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A multilayered sulfonated polyaniline network with entrapped pyrroloquinoline quinone-dependent glucose dehydrogenase: tunable direct bioelectrocatalysis

  • A feasible approach to construct multilayer films of sulfonated polyanilines - PMSA1 and PABMSA1 containing different ratios of aniline, 2-methoxyaniline-5-sulfonic acid (MAS) and 3-aminobenzoic acid (AB), with the entrapped redox enzyme pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH) on Au and ITO electrode surfaces, is described. The formation of layers has been followed and confirmed by electrochemical impedance spectroscopy (EIS), which demonstrates that the multilayer assembly can be achieved in a progressive and uniform manner. The gold and ITO electrodes subsequently modified with PMSA1:PQQ-GDH and PABMSA1 films are studied by cyclic voltammetry (CV) and UV-Vis spectroscopy which show a significant direct bioelectrocatalytical response to the oxidation of the substrate glucose without any additional mediator. This response correlates linearly with the number of deposited layers. Furthermore, the constructed polymer/enzyme multilayer system exhibits a rather good long-term stability, since the catalyticA feasible approach to construct multilayer films of sulfonated polyanilines - PMSA1 and PABMSA1 containing different ratios of aniline, 2-methoxyaniline-5-sulfonic acid (MAS) and 3-aminobenzoic acid (AB), with the entrapped redox enzyme pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH) on Au and ITO electrode surfaces, is described. The formation of layers has been followed and confirmed by electrochemical impedance spectroscopy (EIS), which demonstrates that the multilayer assembly can be achieved in a progressive and uniform manner. The gold and ITO electrodes subsequently modified with PMSA1:PQQ-GDH and PABMSA1 films are studied by cyclic voltammetry (CV) and UV-Vis spectroscopy which show a significant direct bioelectrocatalytical response to the oxidation of the substrate glucose without any additional mediator. This response correlates linearly with the number of deposited layers. Furthermore, the constructed polymer/enzyme multilayer system exhibits a rather good long-term stability, since the catalytic current response is maintained for more than 60% of the initial value even after two weeks of storage. This verifies that a productive interaction of the enzyme embedded in the film of substituted polyaniline can be used as a basis for the construction of bioelectronic units, which are useful as indicators for processes liberating glucose and allowing optical and electrochemical transduction.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:David Sarauli, Chenggang Xu, Birgit Dietzel, Burkhard SchulzORCiDGND, Fred LisdatORCiDGND
DOI:https://doi.org/10.1039/c4tb00336e
ISSN:2050-750X
ISSN:2050-7518
Titel des übergeordneten Werks (Englisch):Journal of materials chemistry : B, Materials for biology and medicine
Verlag:Royal Society of Chemistry
Verlagsort:Cambridge
Publikationstyp:Wissenschaftlicher Artikel
Sprache:Englisch
Jahr der Erstveröffentlichung:2014
Erscheinungsjahr:2014
Datum der Freischaltung:27.03.2017
Band:2
Ausgabe:21
Seitenanzahl:8
Erste Seite:3196
Letzte Seite:3203
Fördernde Institution:BMBF, Germany [02IS2201I]
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer Review:Referiert
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