Untitled

Тарасевич, М. Р.; Bogdanovskaya, V. A.; Kuznetsova, L. N.

doi:10.1023/a:1016791120848

Cited by 35 publications

(24 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This information could provide indirect information on the electron transfer property of laccase [22,27,28,54]. Figure 3 (solid lines) compares cyclic voltammograms (CVs) obtained for the reduction of oxygen at different electrodes in 0.10 M phosphate buffer (pH 6.0).…”

Section: Direct Electron Transfer Of Laccase and Bod At The Mwnt Elecmentioning

confidence: 99%

Direct Electrochemistry of Multi-Copper Oxidases at Carbon Nanotubes Noncovalently Functionalized with Cellulose Derivatives

Zheng

et al. 2006

Electroanalysis

122

View full text Add to dashboard Cite

This study describes the direct electron transfer of multi-copper oxidases, i.e., laccase (from Trametes versicolor) and bilirubin oxidase (BOD, from Myrothecium verrucaria) at multiwalled carbon nanotubes (MWNTs) noncovalently functionalized with biopolymers of cellulose derivatives, i.e., hydroxyethyl cellulose (HEC), methyl cellulose (MC), and carboxymethyl cellulose (CMC). The functionalization of the MWNTs with the cellulose derivatives is found to substantially solubilize the MWNTs into aqueous media and to avoid their aggregation on electrode surface. Under anaerobic conditions, the redox properties of laccase and BOD are difficult to be defined with cyclic voltammetry at either laccase/MWNT-modified or BOD/MWNT-modified electrodes. The direct electron transfer properties of laccase and BOD are thus studied in terms of the bioelectrocatalytic activities of the laccase/MWNT-modified and BOD/MWNT-modified electrodes toward the reduction of oxygen and found to be facilitated at the functionalized MWNTs. The possible application of the laccase-catalyzed O 2 reduction at the laccase/MWNT-modified electrode is illustrated by constructing a CNT-based ascorbate/O 2 biofuel cell with the MWNT-modified electrode as the anode for the oxidation of ascorbate biofuel.

show abstract

Section: Direct Electron Transfer Of Laccase and Bod At The Mwnt Elecmentioning

confidence: 99%

Direct Electrochemistry of Multi-Copper Oxidases at Carbon Nanotubes Noncovalently Functionalized with Cellulose Derivatives

Zheng

et al. 2006

Electroanalysis

122

View full text Add to dashboard Cite

show abstract

“…The characteristics of the electroreduction of oxygen at laccase modified graphite/carbon electrodes depend on the origin and also on the amount of enzyme on the electrode surface [27,29,138]. Laccases from different sources (from Rhus vernicifera and Trametes hirsuta) catalyze the heterogeneous electroreduction of oxygen in very different potential regions.…”

Section: Laccasementioning

confidence: 99%

“…Under aerobic conditions a clear catalytic wave was shown commencing close to the potential of the T1 site. A mechanism for the bioelectrocatalytic reduction of oxygen by laccase adsorbed on carbon electrode materials has been proposed by Tarasevich et al [29]. At potentials close to the steady-state potential, the rate-determining step is proposed to be a concerted transfer of two electrons to the oxygen molecule.…”

Section: Laccasementioning

confidence: 99%

Direct Electron Transfer Between Ligninolytic Redox Enzymes and Electrodes

et al. 2004

View full text Add to dashboard Cite

The electrochemistry of the ligninolytic redox enzymes, which include lignin peroxidase, manganese peroxidase and laccase and possibly also cellobiose dehydrogenase, is reviewed and discussed in conjunction with their basic biochemical characteristics. It is shown that long-range electron transfer between these enzymes and electrodes can be established and their ability to degrade lignin through a direct electron transfer mechanism is discussed.

show abstract

“…Taking into account, BMCO inhibition by halide ions, viz. F -and Cl -ions, NaClO 4 was usually used as base electrolyte [13,14,24,28], but other base electrolytes such as KNO 3 and Na 2 SO 4 can also be employed. In the present study, the activity dependence of native and immobilised Lc on solution ionic strength adjusted using KNO 3 was investigated.…”

Section: Investigations Of Native and Immobilised Trametes Hirsuta Lamentioning

confidence: 99%

“…For more than 30 years, Russian electrochemists have been studying O 2 bioelectroreduction by Lcs adsorbed on different electrode materials [6,7,[25][26][27][28][29]. In many cases bioelectrochemical results from the Russian school are presented as polarisation curves with positive cathodic currents and potentials expressed versus the NHE, which causes some difficulties for other scientists to compare results thus gathered with data already available.…”

Section: Introductionmentioning

confidence: 99%

Stable ‘Floating' Air Diffusion Biocathode Based on Direct Electron Transfer Reactions Between Carbon Particles and High Redox Potential Laccase

et al. 2010

View full text Add to dashboard Cite

We report on the assembly and characterisation of a high potential, stable, mediator‐less and cofactor free biocathode based on a fungal laccase (Lc), adsorbed on highly dispersed carbonaceous materials. First, the stability and activity of Trametes hirsuta Lc immobilised on different carbon particles were studied and compared to the solubilised enzyme. Based on the experimental results and a literature analysis, the carbonaceous material BM‐4 was chosen to design efficient and stable biocatalysts for the production of a ‘floating' air diffusion Lc‐based biocathode. Voltammetric characteristics and operational stability of the biocathode were investigated. The current density of oxygen reduction at the motionless biocathode in a quiet, air saturated citrate buffer (100 mM, pH 4.5, 23 °C) reached values as high as 0.3 mA cm–2 already at 0.7 V versus NHE. The operational stability of the biocathode depended on the current density of the device. For example, at low current density (20 μA cm–2), the biocathode lost only 5× of its initial power after 1 month of continuous operation. However, when the device was polarised at 150 mV it lost more than 32× of its initial power in just 10 min. We also found that co‐immobilisation of Lc and peroxidase on highly dispersed carbon materials could protect the biocatalyst from rapid inactivation by hydrogen peroxide produced during electrocatalytic reactions at high‐current densities.

show abstract

Untitled

Cited by 35 publications

References 4 publications

Direct Electrochemistry of Multi-Copper Oxidases at Carbon Nanotubes Noncovalently Functionalized with Cellulose Derivatives

Direct Electrochemistry of Multi-Copper Oxidases at Carbon Nanotubes Noncovalently Functionalized with Cellulose Derivatives

Direct Electron Transfer Between Ligninolytic Redox Enzymes and Electrodes

Stable ‘Floating' Air Diffusion Biocathode Based on Direct Electron Transfer Reactions Between Carbon Particles and High Redox Potential Laccase

Contact Info

Product

Resources

About