Bioelectrocatalytic dioxygen reduction at hybrid silicate–polyallylamine film with encapsulated laccase

Szot, Katarzyna; Niedziolka, Joanna; Rogalski, Jerzy; Marken, Frank; Opałło, Marcin

doi:10.1016/j.jelechem.2007.08.018

Cited by 17 publications

(19 citation statements)

References 69 publications

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“…Among polymers, ionomers were most frequently selected for enzyme encapsulation [45,46,55,82,104,[133][134][135][136][138][139][140][141][142]144,147,[149][150][151] because the pores of this material are large enough to enable penetration by the surrounding solution, thus increasing protein stability. Also protein electrostatic interaction with charged groups of ionomer may be helpful in preserving activity.…”

Section: Immobilization Of the Enzyme On The Biocathodementioning

confidence: 99%

“…Inorganic polymer, namely, sol-gel processed silicate films, were used for laccase or bilirubin oxidase immobilization [96,139,[169][170][171][172][173][174][175][176]. This is not surprising, because in the early 1990s it was found that encapsulation of enzyme in this material does not affect its activity [177,178].…”

Section: Immobilization Of the Enzyme On The Biocathodementioning

confidence: 99%

“…In the former case this mediator was found to be superior to other water-soluble mediators in terms of current density [56]. The catalytic effect is also observed with laccase encapsulated in porous material such as dialysis membrane [195], sol-gel processed silicate [91,139,169,173,176,199], lipid cubic phases [179,180,182], and poly(N-isopropylacrylamide) gel [148] or bilirubin oxidase encapsulated in the sol-gel processed film modified with CNTs [171,172]. The pores formed by the sol-gel processed polymer (silicate) or peptide assembly--like cubic phases (Fig.…”

Section: Biocathodes Employing Mediated Electrocatalysismentioning

confidence: 99%

“…This system seems to be promising because the continuous supply of the enzyme solves the problem of its instability while microfluidic geometry allows for membraneless contact between the catholyte and the anolyte. However, for the membraneless biofuel cell working in quiet conditions, immobilization of ABTS 2À occurs [101,106,128,129,[131][132][133][134]139,143,155,160,170,175,181,184,203].…”

Section: Biocathodes Employing Mediated Electrocatalysismentioning

confidence: 99%

“…The attraction between functional groups of ionomer film and ABTS 2À [205] was explored for mediator immobilization [134,139]. The composite film consisting of ionomer-polyallylamine for ABTS 2À immobilization and sol-gel processed silicate for laccase encapsulation was proposed as biocathode material [139].…”

Section: Biocathodes Employing Mediated Electrocatalysismentioning

confidence: 99%

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Biocathodes for Dioxygen Reduction in Biofuel Cells

Bilewicz

Opałło

2010

Fuel Cell Science

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Section: Immobilization Of the Enzyme On The Biocathodementioning

confidence: 99%

Section: Immobilization Of the Enzyme On The Biocathodementioning

confidence: 99%

Section: Biocathodes Employing Mediated Electrocatalysismentioning

confidence: 99%

Section: Biocathodes Employing Mediated Electrocatalysismentioning

confidence: 99%

Section: Biocathodes Employing Mediated Electrocatalysismentioning

confidence: 99%

See 3 more Smart Citations

Biocathodes for Dioxygen Reduction in Biofuel Cells

Bilewicz

Opałło

2010

Fuel Cell Science

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Enzyme catalysis in biological fuel cells

Barton

2010

Handbook of Fuel Cells

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Biocatalysts represent a compelling alternative to precious metals as catalysts for low‐temperature fuel cell power systems. Enzymatic catalysts capable of reducing oxygen or oxidizing small organic molecules can be less expensive and manufacturable, and have favorable reaction selectivity as compared to precious metals. The key barriers to realization of practical biocatalyzed fuel cells are the insufficient current, power, and lifetime achievable with current devices. Recently, significant progress has been made in addressing these issues, from the standpoint of fundamental studies of electron transfer to enzymes, mediation of enzyme‐catalyzed reactions, and immobilization of enzymes in materials that confer stability and high surface area for heterogeneous reactions. In this article, we introduce concepts in enzyme catalysis for energy applications and describe important recent progress.

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A His‐Tagged Melanocarpus albomyces Laccase and its Electrochemistry upon Immobilisation on NTA‐Modified Electrodes and in Conducting Polymer Films

2013

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The article describes the construction, immobilisation and electrochemistry of histidine tagged laccase from Melanocarpus albomyces. A facile method of functionalisation of glassy carbon electrodes with nitrilotriacetic acid (NTA) using diazonium grafting and solid state chemistry is described. NTA-modified electrodes are shown to bind laccase which reduces oxygen at neutral pH in the presence of soluble redox mediator. Laccase-modified electrodes are also prepared by enzyme immobilisation within poly(aniline)/poly(vinylsulfonate) films. The polymer is found to efficiently retain the enzyme as well as provide direct electrical contact between the electrode and the enzyme active centre. Cyclic voltammetry reveals the direct electron transfer to the enzyme is dependent on the redox state of the polymer film.

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Bioelectrocatalytic dioxygen reduction at hybrid silicate–polyallylamine film with encapsulated laccase

Cited by 17 publications

References 69 publications

Biocathodes for Dioxygen Reduction in Biofuel Cells

Biocathodes for Dioxygen Reduction in Biofuel Cells

Enzyme catalysis in biological fuel cells

A His‐Tagged Melanocarpus albomyces Laccase and its Electrochemistry upon Immobilisation on NTA‐Modified Electrodes and in Conducting Polymer Films

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