Laccase–gold nanoparticle assisted bioelectrocatalytic reduction of oxygen

Dagys, Marius; Haberska, Karolina; Shleev, Sergey; Arnebrant, Thomas; Kulys, Juozas; Ruzgas, Tautgirdas

doi:10.1016/j.elecom.2010.04.024

Cited by 58 publications

(40 citation statements)

References 28 publications

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“…Usually, in the presence of the bulkier Cl -, the access of redox mediators to the T1 site is blocked and bioelectrocatalytic responses from Lcmodified electrodes are suppressed [16]. However, as previously reported, Cl -does not suppress the bioelectrocatalytic reduction of O 2 in certain cases, e.g., for DET-based biodevices with appropriately oriented Lc on the electrode surface [26] and for MET-based bioelectrodes where the enzyme is incorporated into redox hydrogels [40]. In this study, the addition of Cl -causes a reduction in the bioelectrocatalytic current.…”

Section: Resultsmentioning

confidence: 83%

“…Denaturation (protein unfolding) of the enzymes on bare Au surface can also account for the observed effects. The bioelectrocatalytic reduction of O 2 by laccase on modified Au electrodes [24][25] including nanoparticle modified Au electrodes [26] has been described. The catalytic reduction of O 2 by laccase supported on a nanoporous gold film modified electrode has been described, however at low potentials of ca.…”

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confidence: 99%

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Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes

Salaj-Kośla

Pöller

Schuhmann

et al. 2013

Bioelectrochemistry

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The enzyme Trametes hirsuta laccase undergoes direct electron transfer at unmodified nanoporous gold electrodes, displaying a current density of 28 A/cm 2 . The response indicates that ThLc was immobilised at the surface of the nanopores in a manner which promoted direct electron transfer, in contrast to the absence of a response at unmodified polycrystalline gold electrodes. The bioelectrocatalytic activity of ThLc modified nanoporous gold electrodes was strongly dependent on the presence of halide ions. Fluoride completely inhibited the enzymatic response, whereas in the presence of 150 mM Cl -, the current was reduced to 50% of the response in the absence of Cl -. The current increased by 40% when the temperature was increased from 20°C to 37°C. The response is limited by enzymatic and/or enzyme electrode kinetics and is 30% of that observed for ThLc co-immobilised with an osmium redox polymer. Keywords: Laccase, direct electron transfer, nanoporous gold 2 IntroductionElectron transfer (ET) reactions are ubiquitous in nature. Controlling the rate of these reactions can be of significant benefit in developing biochemical systems that utilise redox proteins and enzymes and in particular, in applications that provide power for implanted or portable electronic devices. ET can be achieved directly (direct electron transfer, DET) or by the use of mediators (mediated electron transfer, MET) to shuttle electrons between the redox centre of the enzyme and the electrode. However, mediators are unselective and can also give rise to interfering effects [1][2][3]. DET-based devices offer high selectivity and sensitivity due to the absence of mediators. In addition, devices based on DET operate at potentials close to the redox potential of the enzyme, maximising the potential difference between the cathode and anode for biofuel cell applications [2]. Moreover, DET can be used to provide detailed information on the kinetics and thermodynamics of the ET process. However, the low stability of the enzyme layer together with the long distances over which ET occurs, represent major obstacles for DET based devices. In addition, the shielding mechanism of the enzymatic redox centre by the protein shell can disrupt DET [2,4]. One approach in optimizing and enabling rapid DET is to design the electrode surface with an architecture which promotes efficient rates of ET. In this way the electrode morphology ensures the most efficient orientation of the enzymatic redox centre and facilitates communication with the electroactive surface. Porous electrodes can be used to encapsulate the enzyme within a network of cavities, shortening the distance for electron transfer to the redox active site, which will promote more efficient and rapid rates of electron transfer [5]. However, the number of redox enzymes capable of interacting directly with the electrode while catalyzing the enzymatic reaction is limited, with estimates of approximately 5% of all enzymes exhibiting such a response [6].DET in enzymes was first described in 1978 fo...

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Section: Resultsmentioning

confidence: 83%

mentioning

confidence: 99%

Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes

Salaj-Kośla

Pöller

Schuhmann

et al. 2013

Bioelectrochemistry

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“…Nevertheless, under aerated conditions the proposed cross-linked laccase-CNP biocathode exhibits better performance, than, e.g. Au NP-modified laccase biocathodes [52]. There was no literature data on the practical applications of the designed biofuel cells, e.g.…”

Section: Discharge Of the Laccase Oxygen Biocathode Versus The Zn Anodementioning

confidence: 98%

Activation of laccase bioelectrocatalysis of O2 reduction to H2O by carbon nanoparticles

Jensen

Vagin

Королева

et al. 2012

Journal of Electroanalytical Chemistry

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“…The higher reduction potential of some laccases close to the thermodynamic potential for oxygen reduction enables the effective reduction reaction at cathode. Laccases were adsorbed on graphite [263,274], carbon aerogel, HOPG [183], carbon nanotubes [184,[275][276][277], nanoparticles [278][279][280], gold nanoparticles [281] to enhance electron transfer rates from laccases. Alternatively, Citation retention of the enzyme behind a membrane at electrode surface [282] and chemical derivatisation to retain laccase through hydrophobic pockets were also studied to enhance the electron transfer rates [283].…”

Section: Cathodic Reduction Reactionsmentioning

confidence: 99%

Enzymatic Electrosynthesis: An Overview on the Progress in Enzyme- Electrodes for the Production of Electricity, Fuels and Chemicals

Satyawali¹

2013

J Microbial Biochem Technol

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Recent interest in the field of biocommodities production through bioelectrochemical systems has generated interest in the enzyme catalyzed redox reactions. Enzyme catalyzed electrodes are well established as sensors and power generators. However, a paradigm shift in recent science towards the production of useful chemicals has changed the face of biofuel cells, keeping the fuels or chemicals production in the upfront. This review article comprehensively presents the progress in the field of enzyme-electrodes for the production of electricity, fuels and chemicals with an aim to represent a practical outline for understanding the use of single or multiple redox enzymes as electrocatalysts for their electron transfer onto electrodes. It also provides the state-of-the-art information regarding the different existing processes to fabricate enzyme electrodes. Successfully-achieved electroenzymatic anodic and cathodic reactions are further discussed, together with their potential applications. Particular focus was made on the novel single/multiple enzyme systems towards product synthesis and other applications. Finally, techno-economic and environmental elements for industrial processing with enzyme catalyzed bioelectrochemical system (e-BES) are anticipated, in order to provide useful strategies for further development of this technology.

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Laccase–gold nanoparticle assisted bioelectrocatalytic reduction of oxygen

Cited by 58 publications

References 28 publications

Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes

Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes

Activation of laccase bioelectrocatalysis of O2 reduction to H2O by carbon nanoparticles

Enzymatic Electrosynthesis: An Overview on the Progress in Enzyme- Electrodes for the Production of Electricity, Fuels and Chemicals

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