TY - JOUR A1 - Röhlen, Desiree A1 - Pilas, Johanna A1 - Schöning, Michael Josef A1 - Selmer, Thorsten T1 - Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid JF - Applied Biochemistry and Biotechnology N2 - Three amperometric biosensors have been developed for the detection of L-malic acid, fumaric acid, and L -aspartic acid, all based on the combination of a malate-specific dehydrogenase (MDH, EC 1.1.1.37) and diaphorase (DIA, EC 1.8.1.4). The stepwise expansion of the malate platform with the enzymes fumarate hydratase (FH, EC 4.2.1.2) and aspartate ammonia-lyase (ASPA, EC 4.3.1.1) resulted in multi-enzyme reaction cascades and, thus, augmentation of the substrate spectrum of the sensors. Electrochemical measurements were carried out in presence of the cofactor β-nicotinamide adenine dinucleotide (NAD+) and the redox mediator hexacyanoferrate (III) (HCFIII). The amperometric detection is mediated by oxidation of hexacyanoferrate (II) (HCFII) at an applied potential of + 0.3 V vs. Ag/AgCl. For each biosensor, optimum working conditions were defined by adjustment of cofactor concentrations, buffer pH, and immobilization procedure. Under these improved conditions, amperometric responses were linear up to 3.0 mM for L-malate and fumarate, respectively, with a corresponding sensitivity of 0.7 μA mM−1 (L-malate biosensor) and 0.4 μA mM−1 (fumarate biosensor). The L-aspartate detection system displayed a linear range of 1.0–10.0 mM with a sensitivity of 0.09 μA mM−1. The sensor characteristics suggest that the developed platform provides a promising method for the detection and differentiation of the three substrates. Y1 - 2017 U6 - https://doi.org/10.1007/s12010-017-2578-1 SN - 1559-0291 VL - 183 SP - 566 EP - 581 PB - Springer CY - Berlin ER - TY - JOUR A1 - Pilas, Johanna A1 - Yazici, Yasemen A1 - Selmer, Thorsten A1 - Keusgen, Michael A1 - Schöning, Michael Josef T1 - Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate JF - Electrochimica Acta N2 - The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided. KW - Simultaneous determination KW - Enzymatic biosensor KW - Diaphorase KW - Dehydrogenase Y1 - 2017 U6 - https://doi.org/10.1016/j.electacta.2017.07.119 SN - 0013-4686 VL - 251 SP - 256 EP - 262 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Albanna, Walid A1 - Lueke, Jan Niklas A1 - Sjapic, Volha A1 - Kotliar, Konstantin A1 - Hescheler, Jürgen A1 - Clusmann, Hans A1 - Sjapic, Sergej A1 - Alpdogan, Serdan A1 - Schneider, Toni A1 - Schubert, Gerrit Alexander A1 - Neumaier, Felix T1 - Electroretinographic Assessment of Inner Retinal Signaling in the Isolated and Superfused Murine Retina JF - Current Eye Research Y1 - 2017 U6 - https://doi.org/10.1080/02713683.2017.1339807 SN - 1460-2202 IS - Article in press SP - 1 EP - 9 PB - Taylor & Francis CY - London ER - TY - CHAP A1 - Breuer, Lars A1 - Guthmann, Eric A1 - Schöning, Michael Josef A1 - Thoelen, Ronald A1 - Wagner, Torsten T1 - Light-Stimulated Hydrogels with Incorporated Graphene Oxide as Actuator Material for Flow Control in Microfluidic Applications T2 - Proceedings Eurosensors 2017 Conference, Paris, France, 3–6 September 2017 Y1 - 2017 U6 - https://doi.org/10.3390/proceedings1040524 SP - 1 EP - 4 ER - TY - JOUR A1 - Kotliar, Konstantin A1 - Hauser, Christine A1 - Ortner, Marion A1 - Muggenthaler, Claudia A1 - Diehl-Schmid, Janine A1 - Angermann, Susanne A1 - Hapfelmeier, Alexander A1 - Schmaderer, Christoph A1 - Grimmer, Timo T1 - Altered neurovascular coupling as measured by optical imaging: a biomarker for Alzheimer’s disease JF - Scientific Reports Y1 - 2017 U6 - https://doi.org/10.1038/s41598-017-13349-5 SN - 2045-2322 N1 - Article 12906 VL - 7 IS - 1 SP - 1 EP - 11 PB - Springer Nature CY - Cham ER - 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 - https://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 - Garibaldi, F. A1 - Beging, Stefan A1 - Canese, R. A1 - Carpinelli, G. A1 - Clinthorne, N. A1 - Colilli, S. A1 - Cosentino, L. A1 - Finocchiaro, P. A1 - Giuliani, F. A1 - Gricia, M. A1 - Lucentini, M. A1 - Majewski, S. A1 - Monno, E. A1 - Musico, P. A1 - Santavenere, F. A1 - Tödter, J. A1 - Wegener, Hans-Peter A1 - Ziemons, Karl T1 - A novel TOF-PET MRI detector for diagnosis and follow up of the prostate cancer JF - European Physical Journal Plus Y1 - 2017 U6 - https://doi.org/10.1140/epjp/i2017-11662-x SN - 2190-5444 VL - 132 IS - 9 PB - Springer CY - Berlin ER - TY - JOUR A1 - Müller, Wolfram A1 - Jung, Alexander A1 - Ahammer, Helmut T1 - Advantages and problems of nonlinear methods applied to analyze physiological time signals: human balance control as an example JF - Scientific Reports Y1 - 2017 SN - 2045-2322 U6 - https://doi.org/10.1038/s41598-017-02665-5 VL - 7 IS - Article number 2464 SP - 1 EP - 11 PB - Springer Nature CY - Cham ER - TY - JOUR A1 - Zange, Jochen A1 - Schopen, Kathrin A1 - Albracht, Kirsten A1 - Gerlach, Darius A. A1 - Frings-Meuthen, Petra A1 - Maffiuletti, Nicola A. A1 - Bloch, Wilhelm A1 - Rittweger, Jörn T1 - Using the Hephaistos orthotic device to study countermeasure effectiveness of neuromuscular electrical stimulation and dietary lupin protein supplementation, a randomised controlled trial JF - Plos one Y1 - 2017 U6 - https://doi.org/10.1371/journal.pone.0171562 VL - 12 IS - 2 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 - https://doi.org/10.1016/j.jbiotec.2017.07.020 SN - 0168-1656 VL - 258 SP - 41 EP - 50 PB - Elsevier CY - Amsterdam ER -