TY - JOUR A1 - Breuer, Lars A1 - Mang, Thomas A1 - Schöning, Michael Josef A1 - Thoelen, Ronald A1 - Wagner, Torsten T1 - Investigation of the spatial resolution of a laser-based stimulation process for light-addressable hydrogels with incorporated graphene oxide by means of IR thermography JF - Sensors and Actuators A: Physical Y1 - 2017 U6 - http://dx.doi.org/10.1016/j.sna.2017.11.031 SN - 0924-4247 VL - 268 SP - 126 EP - 132 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Jildeh, Zaid B. A1 - Kirchner, Patrick A1 - Oberländer, Jan A1 - Kremers, Alexander A1 - Wagner, Torsten A1 - Wagner, Patrick H. A1 - Schöning, Michael Josef T1 - FEM-based modeling of a calorimetric gas sensor for hydrogen peroxide monitoring JF - physica status solidi a : applications and materials sciences N2 - A physically coupled finite element method (FEM) model is developed to study the response behavior of a calorimetric gas sensor. The modeled sensor serves as a monitoring device of the concentration of gaseous hydrogen peroxide (H2 O2) in a high temperature mixture stream in aseptic sterilization processes. The principle of operation of a calorimetric H2 O2 sensor is analyzed and the results of the numerical model have been validated by using previously published sensor experiments. The deviation in the results between the FEM model and experimental data are presented and discussed. Y1 - 2017 U6 - http://dx.doi.org/10.1002/pssa.201600912 SN - 1862-6319 IS - Early View PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Dantism, Shahriar A1 - Takenaga, Shoko A1 - Wagner, Torsten A1 - Wagner, Patrick A1 - Schöning, Michael Josef T1 - Differential imaging of the metabolism of bacteria and eukaryotic cells based on light-addressable potentiometric sensors JF - Electrochimica Acta N2 - A light-addressable potentiometric sensor (LAPS) is a field-effect-based potentiometric sensor with an electrolyte/insulator/semiconductor (EIS) structure, which is able to monitor analyte concentrations of (bio-)chemical species in aqueous solutions in a spatially resolved way. Therefore, it is also an appropriate tool to record 2D-chemical images of concentration variations on the sensor surface. In the present work, two differential, LAPS-based measurement principles are introduced to determine the metabolic activity of Escherichia coli (E. coli) K12 and Chinese hamster ovary (CHO) cells as test microorganisms. Hereby, we focus on i) the determination of the extracellular acidification rate (ΔpH/min) after adding glucose solutions to the cell suspensions; and ii) recording the amplitude increase of the photocurrent (Iph) related to the produced acids from E. coli K12 bacteria and CHO cells on the sensor surface by 2D-chemical imaging. For this purpose, 3D-printed multi-chamber structures were developed and mounted on the planar sensor-chip surface to define four independent compartments, enabling differential measurements with varying cell concentrations. The differential concept allows eliminating unwanted drift effects and, with the four-chamber structures, measurements on the different cell concentrations were performed simultaneously, thus reducing also the overall measuring time. Y1 - 2017 U6 - http://dx.doi.org/10.1016/j.electacta.2017.05.196 SN - 0013-4686 VL - 246 SP - 234 EP - 241 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Miyamoto, Ko-ichiro A1 - Hayashi, Kosuke A1 - Sakamoto, Azuma A1 - Werner, Frederik A1 - Wagner, Torsten A1 - Schöning, Michael Josef A1 - Yoshinobu, Tatsuo T1 - A high-Q resonance-mode measurement of EIS capacitive sensor by elimination of series resistance JF - Sensor and Actuators B: Chemical N2 - An EIS capacitive sensor is a semiconductor-based potentiometric sensor, which is sensitive to the ion concentration or pH value of the solution in contact with the sensing surface. To detect a small change in the ion concentration or pH, a small capacitance change must be detected. Recently, a resonance-mode measurement was proposed, in which an inductor was connected to the EIS capacitive sensor and the resonant frequency was correlated with the pH value. In this study, the Q factor of the resonant circuit was enhanced by canceling the internal resistance of the reference electrode and the internal resistance of the inductor coil with the help of a bypass capacitor and a negative impedance converter, respectively. 1% variation of the signal in the developed system corresponded to a pH change of 3.93 mpH, which was about 1/12 of the conventional method, suggesting a better performance in detection of a small pH change. KW - Negative impedance convertor KW - Resonance-mode measurement KW - Chemical sensor KW - EIS capacitive sensor Y1 - 2017 U6 - http://dx.doi.org/10.1016/j.snb.2017.03.002 SN - 0925-4005 VL - 248 SP - 1006 EP - 1010 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Muschallik, Lukas A1 - Molinnus, Denise A1 - Bongaerts, Johannes A1 - Pohl, Martina A1 - Wagner, Torsten A1 - Schöning, Michael Josef A1 - Siegert, Petra A1 - Selmer, Thorsten T1 - (R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme JF - Journal of Biotechnology N2 - The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33–43%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development. Y1 - 2017 U6 - http://dx.doi.org/10.1016/j.jbiotec.2017.07.020 SN - 0168-1656 VL - 258 SP - 41 EP - 50 PB - Elsevier CY - Amsterdam ER -