Supramolecular Immobilization of Laccase on Carbon Nanotube Electrodes Functionalized with (Methylpyrenylaminomethyl)anthraquinone for Direct Electron Reduction of Oxygen

Bourourou, M.; Elouarzaki, Kamal; Lalaoui, Noémie; Agnès, Charles; Goff, Alan Le; Holzinger, Michael; Maaref, Abderrazak; Cosnier, Serge

doi:10.1002/chem.201301043

Cited by 79 publications

(81 citation statements)

References 22 publications

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“…Similar results have been reported for catalase covalently bound to electrospun nanofiber meshes filled with carbon nanotubes [40]. It was also reported that the conducting carbon nanotubes were able to promote direct electron transport from redox enzymes such as ascorbate oxidase, peroxidase, and Lac [38,[40][41][42][43][44][45][46]. Therefore, PpPD/Fe3O4 nanocomposite may also be suitable for enzyme immobilization, especially for redox enzymes.…”

Section: Removal Of Rb-19supporting

confidence: 80%

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

et al. 2016

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Magnetic poly(p-phenylenediamine) (PpPD) nanocomposite was synthesized via mixing p-phenylenediamine solution and Fe 3 O 4 nanoparticles and used as a carrier for immobilized enzymes. Successful synthesis of PpPD/Fe 3 O 4 nanofiber was confirmed by transmission electron microscopy and Fourier transform infrared spectroscopy. Laccase (Lac) was immobilized on the surface of PpPD/Fe 3 O 4 nanofiber through covalent bonding for reactive blue 19 dye removal. The immobilized Lac-nanofiber conjugates could be recovered from the reaction solution using a magnet. The optimum reaction pH and temperature for the immobilized Lac were 3.5 and 65 • C, respectively. The storage, operational stability, and thermal stability of the immobilized Lac were higher than those of its free counterpart. The dye removal efficiency of immobilized Lac was about 80% in the first 1 h of incubation, while that of free Lac was about 20%. It was found that the unique electronic properties of PpPD might underlie the high dye removal efficiency of immobilized Lac. Over a period of repeated operation, the dye removal efficiency was above 90% during the first two cycles and remained at about 43% after eight cycles. Immobilized Lac on PpPD/Fe 3 O 4 nanofiber showed high stability, easy recovery, reuse capabilities, and a high removal efficiency for reactive blue 19 dye; therefore, it provides an optional tool for dye removal from wastewater.

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Section: Removal Of Rb-19supporting

confidence: 80%

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

et al. 2016

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“…[178][179][180][181][182] Following the same idea, graphite electrodes, either bare or modified by CNTs, were modified with aryl diazonium salts, [66] pyrene derivatives, [57,[183][184][185] or benzoic acid derivatives. [186] Accurate observations revealed a decrease in the hysteresis of the onset of O 2 reduction [57] related to the enzyme orientation of Sreptomyces coelicolor (Sc) LAC, which helps in the efficient bioelectrocatalysis in neutral media and in the presence of chloride.…”

Section: Multicopper Oxidases (Mcos)mentioning

confidence: 99%

“…[181] Many groups have reported LAC and BOD immobilization on CNTbased electrodes. [180,181,183,[226][227][228] Notably, Lalaoui et al electropolymerized pyrroles bearing a pyrene function on MWCNTs for LAC immobilization. [229] The electrode showed a high stability, retaining 50 % activity after one month.…”

Section: Carbon Nanomaterialsmentioning

confidence: 99%

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

et al. 2014

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Among sustainable alternatives to fossil fuel, proton exchange membrane fuel cells are promising devices that deliver electricity from hydrogen and oxygen, producing only water. The transformation of the fuel and oxidant however relies on rare‐metal catalysts. H2/O2 enzymatic biofuel cells thus emerge as sustainable biotechnological devices in which chemical catalysts are replaced by hydrogenases at the anode and multicopper oxidases at the cathode. This review discusses the recent breakthroughs and the limitations in all the components of H2/O2 biofuel cells: 1) Catalytic mechanisms involved in multicopper oxidases and hydrogenases, in addition to the new potential of enzymes from the biodiversity pool, which exhibit outstanding properties. 2) The molecular basis for oriented enzyme immobilization on the electrochemical interfaces as a prerequisite for a fast direct electron‐transfer rate. 3) The requirement for 3D networks to enhance current densities. 4) The production of H2 from biomass. 5) The history of H2/O2 biofuel cells and recent devices, which also highlights the remaining issues that will allow the use of such devices in low‐power applications.

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“…The π-π stacking effect is an effective strategy to immobilize catalysts whereby aromatic moieties are attached to the catalysts, which can then strongly adsorb onto carbon nanotubes. [36][37][38][39][40] This immobilization method via non-covalent bonding provides an easy and recyclable catalyst system. Park and coworkers reported the application of phenanthroline as a ligand to immobilize rhodium complexes within a graphene hydrogel, which demonstrated excellent catalytic activity and good recyclability with a stable regeneration rate, although the loading amount on carbon materials can be improved further.…”

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confidence: 99%

Regeneration of the NADH Cofactor by a Rhodium Complex Immobilized on Multi-Walled Carbon Nanotubes

Tan

Hickey

Milton

et al. 2014

J. Electrochem. Soc.

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The regeneration of the enzymatic cofactor nicotinamide adenine dinucleotide (NADH) by rhodium-based catalysts such as [Rh(Cp * )(bpy)Cl] + (Cp * = pentamethylcyclopentadienyl, bpy = 2,2 -bipyridine) and derivatives have previously been studied extensively in solution. In this work, we report a synthetic route of a rhodium complex with a pyrene-substituted phenanthroline ligand (pyr-Rh). The immobilization of the pyr-Rh complex was accomplished on multi-walled carbon nanotubes (MWCNTs) via π-π stacking to obtain effective and durable indirect electrochemical regeneration of NADH. Cyclic voltammetry and amperometry were used to demonstrate the electrochemical activity of the surface-confined pyr-Rh complex. The loading quantity of the pyr-Rh complex was found to be 47 ± 2 nmol/mg of MWCNTs. The reusability of the electrodes modified with the pyr-Rh complex was investigated and an average turnover frequency of 3.6 ± 0.1 s −1 over ten cycles in the presence of 2 mM nicotinamide adenine dinucleotide (NAD + ) was observed. Lastly, malate dehydrogenase (MDH), a NADH-dependent enzyme, was evaluated in the presence of the immobilized pyr-Rh complex to confirm the catalyst's capability to regenerate biologically active NADH for biocatalysis. In biological systems, the cofactor nicotinamide adenine dinucleotide (NAD + ) and its reduced form (NADH) are of significance in assisting oxidoreductase enzymes to catalyze redox reactions.1 The efficient in situ regeneration of NADH from NAD + is valuable in biocatalysis due to the stoichiometric amount required for NADHdependent enzymes along with its relatively high cost.1 It was reported that the combination of three NAD + -dependent dehydrogenases (formate dehydrogenase, formaldehyde dehydrogenase and alcohol dehydrogenase) is capable of generating methanol from CO 2 by reversing the original enzymatic reaction direction. [2][3][4][5] In this enzyme cascade, one molecule of methanol is produced at the cost of three equivalents of NADH. It is environmentally beneficial to convert CO 2 into useful biofuel by enzymatic reactions, but the high cost of stoichiometric NADH consumption makes this process impractical. Therefore, a regeneration system is necessary. Galarneau and coworkers also investigated the application of this three NADH-dependent dehydrogenases cascade and the use of the enzymatic regeneration of NADH by phosphite dehydrogenase (PTDH). 6 In comparison to enzyme systems which do not incorporate a NADH regeneration system, their polyenzymatic system had a higher activity in generating methanol from carbon dioxide.6 Practical cofactor regeneration is necessary for maintaining stable concentrations of NAD + /NADH, which provides a driving force for the desired enzymatic reactions. The reduced NADH cofactor can be regenerated enzymatically, 7-9 chemically, 10 photochemically 11-13 and electrochemically. 14,15 Two methods are commonly used when electrochemically converting NAD + to NADH: direct and indirect regeneration. In the direct regeneration of NADH, the cofactor N...

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Supramolecular Immobilization of Laccase on Carbon Nanotube Electrodes Functionalized with (Methylpyrenylaminomethyl)anthraquinone for Direct Electron Reduction of Oxygen

Cited by 79 publications

References 22 publications

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

Regeneration of the NADH Cofactor by a Rhodium Complex Immobilized on Multi-Walled Carbon Nanotubes

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Supramolecular Immobilization of Laccase on Carbon Nanotube Electrodes Functionalized with (Methylpyrenylaminomethyl)anthraquinone for Direct Electron Reduction of Oxygen

Cited by 79 publications

References 22 publications

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

Biohydrogen for a New Generation of H2/O2 Biofuel Cells: A Sustainable Energy Perspective

Regeneration of the NADH Cofactor by a Rhodium Complex Immobilized on Multi-Walled Carbon Nanotubes

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Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective