Multi-Substrate Biofuel Cell Utilizing Glucose, Fructose and Sucrose as the Anode Fuels

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.

Mini-Review: Recent Technologies of Electrode and System in the Enzymatic Biofuel Cell (EBFC)

“…The arrangement of the enzyme on the electrode surface plays a vital role so that the utilization of the enzyme can be maximized and provide excellent contact between the enzyme and the electrode surface. The work of Kizling et al [75] resulted in cascade enzyme arrangement at the anode of the EBFC. In this study, various enzymes were used, namely mutarotase, invertase, fructose dehydrogenase, and flavine adenine dinucleotide (FAD)dependent glucose dehydrogenase in addition to using single or mixed substrates such as glucose, fructose, and sucrose.…”

“…The comparison of other studies in this study shows that the resulting bioanode can produce a current as high as 2230 µA/cm 2 and maintain power generation for eight days before falling by 38%. Enzyme arrangement using nanoparticles that have a high surface area to volume ratio for enzyme loading [16] leads to a reduction in the distance of electron transport [75] and thus enhances the performance and stability of the EBFC [33].…”

Advanced Signal-Amplification Strategies for Paper-Based Analytical Devices: A Comprehensive Review

“…The utilization of enzymes for signal amplification is based on the catalytic activity of a natural enzyme that causes oxidation or reduction of a substrate, which in turn leads to sequential activation of the downstream enzymes that result in synergistic signal amplification within seconds. Currently, many multi-enzyme cascade systems have been developed, allowing rapid and sensitive detection of targets by paper-based sensing devices [ 57 , 58 , 59 , 60 , 61 ]. Another way to intensify the enzyme-labeled signal is to functionalize enzymes by linking them with nanoparticles [ 62 ].…”

Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase

“…The ability to use the well-known, well-characterized, inexpensive oxidase of d -glucose as a more general monosaccharide-oxidase, opens the possibility to extend this enzyme’s many applications to new directions, such as using a single enzyme for sugar mixtures, rather than multiple-enzymatic systems for the construction of a biofuel cell 52 . Moreover, GOx can now be utilized as an enzyme for monosaccharides that otherwise do not have naturally occurring oxidase enzymes, such as fructose and xylose.…”