A Bioanode Using Thermostable Alcohol Dehydrogenase for an Ethanol Biofuel Cell Operating at High Temperatures

Kontani, Aya; Masuda, Miyuki; Matsumura, Hirotoshi; Nakamura, Nobuhumi; Yohda, Masafumi; Ohno, Hiroyuki

doi:10.1002/elan.201300514

Cited by 12 publications

(16 citation statements)

References 33 publications

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“…It is important highlight that ADH is a redox enzyme that catalyzes the oxidation of primary and secondary alcohols to aldehydes and ketones, respectively. 36 For instance, this enzymatic reaction can be utilized for determination of ethanol in alcoholic beverages and food, and has applications in forensic science and toxicology. 37,38 ADH is found in many microorganisms, such as in yeast and the liver of animals.…”

Section: Fcfo Play Important Role On Nadh Oxidationmentioning

confidence: 99%

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Bioelectrooxidation of Ethanol Using NAD-Dependent Alcohol Dehydrogenase on Oxidized Flexible Carbon Fiber Arrays

Pereira¹,

Souza²,

Gonçalves³

et al. 2017

J. Braz. Chem. Soc.

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Section: Fcfo Play Important Role On Nadh Oxidationmentioning

confidence: 99%

“…The features described above make ADH a good enzyme for use in bioanodes of biofuel cells. 36,38 Figure 5 shows the electrochemistry of FCF-ADH (Figures 5a and 5b) and FCFO-ADH (Figures 5c and 5d). Black line corresponds to cyclic voltammograms in absence of ethanol.…”

Section: Fcfo Play Important Role On Nadh Oxidationmentioning

confidence: 99%

Bioelectrooxidation of Ethanol Using NAD-Dependent Alcohol Dehydrogenase on Oxidized Flexible Carbon Fiber Arrays

Pereira¹,

Souza²,

Gonçalves³

et al. 2017

J. Braz. Chem. Soc.

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“…To our limited knowledge, this present biobattery is the one running on the second highest temperature among all the EFCs reported. The highest temperature of EFC was 80 °C by using a thermostable alcohol dehydrogenase but its current density was only 0.21 mA cm −2 (5% of this study)37.…”

Section: Discussionmentioning

confidence: 64%

Coenzyme Engineering of a Hyperthermophilic 6-Phosphogluconate Dehydrogenase from NADP+ to NAD+ with Its Application to Biobatteries

Chen

Zhu

Huang

et al. 2016

Sci Rep

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Engineering the coenzyme specificity of redox enzymes plays an important role in metabolic engineering, synthetic biology, and biocatalysis, but it has rarely been applied to bioelectrochemistry. Here we develop a rational design strategy to change the coenzyme specificity of 6-phosphogluconate dehydrogenase (6PGDH) from a hyperthermophilic bacterium Thermotoga maritima from its natural coenzyme NADP+ to NAD+. Through amino acid-sequence alignment of NADP+- and NAD+-preferred 6PGDH enzymes and computer-aided substrate-coenzyme docking, the key amino acid residues responsible for binding the phosphate group of NADP+ were identified. Four mutants were obtained via site-directed mutagenesis. The best mutant N32E/R33I/T34I exhibited a ~6.4 × 104-fold reversal of the coenzyme selectivity from NADP+ to NAD+. The maximum power density and current density of the biobattery catalyzed by the mutant were 0.135 mW cm−2 and 0.255 mA cm−2, ~25% higher than those obtained from the wide-type 6PGDH-based biobattery at the room temperature. By using this 6PGDH mutant, the optimal temperature of running the biobattery was as high as 65 °C, leading to a high power density of 1.75 mW cm−2. This study demonstrates coenzyme engineering of a hyperthermophilic 6PGDH and its application to high-temperature biobatteries.

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“…Third, the operational conditions are very mild and safe. The properties of enzymatic reactions enable EFCs to operate at physiological pH, room temperature, and ambient pressure, although the recent use of stable extremophilic enzymes offers the possibility to work at temperatures of up to 85 °C or at a pH value as low as 2. , In addition, redox enzymes provide exceptional specificity toward their natural substrates, thus allowing the assembly of the bioanode and biocathode in a single membrane-less cell and the miniaturization of EFCs . Another consequence of high enzyme specificity is that EFCs can use fuels without the need for intensive purification steps.…”

Section: Introductionmentioning

confidence: 99%

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

et al. 2019

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The ever-increasing demands for clean and sustainable energy sources combined with rapid advances in bio-integrated portable or implantable electronic devices have stimulated intensive research activities in enzymatic (bio)fuel cells (EFCs). The use of renewable biocatalysts, the utilization of abundant green, safe, and high energy density fuels, together with the capability of working at modest and biocompatible conditions, make EFCs promising as next generation alternative power sources. However, the main challenges (low energy density, relatively low power density, poor operational stability and limited voltage output) hinder future applications of EFCs. This review aims at exploring the underlying mechanism of EFCs and providing possible practical strategies, methodologies and insights to tackle of these issues. Firstly, this review summarizes approaches in achieving high energy densities in EFCs, particularly, employing enzyme cascades for the deep/complete oxidation of fuels. Secondly, strategies for increasing power densities in EFCs, including increasing enzyme activities, facilitating electron transfers, employing nanomaterials, and designing more efficient enzyme-electrode interfaces, are described. The potential of EFCs/(super)capacitor combination is discussed. Thirdly, the review evaluates a range of strategies for improving the stability of EFCs, including the use of different enzyme immobilization approaches, tuning enzyme properties, designing protective matrixes, and using microbial surface displaying enzymes. Fourthly, approaches for the improvement of the cell voltage of EFCs are highlighted. Finally, future developments and a prospective on EFCs are envisioned.

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A Bioanode Using Thermostable Alcohol Dehydrogenase for an Ethanol Biofuel Cell Operating at High Temperatures

Cited by 12 publications

References 33 publications

Bioelectrooxidation of Ethanol Using NAD-Dependent Alcohol Dehydrogenase on Oxidized Flexible Carbon Fiber Arrays

Bioelectrooxidation of Ethanol Using NAD-Dependent Alcohol Dehydrogenase on Oxidized Flexible Carbon Fiber Arrays

Coenzyme Engineering of a Hyperthermophilic 6-Phosphogluconate Dehydrogenase from NADP+ to NAD+ with Its Application to Biobatteries

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

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