TY  - JOUR
A1  - Sarauli, David
A1  - Peters, Kristina
A1  - Xu, Chenggang
A1  - Schulz, Burkhard
A1  - Fattakhova-Rohlfing, Dina
A1  - Lisdat, Fred
T1  - 3D-Electrode architectures for enhanced direct bioelectrocatalysis of pyrroloquinoline quinone-dependent glucose dehydrogenase
JF  - ACS applied materials & interfaces
N2  - We report on the fabrication of a complex electrode architecture for efficient direct bioelectrocatalysis. In the developed procedure, the redox enzyme pyrroloquinoline quinone-dependent glucose dehydrogenase entrapped in a sulfonated polyaniline [poly(2-methoxyaniline-5-sulfonic acid)-co-aniline] was immobilized on macroporous indium tin oxide (macroITO) electrodes. The use of the 3D-conducting scaffold with a large surface area in combination with the conductive polymer enables immobilization of large amounts of enzyme and its efficient communication with the electrode, leading to enhanced direct bioelectrocatalysis. In the presence of glucose, the fabricated bioelectrodes show an exceptionally high direct bioelectrocatalytical response without any additional mediator. The catalytic current is increased more than 200-fold compared to planar ITO electrodes. Together with a high long-term stability (the current response is maintained for >90% of the initial value even after 2 weeks of storage), the transparent 3D macroITO structure with a conductive polymer represents a valuable basis for the construction of highly efficient bioelectronic units, which are useful as indicators for processes liberating glucose and allowing optical and electrochemical transduction.
KW  - 3D electrode structures
KW  - macroITO
KW  - conductive polymer
KW  - PQQ-GDH
KW  - direct bioelectrocatalysis
KW  - bioelectrochemistry
Y1  - 2014
U6  - https://doi.org/10.1021/am5046026
SN  - 1944-8244
VL  - 6
IS  - 20
SP  - 17887
EP  - 17893
PB  - American Chemical Society
CY  - Washington
ER  - 
TY  - JOUR
A1  - Sarauli, David
A1  - Xu, Chenggang
A1  - Dietzel, Birgit
A1  - Schulz, Burkhard
A1  - Lisdat, Fred
T1  - A multilayered sulfonated polyaniline network with entrapped pyrroloquinoline quinone-dependent glucose dehydrogenase: tunable direct bioelectrocatalysis
JF  - Journal of materials chemistry : B, Materials for biology and medicine
N2  - 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.
Y1  - 2014
U6  - https://doi.org/10.1039/c4tb00336e
SN  - 2050-750X
SN  - 2050-7518
VL  - 2
IS  - 21
SP  - 3196
EP  - 3203
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  -