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Electroenzymatic reactions with sorbitol dehydrogenase on gold electrodes

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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.

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Acknowledgments

We are thankful to R. Heisel and Prof. Dr. G. Wenz (Macromolecular Organic Chemistry, Saarland University) for the synthesis of the mediator.

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Authors and Affiliations

  1. Physikalische Chemie, Gebäude B2 2, Universität des Saarlandes, 66123, Saarbrücken, Germany

    J. Gajdzik, R. Szamocki, H. Natter & R. Hempelmann

  2. Angewandte Mikrobiologie, Gebäude A1 5, Universität des Saarlandes, 66123, Saarbrücken, Germany

    G. W. Kohring & F. Giffhorn

Authors
  1. J. Gajdzik
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  2. R. Szamocki
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  3. H. Natter
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  4. G. W. Kohring
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  5. F. Giffhorn
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  6. R. Hempelmann
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Correspondence to R. Hempelmann.

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Gajdzik, J., Szamocki, R., Natter, H. et al. Electroenzymatic reactions with sorbitol dehydrogenase on gold electrodes. J Solid State Electrochem 11, 144–149 (2007). https://doi.org/10.1007/s10008-006-0213-0

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  • DOI: https://doi.org/10.1007/s10008-006-0213-0

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