TY - GEN A1 - Spricigo, Roberto A1 - Dronov, Roman A1 - Lisdat, Fred A1 - Leimkühler, Silke A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - An efficient electrocatalytic biosensor for sulfite detection was developed by co-immobilizing sulfite oxidase and cytochrome c with polyaniline sulfonic acid in a layer-by-layer assembly. QCM, UV-Vis spectroscopy and cyclic voltammetry revealed increasing loading of electrochemically active protein with the formation of multilayers. The sensor operates reagentless at low working potential. A catalytic oxidation current was detected in the presence of sulfite at the modified gold electrode, polarized at +0.1 V ( vs. Ag/AgCl 1 M KCl). The stability of the biosensor performance was characterized and optimized. A 17-bilayer electrode has a linear range between 1 and 60 mu M sulfite with a sensitivity of 2.19 mA M-1 sulfite and a response time of 2 min. The electrode retained a stable response for 3 days with a serial reproducibility of 3.8% and lost 20% of sensitivity after 5 days of operation. It is possible to store the sensor in a dry state for more than 2 months. The multilayer electrode was used for determination of sulfite in unspiked and spiked samples of red and white wine. The recovery and the specificity of the signals were evaluated for each sample. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 945 KW - bioelectrocatalysis KW - sulfite KW - sulfite oxidase KW - cytochrome c KW - multilayer Y1 - 2020 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-431176 SN - 1866-8372 IS - 945 SP - 225 EP - 233 ER - TY - JOUR A1 - Kröning, Steffen A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Lisdat, Fred T1 - Myoglobin-Clay Electrode for Nitric Oxide (NO) Detection in Solution Y1 - 2004 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Lisdat, Fred A1 - Wollenberger, Ursula T1 - Application of electrically contacted enzymes for biosensors Y1 - 2005 SN - 3-527- 30690-0 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Lei, Chenghong A1 - Jin, Wen A1 - Ge, Bixia A1 - Lehmann, Claudia A1 - Lisdat, Fred A1 - Fridman, Vadim T1 - Bioelectrocatalysis by redox enzymes at modified electrodes Y1 - 2002 UR - www.elsevier.nl/inca/publications/6/0/1/3/4/7/index.htt ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Lisdat, Fred A1 - Scheller, Frieder W. T1 - Enzymatic substrade recycling electrodes Y1 - 1997 ER - TY - JOUR A1 - Szeponik, Jan A1 - Möller, B. A1 - Pfeiffer, Dorothea A1 - Lisdat, Fred A1 - Wollenberger, Ursula A1 - Makower, Alexander A1 - Scheller, Frieder W. T1 - Ultrasensitive bienzyme sensor for adrenaline Y1 - 1997 ER - TY - JOUR A1 - Lisdat, Fred A1 - Wollenberger, Ursula A1 - Paeschke, Manfred A1 - Scheller, Frieder W. T1 - Sensitive catecholamine measurement using a monoenzymatic recycling system Y1 - 1998 ER - TY - JOUR A1 - Spricigo, Roberto A1 - Dronov, Roman A1 - Lisdat, Fred A1 - Leimkühler, Silke A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer N2 - An efficient electrocatalytic biosensor for sulfite detection was developed by co-immobilizing sulfite oxidase and cytochrome c with polyaniline sulfonic acid in a layer-by-layer assembly. QCM, UV-Vis spectroscopy and cyclic voltammetry revealed increasing loading of electrochemically active protein with the formation of multilayers. The sensor operates reagentless at low working potential. A catalytic oxidation current was detected in the presence of sulfite at the modified gold electrode, polarized at +0.1 V ( vs. Ag/AgCl 1 M KCl). The stability of the biosensor performance was characterized and optimized. A 17-bilayer electrode has a linear range between 1 and 60 mu M sulfite with a sensitivity of 2.19 mA M-1 sulfite and a response time of 2 min. The electrode retained a stable response for 3 days with a serial reproducibility of 3.8% and lost 20% of sensitivity after 5 days of operation. It is possible to store the sensor in a dry state for more than 2 months. The multilayer electrode was used for determination of sulfite in unspiked and spiked samples of red and white wine. The recovery and the specificity of the signals were evaluated for each sample. Y1 - 2009 UR - http://www.springerlink.com/content/100417 U6 - https://doi.org/10.1007/s00216-008-2432-y SN - 1618-2642 ER - TY - JOUR A1 - Lisdat, Fred A1 - Ho, Wah O. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Richter, Torsten A1 - Bilitewski, Ursula T1 - Recycling systems based on screen-printed electrodes Y1 - 1998 ER - TY - JOUR A1 - Kepplinger, Christian A1 - Lisdat, Fred A1 - Wollenberger, Ursula T1 - Cytochrome c/polyelectrolyte multilayers investigated by E-QCM-D - effect of temperature on the assembly structure JF - Langmuir N2 - Protein multilayers, consisting of cytochrome c (cyt c) and poly(aniline sulfonic acid) (PASA), are investigated by electrochemical quartz crystal microbalance with dissipation monitoring (E-QCM-D). This technique reveals that a four-bilayer assembly has rather rigid properties. A thickness of 16.3 +/- 0.8 nm is calculated with the Sauerbrey equation and is found to be in good agreement with a viscoelastic model. The electroactive amount of cyt c is estimated by the deposited mass under the assumption of 50% coupled water. Temperature-induced stabilization of the multilayer assembly has been investigated in the temperature range between 30 and 45 degrees C. The treatment results in a loss of material and a contraction of the film. The electroactive amount of cyt c also decreases during heating and remains constant after the cooling period. The contraction of the film is accompanied by the enhanced stability of the assembly. In addition, it is found that cyt c and PASA can be assembled at higher temperatures, resulting in the formation of multilayer systems with less dissipation. Y1 - 2011 U6 - https://doi.org/10.1021/la200860p SN - 0743-7463 VL - 27 IS - 13 SP - 8309 EP - 8315 PB - American Chemical Society CY - Washington ER - TY - JOUR A1 - Sarauli, David A1 - Riedel, Marc A1 - Wettstein, Christoph A1 - Hahn, Robert A1 - Stiba, Konstanze A1 - Wollenberger, Ursula A1 - Leimkühler, Silke A1 - Schmuki, Patrik A1 - Lisdat, Fred T1 - Semimetallic TiO2 nanotubes new interfaces for bioelectrochemical enzymatic catalysis JF - Journal of materials chemistry N2 - Different self-organized TiO2 nanotube structures are shown to represent new interfaces for the achievement of bioelectrochemical enzymatic catalysis involving redox proteins and enzymes without further surface modification or the presence of mediators. Y1 - 2012 U6 - https://doi.org/10.1039/c2jm16427b SN - 0959-9428 VL - 22 IS - 11 SP - 4615 EP - 4618 PB - Royal Society of Chemistry CY - Cambridge ER - TY - JOUR A1 - Wettstein, Christoph A1 - Kano, Kenji A1 - Schaefer, Daniel A1 - Wollenberger, Ursula A1 - Lisdat, Fred T1 - Interaction of Flavin-Dependent Fructose Dehydrogenase with Cytochrome c as Basis for the Construction of Biomacromolecular Architectures on Electrodes JF - Analytical chemistry N2 - The creation of electron transfer (ET) chains based on the defined arrangement of enzymes and redox proteins on electrode surfaces represents an interesting approach within the field of bioelectrocatalysis. In this study, we investigated the ET reaction of the flavin-dependent enzyme fructose dehydrogenase (FDH) with the redox protein cytochrome c (cyt c). Two different pH optima were found for the reaction in acidic and neutral solutions. When cyt c was adsorbed on an electrode surface while the enzyme remained in solution, ET proceeded efficiently in media of neutral pH. Interprotein ET was also observed in acidic media; however, it appeared to be less efficient. These findings suggest that two different ET pathways between the enzyme and cyt c may occur. Moreover, cyt c and FDH were immobilized in multiple layers on an electrode surface by means of another biomacromolecule: DNA (double stranded) using the layer -by -layer technique. The biprotein multilayer architecture showed a catalytic response in dependence on the fructose concentration, indicating that the ET reaction between both proteins is feasible even in the immobilized state. The electrode showed a defined response to fructose and a good storage stability. Our results contribute to the better understanding of the ET reaction between FDH and cyt c and provide the basis for the creation of all-biomolecule based fructose sensors the sensitivity of which can be controlled by the layer preparation. Y1 - 2016 U6 - https://doi.org/10.1021/acs.analchem.6b00815 SN - 0003-2700 SN - 1520-6882 VL - 88 SP - 6382 EP - 6389 PB - American Chemical Society CY - Washington ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Warsinke, Axel A1 - Lisdat, Fred T1 - Research and development in biosensors Y1 - 2001 ER - TY - JOUR A1 - Fridman, Vadim A1 - Wollenberger, Ursula A1 - Bogdanovskaya, V. A. A1 - Lisdat, Fred A1 - Ruzgas, T. A1 - Lindgren, A. A1 - Gorton, Lo A1 - Scheller, Frieder W. T1 - Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator Y1 - 2000 ER - TY - JOUR A1 - Ge, Bixia A1 - Meyer, T. A1 - Schöning, M. J. A1 - Wollenberger, Ursula A1 - Lisdat, Fred T1 - Cytochrome c from chromatium vinosum on gold electrodes Y1 - 2000 ER - TY - JOUR A1 - Chen, Jian A1 - Wollenberger, Ursula A1 - Lisdat, Fred A1 - Ge, Bixia A1 - Scheller, Frieder W. T1 - Superoxide sensor based on hemin modified electrode Y1 - 2000 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Jin, Wen A1 - Ehrentreich-Förster, Eva A1 - Ge, Bixia A1 - Lisdat, Fred A1 - Büttemeyer, R. A1 - Wollenberger, Ursula T1 - Cytochrome c based superoxide sensor for in vivo application Y1 - 1999 ER - TY - JOUR A1 - Lei, Chenghong A1 - Lisdat, Fred A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Cytochrome c : Clay-modified electrode Y1 - 1999 ER -