Biofuel Cells. Группа авторов

Biofuel Cells - Группа авторов


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V with a maximum power density of 0.9 mW cm−2.

      1.4.4 Metal–Organic Framework (MOF)-Based Carbonaceous Materials as Bioelectrodes for BFCs

      On the other hand, the use of MOF for the preparation of enzymatic electrodes is limited. Li et al. [124] developed an enzymatic BFC encapsulating laccase in the ZIF-8 MOF. This electrode array was combined with bacterial cellulose and carboxylated carbon nanotubes achieving OCVs close to 0.3 V, and a maximum current density of 3.68 W m−3. Zhang et al. [125] reported the use of the IRMOF-8 impregnated in carbon nanotubes to develop a porous carbon intercalated by multi-walled carbon nanotubes (PC/MWCNTs) as anode for the immobilization of alcohol dehydrogenase. This material had a BET surface area of 1,166 m2 g-1, while the electrochemical evaluation in half-cell tests demonstrated the superior activity for alcohol oxidation than PC and MWCNTs alone. Nonetheless, full-cell tests were not presented.

      1.4.5 Flexible Bioelectrodes for Flexible BFCs

      It is worth mentioning that in all of these works, bending tests were not presented, nor in other revised works [129]. Thus, the development of fully functional bendable and flexible biofuel cells is still a hot topic area.

      1.5.1 Enzyme-Electrode Electron Transfer

      For the enzymatic redox reactions to be useful in systems containing bioelectrodes (such as fuel cells), the electrode must replace one of the half reactions of the enzyme in its natural environment. This is, the electrode must function as the final electron acceptor or donor, depending on whether it is working as a bioanode or biocathode, respectively. For this to occur, the electrons must travel between the enzyme active sites and the electrode surface in a process termed “electron transfer”. In the context of enzymatic electrodes, this term is employed more loosely than in pure electrochemical sciences, in that the process can involve non-electrochemical charge transport steps, for instance, the diffusion of a mediator (see below) to/from the electrode surface.

      Mediated electrodes incorporate a molecule that acts as an electron carrier between the enzyme’s active site and the electrode surface. After reacting with their substrate, enzymes change their oxidation state. In their native environment, the enzyme then reacts with another molecule (e.g. O2 for GOx) and returns to their original oxidation state. The mediators must be able to substitute these natural electron donors/acceptors and readily exchange electrons with the enzyme cofactor. To this end, they must possess the adequate size and charge to be able to access the active site, which can be insulated by oligopeptide and saccharide shells. Furthermore, mediators must also be capable of undergoing a reversible reaction on the electrode surface.

      A variety of transition metal (e.g. Os, Fe, Ru, Co) coordination compounds have been employed to this end [16, 56]. Among the ligants used are derivatives of cyclopentadiene [7, 44, 51, 63–65], bipyridine (bpy) [50, 56, 66] and phenanthroline [130]. Careful modification of these ligands with electron donor or withdrawing groups allow for a fine tuning of the redox potential of the mediator. In general, electron donating substituents will increase the electron density of the


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