode via a redox polymer network Title Electron transfer between a quinohemoprotein alcohol dehydrogenase and an electrode via a redox polymer network Author Stigter, E.C.A. de Jong, G.A.H. Jongejan, J.A. Duine, J.A. van der Lugt, J.P. Somers, W.A.C. TNO Voeding Publication year 1996 Abstract A quinohemoprotein alcohol dehydrogenase (QH-EDH) from Comamonas testosteroni was immobilized on an electrode in a redox polymer network consisting of a polyvinylpyridine partially N-complexed with osmiumbis-(bipyridine)chloride. The enzyme effectively transfers electrons to the electrode via the polymer. An average maximum catalytic current of 11 μA cm-2 was observed with 1-propanol as the substrate. The maximum activity of the enzyme electrode (current density) for primary alcohols is independent of the type of substrate in contrast with the activity of the free enzyme. Affinity constants of the immobilized QH-EDH for different substrates are comparable with the values found for the free enzyme. Typical half-lives for the immobilized enzyme electrodes are in the order of 5 h. A quinohemoprotein alcohol dehydrogenase (QH-EDH) from Comamonas testosteroni was immobilized on an electrode in a redox polymer network consisting of a polyvinylpyridine partially N-complexed with osmiumbis-(bipyridine)chloride. The enzyme effectively transfers electrons to the electrode via the polymer. An average maximum catalytic current of 11 μA cm-2 was observed with 1-propanol as the substrate. The maximum activity of the enzyme electrode (current density) for primary alcohols is independent of the type of substrate in contrast with the activity of the free enzyme. Affinity constants of the immobilized QH-EDH for different substrates are comparable with the values found for the free enzyme. Typical half-lives for the immobilized enzyme electrodes are in the order of 5 h. Subject NutritionImmobilizationQuinohemoprotein alcohol dehydrogenaseAlcoholsBiochemistryCharge transferCurrent densityElectrochemistryElectronsEnzyme immobilizationEnzyme sensorsPolymersProteinsAffinity constantsBioelectrochemistryElectron transferEnzyme electrodeRedox polymer networkEnzymesAlcohol dehydrogenaseAlcohol derivativeBipyridine derivativeHemoproteinOsmium derivativePropanolPyridine derivativeElectron transportEnzyme substrateOxidation reduction reaction To reference this document use: http://resolver.tudelft.nl/uuid:0bc8d60b-cba8-4faf-a0f2-6e933ff8b9be DOI https://doi.org/10.1016/0141-0229(95)00158-1 TNO identifier 233322 ISSN 0141-0229 Source Enzyme and Microbial Technology, 18 (7), 489-494 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.