Biosurfactant functionalized single-walled carbon nanotubes to promote laccase bioelectrocatalysis

Tominaga, Masato; Sasaki, Aiko; Tsushida, Masayuki; Togami, Makoto

doi:10.1039/c6nj02287a

Cited by 7 publications

(4 citation statements)

References 48 publications

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“…The hydrophobic interactions between electrode and substrate-binding pocket was also exploited for SW-CNTs modified with a steroid biosurfactant bearing a large, rigid, and planar hydrophobic moiety. , This allowed very fast heterogeneous electron transfer rates between T1 Cu site and SW-CNTs (3000 s –1 ). Hydrophobic polymers were also able to act as a conductive wire approached to the T1 via π–π stacking. , …”

Section: Enzymatic O2 Reductionmentioning

confidence: 99%

O₂Reduction in Enzymatic Biofuel Cells

2017

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Catalytic four-electron reduction of O to water is one of the most extensively studied electrochemical reactions due to O exceptional availability and high O/HO 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 O 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/O EBFC, with a glucose oxidizing anode and a O 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 electrochemistry to understand these enzymes and how they behave once connected at electrodes are described. Progresses realized in the development of efficient biocathodes for O reduction relying both on direct and mediated electron transfer mechanism are then discussed. Some implementations in EBFCs are finally presented.

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Section: Enzymatic O2 Reductionmentioning

confidence: 99%

O₂Reduction in Enzymatic Biofuel Cells

2017

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“…Aer injecting O 2 gas, the cathodic catalytic current from the direct electron transfer reaction of Lac had a high positive potential of around 0.6 V (vs. Ag/AgCl/saturated KCl), which was in good agreement with our previous results for a single-walled carbon nanotube-modied electrode. 33,37 This result means that the Lac immobilized SC/MWCNT/CNF sheet has potential for use as a cathode in an enzymatic biofuel cell.…”

Section: Lac-modied and Fad-gdh-modied Mwcnt/cnf Sheetsmentioning

confidence: 93%

“…(Enzyme Commission number EC 1.10.3.2) was obtained from Amano Enzyme (Nagoya, Japan) and puried according to an established method. 33 The purity of Lac was conrmed by SDS-PAGE, which gave a single band at approximately 63 kDa. 30 The Lac concentration was determined from its molar absorption coefficient of 5700 (mol dm À3 ) À1 cm À1 at 614 nm.…”

Section: Methodsmentioning

confidence: 99%

Cellulose nanofiber-based electrode as a component of an enzyme-catalyzed biofuel cell

et al. 2020

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“…SC molecules act as an insulating barrier and inhibit fast electron transfer when the SC molecules form a multilayer on the HOPG interface. The electron transfer rate constant (k˚') for Lac at the SC-modified HOPG was evaluated by previously reported methods [25][26][27]. Figure 7a shows the catalytic current steady-state voltammograms and their fittings with simulated plots (Supplementary Material).…”

Section: = (−2 )mentioning

confidence: 99%

Cholate Adsorption Behavior at Carbon Electrode Interface and Its Promotional Effect in Laccase Direct Bioelectrocatalysis

Tominaga¹,

Tsutsui²,

Takatori³

2018

Colloids and Interfaces

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Fast electron transfer between laccase (Lac) and single-walled carbon nanotubes (SWCNTs) can be achieved at a cholate-modified SWCNT interface. Furthermore, the catalytic reduction of O 2 starts at a high potential, close to the equilibrium redox potential of the O 2 /H 2 O couple. A sodium cholate (SC)-modified electrode interface provides suitable conditions for Lac direct bioelectrocatalysis. In the present study, the SC promotional effect in Lac direct bioelectrocatalysis was investigated using various types of electrode materials. The fully hydrophilic surface of indium tin oxide and an Au electrode surface did not show a SC promotional effect, because SC did not bind to these surfaces. A carbon surface with a large number of defects was unsuitable for SC binding because of hydrophilic functional groups at the defect sites. Carbon surfaces with few defects, for example, basal-plane highly oriented pyrolytic graphite (HOPG), gave a SC promotional effect.

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Biosurfactant functionalized single-walled carbon nanotubes to promote laccase bioelectrocatalysis

Abstract: The type and coverage of biosurfactants adsorbed on single-walled carbon nanotubes strongly influence the direct electron transfer reaction of laccase.

Cited by 7 publications

References 48 publications

O₂Reduction in Enzymatic Biofuel Cells

O₂Reduction in Enzymatic Biofuel Cells

Cellulose nanofiber-based electrode as a component of an enzyme-catalyzed biofuel cell

Cholate Adsorption Behavior at Carbon Electrode Interface and Its Promotional Effect in Laccase Direct Bioelectrocatalysis

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Biosurfactant functionalized single-walled carbon nanotubes to promote laccase bioelectrocatalysis

Abstract: The type and coverage of biosurfactants adsorbed on single-walled carbon nanotubes strongly influence the direct electron transfer reaction of laccase.

Cited by 7 publications

References 48 publications

O2Reduction in Enzymatic Biofuel Cells

O2Reduction in Enzymatic Biofuel Cells

Cellulose nanofiber-based electrode as a component of an enzyme-catalyzed biofuel cell

Cholate Adsorption Behavior at Carbon Electrode Interface and Its Promotional Effect in Laccase Direct Bioelectrocatalysis

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Product

Resources

About

O₂Reduction in Enzymatic Biofuel Cells

O₂Reduction in Enzymatic Biofuel Cells