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Potential-step coulometry of d-glucose using a novel FAD-dependent glucose dehydrogenase

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Abstract

This paper describes the construction and characterization of a batch-type coulometric system for the detection of d-glucose using a novel FAD-dependent glucose dehydrogenase. In order to overcome the problem of interferents, such as ascorbate and urate, a potential-step method was proposed to separate the electrolysis reactions of interferents and d-glucose by selecting a mediator possessing an appropriate formal potential. The rapid oxidative consumption of the interferents proceeded in the first step, whereas the mediator and glucose remained reduced. In the second step, the mediator was immediately oxidized, and subsequent bioelectrocatalytic oxidation of d-glucose occurred with the aid of aldose 1-epimerase. In this study, potassium octacyanomolybdate (IV) with a formal potential of 0.6 V vs. Ag|AgCl was chosen as a mediator, and the first and second electrolysis potentials were set at 0.4 V and 0.8 V, respectively, by considering the heterogeneous electron-transfer kinetics and the potential window. The background-corrected response in charge corresponded to 99±2 % efficiency in terms of the amount of d-glucose.

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Acknowledgements

The authors would like to thank Ikeda Food Research Co., Ltd (Japan) for kindly donating FAD-GDH. This work was supported in part by grant-aid for scientific research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (MECSSTJ), and by COE for Microbial Process Development Pioneering Future Production Systems (COE program of MECSSTJ).

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Authors and Affiliations

  1. Division of Applied Life Science, Graduated School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan

    Seiya Tsujimura, Shinki Kojima, Tokuji Ikeda & Kenji Kano

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  1. Seiya Tsujimura
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  2. Shinki Kojima
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  3. Tokuji Ikeda
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  4. Kenji Kano
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Correspondence to Seiya Tsujimura.

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Tsujimura, S., Kojima, S., Ikeda, T. et al. Potential-step coulometry of d-glucose using a novel FAD-dependent glucose dehydrogenase. Anal Bioanal Chem 386, 645–651 (2006). https://doi.org/10.1007/s00216-006-0421-6

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  • DOI: https://doi.org/10.1007/s00216-006-0421-6

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