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Sensors 2017, 17(11), 2636; https://doi.org/10.3390/s17112636

Mediator Preference of Two Different FAD-Dependent Glucose Dehydrogenases Employed in Disposable Enzyme Glucose Sensors

1
Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan
2
Institute of Global Innovation Research, Tokyo University of Agriculture and Technology, 3-8-1 Harumi-cho, Fuchu, Tokyo 183-8538, Japan
3
Ultizyme International Ltd., 1-13-16, Minami, Meguro, Tokyo 152-0013, Japan
*
Author to whom correspondence should be addressed.
Received: 10 October 2017 / Revised: 13 November 2017 / Accepted: 14 November 2017 / Published: 16 November 2017
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Abstract

Most commercially available electrochemical enzyme sensor strips for the measurement of blood glucose use an artificial electron mediator to transfer electrons from the active side of the enzyme to the electrode. One mediator recently gaining attention for commercial sensor strips is hexaammineruthenium(III) chloride. In this study, we investigate and compare the preference of enzyme electrodes with two different FAD-dependent glucose dehydrogenases (FADGDHs) for the mediators hexaammineruthenium(III) chloride, potassium ferricyanide (the most common mediator in commercial sensor strips), and methoxy phenazine methosulfate (mPMS). One FADGDH is a monomeric fungal enzyme, and the other a hetero-trimeric bacterial enzyme. With the latter, which contains a heme-subunit facilitating the electron transfer, similar response currents are obtained with hexaammineruthenium(III), ferricyanide, and mPMS (6.8 µA, 7.5 µA, and 6.4 µA, respectively, for 10 mM glucose). With the fungal FADGDH, similar response currents are obtained with the negatively charged ferricyanide and the uncharged mPMS (5.9 µA and 6.7 µA, respectively, for 10 mM glucose), however, no response current is obtained with hexaammineruthenium(III), which has a strong positive charge. These results show that access of even very small mediators with strong charges to a buried active center can be almost completely blocked by the protein. View Full-Text
Keywords: glucose dehydrogenase; flavin adenine dinucleotide; Aspergillus flavus; Burkholderia cepacia; enzyme sensor strip; mediated electron transfer; potassium ferricyanide; methoxy phenazine methosulfate; hexaammineruthenium chloride glucose dehydrogenase; flavin adenine dinucleotide; Aspergillus flavus; Burkholderia cepacia; enzyme sensor strip; mediated electron transfer; potassium ferricyanide; methoxy phenazine methosulfate; hexaammineruthenium chloride
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Loew, N.; Tsugawa, W.; Nagae, D.; Kojima, K.; Sode, K. Mediator Preference of Two Different FAD-Dependent Glucose Dehydrogenases Employed in Disposable Enzyme Glucose Sensors. Sensors 2017, 17, 2636.

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