Abstract
A significant problem still exists with the low power output and durability of the bioelectrochemical fuel cells. We constructed a fuel cell with an enzymatic cascade at the anode for efficient energy conversion. The construction involved fabrication of the flow-through cell by three-dimensional printing. Gold nanoparticles with covalently bound naphthoquinone moieties deposited on cellulose/polypyrrole (CPPy) paper allowed us to significantly improve the catalysis rate, both at the anode and cathode of the fuel cell. The enzymatic cascade on the anode consisted of invertase, mutarotase, Flavine Adenine Dinucleotide (FAD)-dependent glucose dehydrogenase and fructose dehydrogenase. The multi-substrate anode utilized glucose, fructose, sucrose, or a combination of them, as the anode fuel and molecular oxygen were the oxidant at the laccase-based cathode. Laccase was adsorbed on the same type of naphthoquinone modified gold nanoparticles. Interestingly, the naphthoquinone modified gold nanoparticles acted as the enzyme orienting units and not as mediators since the catalyzed oxygen reduction occurred at the potential where direct electron transfer takes place. Thanks to the good catalytic and capacitive properties of the modified electrodes, the power density of the sucrose/oxygen enzymatic fuel cells (EFC) reached 0.81 mW cm−2, which is beneficial for a cell composed of a single cathode and anode.
Highlights
Enzymatic fuel cells (EFCs) are energy converting devices that are capable of delivering power when operating in biological solutions
The cellulose/polypyrrole paper-based EFC was composed of an anode comprising four enzymes: invertase, mutarotase, fructose dehydrogenase and glucose dehydrogenase (FAD dependent) and a cathode based on laccase
INV, from Saccharomyces cerevisiae (EC 3.2.1.26) and laccase, LAC, from Trametes Hirsuta (1.10.3.2) from Sigma-Aldrich (Poznan, Poland), Flavine Adenine Dinucleotide (FAD)-dependent glucose dehydrogenase, GDH, (E.C. 1.1.99.10, Aspergillus sp.) from Sekisui Diagnostics (Maidstone, UK), D-fructose dehydrogenase, FDH, from Gluconobacter sp. (EC 1.1.99.11) from Sorachim, mutarotase, MUT, from porcine (EC 5.1.3.3) from Sinus Biochemistry and Electrophoresis, and GmbH were used without any further purification
Summary
Enzymatic fuel cells (EFCs) are energy converting devices that are capable of delivering power when operating in biological solutions. EFCs have the capability to operate at room temperature and neutral pH, conditions which cannot typically be employed with a conventional fuel cell. The obtained power and energy densities are always significantly lower than the theoretical values, due to the fact that energy is harvested from the first oxidation step of a single enzyme. Most of the studies on EFCs have focused on single enzyme electrodes generating current via an enzymatically catalyzed transformation step [1,2,3]. In order to further exploit the energy stored in the substrate or broaden the range of applicable fuels, the electrodes can be modified with several enzymes working in parallel or showing cascading functions. One of the most effective coulombic efficiencies was reported by Zhang et al, who employed the pentose phosphate pathway and obtained current density, 6 mA cm−2, and power density, 0.8 mW cm−2 [7,8]
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