Electroenzymatic reactions with sorbitol dehydrogenase on gold electrodes |
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Authors: | J. Gajdzik R. Szamocki H. Natter G. W. Kohring F. Giffhorn R. Hempelmann |
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Affiliation: | 1.Physikalische Chemie, Geb?ude B2 2,Universit?t des Saarlandes,Saarbrücken,Germany;2.Angewandte Mikrobiologie, Geb?ude A1 5,Universit?t des Saarlandes,Saarbrücken,Germany |
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Abstract: | Sorbitol dehydrogenase (SDH) originating from recombinant Escherichia coli cells is immobilized on gold electrodes. First of all, (4-carboxy-2,5,7-trinitrofluorenyliden)malon-nitrile (CTFM) is adsorbed on the surface as mediator. In a second step, the cofactor β-nicotinamide adenine dinucleotide (NAD+) is immobilized on the gold electrode. Due to the formation of a complex between the mediator and the cofactor, the electron transfer rate can be enhanced by adding calcium ions to the buffer. The immobilization of NAD+ and SDH on the surface has been achieved by cross-linking with the glutaraldehyde/bovine serum albumin system. The successful biofunctionalization is monitored by cyclic voltammetry.Paper presented at the “Jahrestagung der Fachgruppe Angewandte Electrochemie der Gesellschaft Deutscher Chemiker, Düsseldorf, 11.-14.09.2005”. |
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Keywords: | Biofunctionalized electrodes Electroenzymatics NAD+/NADH Sorbitol dehydrogenase Glutaraldehyde |
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