Catalytic four-electron reduction of O2 to water is one of the most extensively studied electrochemical reactions due to O2 exceptional availability and high O2/H2O redox potential, which may in particular allow highly energetic reactions in fuel cells. To circumvent the use of expensive and inefficient Pt catalysts, multicopper oxidases (MCOs) have been envisioned because they provide efficient O2 reduction with almost no overpotential. MCOs have been used to elaborate enzymatic biofuel cells (EBFCs), a subclass of fuel cells in which enzymes replace the conventional catalysts. A glucose/O2 EBFC, with a glucose oxidizing anode and a O2 reducing MCO cathode, could become the in vivo source of electricity that would power sometimes in the future integrated medical devices. This review covers the challenges and advances in the electrochemistry of MCOs and their use in EBFCs with a particular emphasis on the last 6 years. First basic features of MCOs and EBFCs are presented. Clues provided by electrochemistr...

/pdf/o2-reduction-in-enzymatic-biofuel-cells-49p4w8k9ml.pdf

O2 Reduction in Enzymatic Biofuel Cells

Enzymatic degradation and detoxification of azo dye Congo red by a new laccase from Oudemansiella canarii.

https://ro.uow.edu.au/cgi/viewcontent.cgi?article=7455&context=eispapers

Direct immobilization of laccase on titania nanoparticles from crude enzyme extracts of P. ostreatus culture for micro-pollutant degradation

Carbon nanotubes (CNTs) have been widely exploited for the development of enzymatic biofuel cells with sufficient power densities in the μW to mW range for operating low-power bioelectronic devices from renewable substrates. Buckypaper is a randomly oriented self-supporting film of carbon nanotubes, resembling an electronic paper, with excellent prospects for the construction of high performance enzymatic electrodes for use in biofuel cells. Attractive properties of buckypaper materials include large specific surface areas, high electrical conductivity, flexibility, biocompatibility, scalable production and the ability for efficient electron transfer with enzymes. Buckypapers are ideal self-supporting frameworks for enzymes and guest molecules such as metals, polymers and redox molecules, permitting the development of a wide range of catalytic bioelectrode interfaces. This review summarizes recent developments and advances of buckypaper bioelectrodes as an emerging component for body-integrated energy harvesting biodevices.

/pdf/buckypaper-bioelectrodes-emerging-materials-for-implantable-2qib68tbd9.pdf

Buckypaper bioelectrodes: emerging materials for implantable and wearable biofuel cells

Design of a microbial consortium is a newly emerging field that enables researchers to extend the frontiers of biotechnology from a pure culture to mixed cultures. A microbial consortium enables microbes to use a broad range of carbon sources. It provides microbes with robustness in response to environmental stress factors. Microbes in a consortium can perform complex functions that are impossible for a single organism. With advancement of technology, it is now possible to understand microbial interaction mechanism and construct consortia. Microbial consortia can be classified in terms of their construction, modes of interaction, and functions. Here we discuss different trends in the study of microbial functions and interactions, including single-cell genomics (SCG), microfluidics, fluorescent imaging, and membrane separation. Community profile studies using polymerase chain-reaction denaturing gradient gel electrophoresis (PCR-DGGE), amplified ribosomal DNA restriction analysis (ARDRA), and terminal restriction fragment-length polymorphism (T-RFLP) are also reviewed. We also provide a few examples of their possible applications in areas of biopolymers, bioenergy, biochemicals, and bioremediation.

Biotechnological potential of microbial consortia and future perspectives.

Improving the performance of a biofuel cell cathode with laccase-containing culture supernatant from Pycnoporus sanguineus

Side chain-containing steroids are ubiquitous constituents of biological membranes that are persistent to biodegradation. Aerobic, steroid-degrading bacteria employ oxygenases for isoprenoid side chain and tetracyclic steran ring cleavage. In contrast, a Mo-containing steroid C-25 dehydrogenase (S25DH) of the dimethyl sulfoxide (DMSO) reductase family catalyzes the oxygen-independent hydroxylation of tertiary C-25 in the anaerobic, cholesterol-degrading bacterium Sterolibacterium denitrificans Its genome contains eight paralogous genes encoding active site α-subunits of putative S25DH-like proteins. The difficult enrichment of labile, oxygen-sensitive S25DH from the wild-type bacteria and the inability of its active heterologous production have largely hampered the study of S25DH-like gene products. Here we established a heterologous expression platform for the three structural genes of S25DH subunits together with an essential chaperone in the denitrifying betaproteobacterium Thauera aromatica K172. Using this system, S25DH1 and three isoenzymes (S25DH2, S25DH3, and S25DH4) were overproduced in a soluble, active form allowing a straightforward purification of nontagged αβγ complexes. All S25DHs contained molybdenum, four [4Fe-4S] clusters, one [3Fe-4S] cluster, and heme B and catalyzed the specific, water-dependent C-25 hydroxylations of various 4-en-3-one forms of phytosterols and zoosterols. Crude extracts from T. aromatica expressing genes encoding S25DH1 catalyzed the hydroxylation of vitamin D3 (VD3) to the clinically relevant 25-OH-VD3 with >95% yield at a rate 6.5-fold higher than that of wild-type bacterial extracts; the specific activity of recombinant S25DH1 was twofold higher than that of wild-type enzyme. These results demonstrate the potential application of the established expression platform for 25-OH-VD3 synthesis and pave the way for the characterization of previously genetically inaccessible S25DH-like Mo enzymes of the DMSO reductase family.IMPORTANCE Steroids are ubiquitous bioactive compounds, some of which are considered an emerging class of micropollutants. Their degradation by microorganisms is the major process of steroid elimination from the environment. While oxygenase-dependent steroid degradation in aerobes has been studied for more than 40 years, initial insights into the anoxic steroid degradation have only recently been obtained. Molybdenum-dependent steroid C25 dehydrogenases (S25DHs) have been proposed to catalyze oxygen-independent side chain hydroxylations of globally abundant zoo-, phyto-, and mycosterols; however, so far, their lability has allowed only the initial characterization of a single S25DH. Here we report on a heterologous gene expression platform that allowed for easy isolation and characterization of four highly active S25DH isoenzymes. The results obtained demonstrate the key role of S25DHs during anoxic degradation of various steroids. Moreover, the platform is valuable for the efficient enzymatic hydroxylation of vitamin D3 to its clinically relevant C-25-OH form.

/pdf/four-molybdenum-dependent-steroid-c-25-hydroxylases-57ym1idz5q.pdf

Four Molybdenum-Dependent Steroid C-25 Hydroxylases: Heterologous Overproduction, Role in Steroid Degradation, and Application for 25-Hydroxyvitamin D3 Synthesis.

Selective natural induction of laccases in Pleurotus sajor-caju, suitable for application at a biofuel cell cathode at neutral pH

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Improving the performance of a biofuel cell cathode with laccase-containing culture supernatant from Pycnoporus sanguineus

Four Molybdenum-Dependent Steroid C-25 Hydroxylases: Heterologous Overproduction, Role in Steroid Degradation, and Application for 25-Hydroxyvitamin D3 Synthesis.

Selective natural induction of laccases in Pleurotus sajor-caju, suitable for application at a biofuel cell cathode at neutral pH