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  - https://doi.org/10.1016/j.snb.2017.03.002
SN  - 0925-4005
VL  - 248
SP  - 1006
EP  - 1010
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - CHAP
A1  - Walenta, Robert
A1  - Schellekens, Twan
A1  - Ferrein, Alexander
A1  - Schiffer, Stefan
T1  - A decentralised system approach for controlling AGVs with ROS
T2  - AFRICON, Proceedings
Y1  - 2017
SN  - 978-1-5386-2775-4
U6  - https://doi.org/10.1109/AFRCON.2017.8095693
SN  - 2153-0033
N1  - AFRICON <2017, 18-20 Sept., Cape Town, South Africa>
SP  - 1436
EP  - 1441
PB  - IEEE
ER  - 
TY  - CHAP
A1  - Funke, Harald
A1  - Beckmann, Nils
A1  - Abanteriba, Sylvester
T1  - A comparison of complex chemistry mechanisms for hydrogen methane blends based on the Sandia / Sydney Bluff-Body Flame HM1
T2  - Proceedings of the Eleventh Asia‐Pacific Conference on Combustion (ASPACC 2017), New South Wales, Australia, 10-14 December 2017
Y1  - 2017
SN  - 978-1-5108-5646-2
SP  - 262
EP  - 265
ER  - 
TY  - JOUR
A1  - Wilke, Thomas
T1  - [Rezension zu:] Deutsch, Kristina: Jean Marot. Un graveur d'architecture à l'époque de Louis XIV. (= Ars et Scientia; 12), Berlin; Boston 2015.
JF  - ArtHist.net
Y1  - 2017
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  -