@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}
}
@article{WagnerWernerMiyamotoetal.2009,
  author    = {Wagner, Torsten and Werner, Frederik and Miyamoto, K. and Sch{\"o}ning, Michael Josef and Yoshinobu, T.},
  title     = {A high-density multi-point LAPS set-up using a VCSEL array and FPGA control},
  series = {Procedia Chemistry. 1 (2009), H. 1},
  journal   = {Procedia Chemistry. 1 (2009), H. 1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {1876-6196},
  pages     = {1483 -- 1486},
  year      = {2009},
  language  = {en}
}
@article{WagnerWernerMiyamotoetal.2011,
  author    = {Wagner, Torsten and Werner, Frederik and Miyamoto, Ko-Ichiro and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo},
  title     = {A high-density multi-point LAPS set-up using a VCSEL array and FPGA control},
  series = {Sensors and Actuators B: Chemical. 154 (2011), H. 2},
  journal   = {Sensors and Actuators B: Chemical. 154 (2011), H. 2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {1873-3077},
  pages     = {124 -- 128},
  year      = {2011},
  language  = {en}
}
@article{WagnerSchoeningOttoetal.2004,
  author    = {Wagner, Torsten and Sch{\"o}ning, Michael Josef and Otto, R. and Yoshinobu, T.},
  title     = {A handheld 16 channel pen-type LAPS as a platform for (bio-)electrochemical sensing},
  series = {Biomedizinische Technik. 49 (2004), H. 2},
  journal   = {Biomedizinische Technik. 49 (2004), H. 2},
  isbn      = {0932-4666},
  pages     = {996 -- 997},
  year      = {2004},
  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}
}