@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{SchiffelsSelmer2015,
  author    = {Schiffels, Johannes and Selmer, Thorsten},
  title     = {A flexible toolbox to study protein-assisted metalloenzyme assembly in vitro},
  series = {Biotechnology and Bioengineering},
  volume    = {112},
  journal   = {Biotechnology and Bioengineering},
  number    = {11},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1097-0290},
  doi       = {10.1002/bit.25658},
  pages     = {2360 -- 2372},
  year      = {2015},
  language  = {en}
}
@article{SchiffelsPinkenburgScheldenetal.2013,
  author    = {Schiffels, Johannes and Pinkenburg, Olaf and Schelden, Maximilian and Aboulnaga, El-Hussiny A. A. and Baumann, Marcus and Selmer, Thorsten},
  title     = {An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from cupriavidus necator in Escherichia coli},
  series = {PLOS one. 2013},
  journal   = {PLOS one. 2013},
  publisher = {Public Library of Science},
  address   = {San Francisco, California},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0068812},
  year      = {2013},
  language  = {en}
}
@article{PilasYaziciSelmeretal.2018,
  author    = {Pilas, Johanna and Yazici, Y. and Selmer, Thorsten and Keusgen, M. and Sch{\"o}ning, Michael Josef},
  title     = {Application of a portable multi-analyte biosensor for organic acid determination in silage},
  series = {Sensors},
  volume    = {18},
  journal   = {Sensors},
  number    = {5},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s18051470},
  pages     = {12 Seiten},
  year      = {2018},
  abstract  = {Multi-analyte biosensors may offer the opportunity to perform cost-effective and rapid analysis with reduced sample volume, as compared to electrochemical biosensing of each analyte individually. This work describes the development of an enzyme-based biosensor system for multi-parametric determination of four different organic acids. The biosensor array comprises five working electrodes for simultaneous sensing of ethanol, formate, d-lactate, and l-lactate, and an integrated counter electrode. Storage stability of the biosensor was evaluated under different conditions (stored at +4 °C in buffer solution and dry at -21 °C, +4 °C, and room temperature) over a period of 140 days. After repeated and regular application, the individual sensing electrodes exhibited the best stability when stored at -21 °C. Furthermore, measurements in silage samples (maize and sugarcane silage) were conducted with the portable biosensor system. Comparison with a conventional photometric technique demonstrated successful employment for rapid monitoring of complex media.},
  language  = {en}
}
@article{WernerGroebelSchuhmacheretal.2009,
  author    = {Werner, Frederik and Groebel, Simone and Schuhmacher, K. and Spelthahn, Heiko and Wagner, Torsten and Selmer, Thorsten and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Bestimmung der metabolischen Aktivit{\"a}t von Mikroorganismen w{\"a}hrend des Biogasbildungsprozesses},
  series = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]},
  journal   = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]},
  publisher = {TUDpress},
  address   = {Dresden},
  isbn      = {978-3-941298-44-6},
  pages     = {201 -- 204},
  year      = {2009},
  language  = {de}
}
@inproceedings{KasperSchiffelsKrafftetal.2016,
  author    = {Kasper, Katharina and Schiffels, Johannes and Krafft, Simone and Kuperjans, Isabel and Elbers, Gereon and Selmer, Thorsten},
  title     = {Biogas Production on Demand Regulated by Butyric Acid Addition},
  series = {IOP Conference Series: Earth and Environmental Science. Bd. 32},
  volume    = {32},
  booktitle = {IOP Conference Series: Earth and Environmental Science. Bd. 32},
  issn      = {1755-1315},
  doi       = {10.1088/1755-1315/32/1/012009},
  pages     = {012009/1 -- 012009/4},
  year      = {2016},
  language  = {en}
}
@article{SchiffelsSelmer2019,
  author    = {Schiffels, Johannes and Selmer, Thorsten},
  title     = {Combinatorial assembly of ferredoxin-linked modules in Escherichia coli yields a testing platform for Rnf-complexes},
  series = {Biotechnology and Bioengineering},
  journal   = {Biotechnology and Bioengineering},
  number    = {accepted article},
  publisher = {Wiley},
  address   = {Weinheim},
  doi       = {10.1002/bit.27079},
  pages     = {1 -- 36},
  year      = {2019},
  language  = {en}
}
@article{PinkenburgSchiffelsSelmer2016,
  author    = {Pinkenburg, Olaf and Schiffels, Johannes and Selmer, Thorsten},
  title     = {Das CoLibry-Konzept - ein Werkzeugkasten f{\"u}r die Synthetische Biologie: Bioproduktion},
  series = {BIOspektrum},
  volume    = {22},
  journal   = {BIOspektrum},
  number    = {6},
  publisher = {Springer},
  address   = {Berlin},
  doi       = {10.1007/s12268-016-0734-8},
  pages     = {593 -- 595},
  year      = {2016},
  abstract  = {Regardless of size or destination, synthetic biology starts with com-parably small information units, which need to be combined and properly arranged in order to achieve a certain goal. This may be the de novo synthesis of individual genes from oligonucleotides, a shuffling of protein domains in order to create novel biocatalysts, the assembly of multiple enzyme encoding genes in metabolic pathway design, or strain development at the production stage. The CoLibry concept has been designed in order to close the gap between recombinant production of individual genes and genome editing.},
  language  = {de}
}
@article{WernerKrumbeSchumacheretal.2011,
  author    = {Werner, Frederik and Krumbe, Christoph and Schumacher, Katharina and Groebel, Simone and Spelthahn, Heiko and Stellberg, Michael and Wagner, Torsten and Yoshinobu, Tatsuo and Selmer, Thorsten and Keusgen, Michael and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Determination of the extracellular acidification of Escherichia coli by a light-addressable potentiometric sensor},
  series = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  journal   = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  publisher = {Wiley},
  address   = {Weinheim},
  isbn      = {1862-6319},
  pages     = {1340 -- 1344},
  year      = {2011},
  language  = {en}
}
@article{MolinnusMuschallikGonzalezetal.2018,
  author    = {Molinnus, Denise and Muschallik, Lukas and Gonzalez, Laura Osorio and Bongaerts, Johannes and Wagner, Torsten and Selmer, Thorsten and Siegert, Petra and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Development and characterization of a field-effect biosensor for the detection of acetoin},
  series = {Biosensors and Bioelectronics},
  volume    = {115},
  journal   = {Biosensors and Bioelectronics},
  publisher = {Elsevier},
  address   = {Amsterdam},
  doi       = {10.1016/j.bios.2018.05.023},
  pages     = {1 -- 6},
  year      = {2018},
  abstract  = {A capacitive electrolyte-insulator-semiconductor (EIS) field-effect biosensor for acetoin detection has been presented for the first time. The EIS sensor consists of a layer structure of Al/p-Si/SiO₂/Ta₂O₅/enzyme acetoin reductase. The enzyme, also referred to as butane-2,3-diol dehydrogenase from B. clausii DSM 8716T, has been recently characterized. The enzyme catalyzes the (R)-specific reduction of racemic acetoin to (R,R)- and meso-butane-2,3-diol, respectively. Two different enzyme immobilization strategies (cross-linking by using glutaraldehyde and adsorption) have been studied. Typical biosensor parameters such as optimal pH working range, sensitivity, hysteresis, linear concentration range and long-term stability have been examined by means of constant-capacitance (ConCap) mode measurements. Furthermore, preliminary experiments have been successfully carried out for the detection of acetoin in diluted white wine samples.},
  language  = {en}
}