Increasing the coulombic efficiency of glucose biofuel cell anodes by combination of redox enzymes

Tasca, Federico; Gorton, Lo; Kujawa, Magdalena; Patel, Ilabahen; Harreither, Wolfgang; Peterbauer, Clemens K.; Ludwig, Roland; Nöll, Gilbert

doi:10.1016/j.bios.2009.12.017

Cited by 87 publications

(86 citation statements)

References 51 publications

(93 reference statements)

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“…Anodic reactions will consume part of that glucose and oxidize it to gluconic acid, pKa 3.86. Usage of a multiple enzyme bioanode [4] would produce additional acidic compounds such as 2,3--diketogluconate, locally increasing the acidity. Placing the biocathode next to the bioanode output would produce an acidification of biocathode environment; improving its performance in the case of a Lc--modified electrode.…”

Section: Introductionmentioning

confidence: 99%

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Laccase cathode approaches to physiological conditions by local pH acidification

Clot

Gutiérrez-Sánchez

Shleev

et al. 2012

Electrochemistry Communications

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Section: Introductionmentioning

confidence: 99%

“…glucose in biofluids) as fuel. [2,3] The oxidation of the organic compound takes place at a bioanode [4] and the reduction of the oxygen takes place at a biocathode. [5] While the anode has been the subject of extensive research and development, [6] the performance of O2 reducing cathodes needs improvement.…”

Section: Introductionmentioning

confidence: 99%

Laccase cathode approaches to physiological conditions by local pH acidification

Clot

Gutiérrez-Sánchez

Shleev

et al. 2012

Electrochemistry Communications

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“…Using 50 mM glucose, the obtained OCV of 0.6 V and P max of 167 μW cm −2 surpass the only reported hybrid EFC (using PDH-CDH bioanode and Pt cathode), that yielded an OCV of 0.5 V and P max of 135 μW cm −2 operating in 100 mM glucose. 33 The origin of this enhanced performance is attributed to different reasons including: (i) the performance of the engineered glucose oxidase compared to CDH, (ii) the FcMe 2 -C 3 -LPEI redox polymer used to facilitate MET from PDH compared to the Os redox polymer hydrogel employed in the reference and (iii) the use of bilirubin oxidase at the biocathode that enables the a 4e − reduction of O 2 to H 2 O at a high potential compared to a Pt abiotic cathode.…”

Section: Resultsmentioning

confidence: 99%

“…32 The combination of two anodic enzymes to improve the coulombic efficiency of EFC was reported between 2010-2013 using PDH and CDH. [33][34][35] Photometric measurements showed that possibility of performing a 4e − oxidation of glucose by PDH bioelectrodes and a 6e − oxidation of glucose at PDH + CDH bioelectrodes. The first constructed hybrid EFC (using a Pt black electrode as the cathode) yielded an open circuit voltage of 0.5 V and maximum power density of 135 μW cm −2 in 100 mM glucose at pH 7.4.…”

Section: Yields 24ementioning

confidence: 99%

“…The first constructed hybrid EFC (using a Pt black electrode as the cathode) yielded an open circuit voltage of 0.5 V and maximum power density of 135 μW cm −2 in 100 mM glucose at pH 7.4. 36 However, no stability tests were performed to evaluate the real suitability of the approach. In addition, the versatility is limited by CDH that cannot oxidize a large range of substrates.…”

Section: Yields 24ementioning

confidence: 99%

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Rational Combination of Promiscuous Enzymes Yields a Versatile Enzymatic Fuel Cell with Improved Coulombic Efficiency

Holade

Yuan

Milton

et al. 2016

J. Electrochem. Soc.

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Enzymatic fuel cells (EFCs) utilize enzymatic catalysts to convert chemical energy to electrical energy, typically by performing a 2e − oxidation of saccharides. In the case of sugars, a single 2e − oxidation does not fully exploit this energy-dense fuel that is capable of producing 24e − from its complete oxidation to CO 2 . Here, we propose an efficient approach to design a versatile EFC that can produce electrical energy from 12 (oligo)saccharides by combining two enzymes that possess diverse substrate specificities: pyranose dehydrogenase (PDH) and a broad glucose oxidase (bGOx). Additionally, PDH is able to perform single or two sequential oxidations of glucose (at C2 and/or C3) yielding up to 4e − , whereas bGOx only performs a single 2e − oxidation at the anomeric (C1) position. By combining PDH and bGOx, we demonstrate the ability to achieve deep oxidation of glucose and xylose, whereby each is able to undergo sequential oxidations by PDH and bGOx. Additionally, we demonstrate that this deep oxidation can yield improved performances of EFCs. For example, an EFC comprised of a bi-enzymatic PDH/bGOx bioanode using xylose as a fuel yields a maximum current density of 586 ± 3 μAcm −2 whereas mono-enzymatic PDH or bGOx EFC bioanodes result in current densities of 440 ± 4 μAcm −2 and 120 ± 1 μAcm −2 , respectively. Owing to their high selectivity, enzymatic fuel cells (EFCs) are devices that offer multiple advantages over traditional fuel cell systems (i.e. H 2 /O 2 ) such that they are able to operate under physiological temperature and pH and are able to produce electrical energy from common energy-dense fuels, such as glucose. [1][2][3][4][5] In contrast to traditional fuel cells that operate on precious metal catalysts, EFCs employ enzymes as biocatalysts at the anode and cathode. In addition to mild operational requirements, inherent substrate specificity of enzymes can allow for the operation of EFCs in the absence of a membrane separator between the anodic and cathodic compartments. 6 Theoretically, the complete oxidation of a single glucose molecule to CO 2 yields 24e − that could be harnessed within an EFC. 7 While many examples of high power EFCs can be found, [8][9][10][11][12] the vast majority of glucose EFCs report only a single 2e − oxidation, thereby operating at <10 % efficiency. In the recent past, alternative enzymes to the commonly used glucose oxidase (GOx) for glucose oxidation have been explored, namely flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH), 8,[13][14][15] nicotinamide adenine dinucleotidedependent glucose dehydrogenase (NAD-GDH), [16][17][18] pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH), 19,20 cellobiose dehydrogenase (CDH), 21,22 pyranose oxidase (POx) 23 and pyranose dehydrogenase (PDH).24-27 FAD-GDH and CDH, which both oxidize their substrates at the anomeric (C1) position, are promising alternatives to GOx, because they do not utilize molecular oxygen as their electron acceptor, thus bioanode efficiency is retained in the presenc...

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Anodic Bioelectrocatalysis: From Metabolic Pathways To Metabolons

Pelster

Rasmussen

2014

Enzymatic Fuel Cells

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Increasing the coulombic efficiency of glucose biofuel cell anodes by combination of redox enzymes

Cited by 87 publications

References 51 publications

Laccase cathode approaches to physiological conditions by local pH acidification

Laccase cathode approaches to physiological conditions by local pH acidification

Rational Combination of Promiscuous Enzymes Yields a Versatile Enzymatic Fuel Cell with Improved Coulombic Efficiency

Anodic Bioelectrocatalysis: From Metabolic Pathways To Metabolons

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