@article{MiyamotoHayashiSakamotoetal.2017, author = {Miyamoto, Ko-ichiro and Hayashi, Kosuke and Sakamoto, Azuma and Werner, Frederik and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo}, title = {A high-Q resonance-mode measurement of EIS capacitive sensor by elimination of series resistance}, series = {Sensor and Actuators B: Chemical}, volume = {248}, journal = {Sensor and Actuators B: Chemical}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0925-4005}, doi = {10.1016/j.snb.2017.03.002}, pages = {1006 -- 1010}, year = {2017}, abstract = {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.}, language = {en} } @inproceedings{MiyamotoSutoWerneretal.2017, author = {Miyamoto, Ko-ichiro and Suto, Takeyuki and Werner, Frederik and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo}, title = {Restraining the Diffusion of Photocarriers to Improve the Spatial Resolution of the Chemical Imaging Sensor}, series = {MDPI Proceedings}, volume = {1}, booktitle = {MDPI Proceedings}, number = {4}, doi = {10.3390/proceedings1040477}, pages = {4 Seiten}, year = {2017}, language = {en} } @inproceedings{MolinnusHardtKaeveretal.2017, author = {Molinnus, Denise and Hardt, Gabriel and K{\"a}ver, Larissa and Willenberg, Holger S. and Poghossian, Arshak and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Detection of Adrenaline Based on Bioelectrocatalytical System to Support Tumor Diagnostic Technology}, series = {MDPI Proceedings}, booktitle = {MDPI Proceedings}, doi = {10.3390/proceedings1040506}, pages = {4 Seiten}, year = {2017}, language = {en} } @article{MolinnusPoghossianKeusgenetal.2017, author = {Molinnus, Denise and Poghossian, Arshak and Keusgen, Michael and Katz, Evgeny and Sch{\"o}ning, Michael Josef}, title = {Coupling of Biomolecular Logic Gates with Electronic Transducers: From Single Enzyme Logic Gates to Sense/Act/Treat Chips}, series = {Electroanalysis}, volume = {29}, journal = {Electroanalysis}, number = {8}, publisher = {Wiley}, address = {Weinheim}, issn = {1521-4109}, doi = {10.1002/elan.201700208}, pages = {1840 -- 1849}, year = {2017}, abstract = {The integration of biomolecular logic principles with electronic transducers allows designing novel digital biosensors with direct electrical output, logically triggered drug-release, and closed-loop sense/act/treat systems. This opens new opportunities for advanced personalized medicine in the context of theranostics. In the present work, we will discuss selected examples of recent developments in the field of interfacing enzyme logic gates with electrodes and semiconductor field-effect devices. Special attention is given to an enzyme OR/Reset logic gate based on a capacitive field-effect electrolyte-insulator-semiconductor sensor modified with a multi-enzyme membrane. Further examples are a digital adrenaline biosensor based on an AND logic gate with binary YES/NO output and an integrated closed-loop sense/act/treat system comprising an amperometric glucose sensor, a hydrogel actuator, and an insulin (drug) sensor.}, language = {en} } @article{MoraisGomesSilvaetal.2017, author = {Morais, Paulo V. and Gomes, Vanderley F., Jr. and Silva, Anielle C. A. and Dantas, Noelio O. and Sch{\"o}ning, Michael Josef and Siqueira, Jos{\´e} R., Jr.}, title = {Nanofilm of ZnO nanocrystals/carbon nanotubes as biocompatible layer for enzymatic biosensors in capacitive field-effect devices}, series = {Journal of Materials Science}, volume = {52}, journal = {Journal of Materials Science}, number = {20}, publisher = {Springer}, address = {Berlin}, issn = {1573-4803}, doi = {10.1007/s10853-017-1369-y}, pages = {12314 -- 12325}, year = {2017}, abstract = {The incorporation of nanomaterials that are biocompatible with different types of biological compounds has allowed the development of a new generation of biosensors applied especially in the biomedical field. In particular, the integration of film-based nanomaterials employed in field-effect devices can be interesting to develop biosensors with enhanced properties. In this paper, we studied the fabrication of sensitive nanofilms combining ZnO nanocrystals and carbon nanotubes (CNTs), prepared by means of the layer-by-layer (LbL) technique, in a capacitive electrolyte-insulator-semiconductor (EIS) structure for detecting glucose and urea. The ZnO nanocrystals were incorporated in a polymeric matrix of poly(allylamine) hydrochloride (PAH), and arranged with multi-walled CNTs in a LbL PAH-ZnO/CNTs film architecture onto EIS chips. The electrochemical characterizations were performed by capacitance-voltage and constant capacitance measurements, while the morphology of the films was characterized by atomic force microscopy. The enzymes glucose oxidase and urease were immobilized on film's surface for detection of glucose and urea, respectively. In order to obtain glucose and urea biosensors with optimized amount of sensitive films, we investigated the ideal number of bilayers for each detection system. The glucose biosensor showed better sensitivity and output signal for an LbL PAH-ZnO/CNTs nanofilm with 10 bilayers. On the other hand, the urea biosensor presented enhanced properties even for the first bilayer, exhibiting high sensitivity and output signal. The presence of the LbL PAH-ZnO/CNTs films led to biosensors with better sensitivity and enhanced response signal, demonstrating that the adequate use of nanostructured films is feasible for proof-of-concept biosensors with improved properties that may be employed for biomedical applications.}, language = {en} } @article{MuschallikMolinnusBongaertsetal.2017, author = {Muschallik, Lukas and Molinnus, Denise and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Siegert, Petra and Selmer, Thorsten}, title = {(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme}, series = {Journal of Biotechnology}, volume = {258}, journal = {Journal of Biotechnology}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0168-1656}, doi = {10.1016/j.jbiotec.2017.07.020}, pages = {41 -- 50}, year = {2017}, abstract = {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.}, language = {en} } @article{MuellerJungAhammer2017, author = {M{\"u}ller, Wolfram and Jung, Alexander and Ahammer, Helmut}, title = {Advantages and problems of nonlinear methods applied to analyze physiological time signals: human balance control as an example}, series = {Scientific Reports}, volume = {7}, journal = {Scientific Reports}, number = {Article number 2464}, publisher = {Springer Nature}, address = {Cham}, isbn = {2045-2322}, doi = {10.1038/s41598-017-02665-5}, pages = {1 -- 11}, year = {2017}, language = {en} } @article{NeuJanserKhatibietal.2017, author = {Neu, Eugen and Janser, Frank and Khatibi, Akbar A. and Orifici, Adrian C.}, title = {Fully Automated Operational Modal Analysis using multi-stage clustering}, series = {Mechanical Systems and Signal Processing}, volume = {Vol. 84, Part A}, journal = {Mechanical Systems and Signal Processing}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0888-3270}, doi = {10.1016/j.ymssp.2016.07.031}, pages = {308 -- 323}, year = {2017}, language = {en} } @inproceedings{NiemuellerNeumannHenkeetal.2017, author = {Niemueller, Tim and Neumann, Tobias and Henke, Christoph and Sch{\"o}nitz, Sebastian and Reuter, Sebastian and Ferrein, Alexander and Jeschke, Sabina and Lakemeyer, Gerhard}, title = {Improvements for a robust production in the RoboCup logistics league 2016}, series = {RoboCup 2016: Robot World Cup XX. RoboCup 2016.}, booktitle = {RoboCup 2016: Robot World Cup XX. RoboCup 2016.}, publisher = {Springer}, address = {Cham}, isbn = {978-3-319-68792-6}, doi = {10.1007/978-3-319-68792-6_49}, pages = {589 -- 600}, year = {2017}, language = {en} } @inproceedings{NiemuellerNeumannHenkeetal.2017, author = {Niemueller, Tim and Neumann, Tobias and Henke, Christoph and Sch{\"o}nitz, Sebastian and Reuter, Sebastian and Ferrein, Alexander and Jeschke, Sabina and Lakemeyer, Gerhard}, title = {International Harting Open Source Award 2016: Fawkes for the RoboCup Logistics League}, series = {RoboCup 2016: RoboCup 2016: Robot World Cup XX. RoboCup 2016}, booktitle = {RoboCup 2016: RoboCup 2016: Robot World Cup XX. RoboCup 2016}, publisher = {Springer}, address = {Cham}, isbn = {978-3-319-68792-6}, doi = {10.1007/978-3-319-68792-6_53}, pages = {634 -- 642}, year = {2017}, language = {en} }