@article{SarauliXuDietzeletal.2014,
  author    = {Sarauli, David and Xu, Chenggang and Dietzel, Birgit and Schulz, Burkhard and Lisdat, Fred},
  title     = {A multilayered sulfonated polyaniline network with entrapped pyrroloquinoline quinone-dependent glucose dehydrogenase: tunable direct bioelectrocatalysis},
  series = {Journal of materials chemistry : B, Materials for biology and medicine},
  volume    = {2},
  journal   = {Journal of materials chemistry : B, Materials for biology and medicine},
  number    = {21},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2050-750X},
  doi       = {10.1039/c4tb00336e},
  pages     = {3196 -- 3203},
  year      = {2014},
  abstract  = {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 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.},
  language  = {en}
}
@misc{SarauliXuDietzeletal.2014,
  author    = {Sarauli, David and Xu, Chenggang and Dietzel, Birgit and Schulz, Burkhard and Lisdat, Fred},
  title     = {A multilayered sulfonated polyaniline network with entrapped pyrroloquinoline quinone-dependent glucose dehydrogenase},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-98744},
  year      = {2014},
  abstract  = {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 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.},
  language  = {en}
}