@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{JossekBongaertsSprenger2001,
  author    = {Jossek, Ralf and Bongaerts, Johannes and Sprenger, Georg A.},
  title     = {Characterization of a new feedback-resistant 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase AroF of Escherichia coli},
  series = {FEMS microbiology letters},
  volume    = {Vol. 202},
  journal   = {FEMS microbiology letters},
  number    = {Iss. 1},
  issn      = {1574-6968},
  pages     = {145 -- 148},
  year      = {2001},
  language  = {en}
}
@article{WilmingBegemannKuhneetal.2013,
  author    = {Wilming, Anja and Begemann, Jens and Kuhne, Stefan and Regestein, Lars and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and B{\"u}chs, Jochen},
  title     = {Metabolic studies of γ-polyglutamic acid production in Bacillus licheniformis by small-scale continuous cultivations},
  series = {Biochemical engineering journal},
  volume    = {Vol. 73},
  journal   = {Biochemical engineering journal},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-295X (E-Journal); 1369-703X (Print)},
  pages     = {29 -- 37},
  year      = {2013},
  language  = {en}
}
@article{SeifarthGrosseGrossmannetal.2017,
  author    = {Seifarth, Volker and Grosse, Joachim O. and Grossmann, Matthias and Janke, Heinz Peter and Arndt, Patrick and Koch, Sabine and Epple, Matthias and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l},
  title     = {Mechanical induction of bi-directional orientation of primary porcine bladder smooth muscle cells in tubular fibrin-poly(vinylidene fluoride) scaffolds for ureteral and urethral repair using cyclic and focal balloon catheter stimulation},
  series = {Journal of Biomaterials Applications},
  volume    = {32},
  journal   = {Journal of Biomaterials Applications},
  number    = {3},
  publisher = {Sage},
  address   = {London},
  issn      = {1530-8022},
  doi       = {10.1177/0885328217723178},
  pages     = {321 -- 330},
  year      = {2017},
  language  = {en}
}
@article{SeifarthGossmannGrosseetal.2015,
  author    = {Seifarth, Volker and Goßmann, Matthias and Grosse, J. O. and Becker, C. and Heschel, I. and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l},
  title     = {Development of a Bioreactor to Culture Tissue Engineered Ureters Based on the Application of Tubular OPTIMAIX 3D Scaffolds},
  series = {Urologia Internationalis},
  volume    = {2015},
  journal   = {Urologia Internationalis},
  number    = {95},
  publisher = {Karger},
  address   = {Basel},
  issn      = {0042-1138},
  doi       = {10.1159/000368419},
  pages     = {106 -- 113},
  year      = {2015},
  language  = {en}
}
@misc{O'ConnellSiegertEversetal.2010,
  author    = {O'Connell, Timothy and Siegert, Petra and Evers, Stefan and Bongaerts, Johannes and Weber, Thomas and Maurer, Karl-Heinz and Bessler, Cornelius},
  title     = {Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft [Offenlegungsschrift]},
  publisher = {Deutsches Patentamt},
  address   = {M{\"u}nchen},
  pages     = {1 -- 34},
  year      = {2010},
  language  = {de}
}
@article{ScheeleOertelBongaertsetal.2013,
  author    = {Scheele, Sandra and Oertel, Dan and Bongaerts, Johannes and Evers, Stefan and Hellmuth, Hendrik and Maurer, Karl-Heinz and Bott, Michael and Freudl, Roland},
  title     = {Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol-xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum},
  series = {Microbial biotechnology},
  journal   = {Microbial biotechnology},
  publisher = {Wiley-Blackwell},
  address   = {Oxford},
  issn      = {1751-7915},
  pages     = {202 -- 206},
  year      = {2013},
  language  = {en}
}
@techreport{HaegerBongaertsSiegert2023,
  author    = {Haeger, Gerrit and Bongaerts, Johannes and Siegert, Petra},
  title     = {Abschlussbericht Teil II: Eingehende Darstellung Neue biobasierte Lipopeptide aus nachhaltiger Produktion (LipoPep)},
  pages     = {17Seiten},
  year      = {2023},
  language  = {de}
}
@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}
}
@article{SchroeterHoffmannVoigtetal.2014,
  author    = {Schroeter, Rebecca and Hoffmann, Tamara and Voigt, Birgit and Meyer, Hanna and Bleisteiner, Monika and Muntel, Jan and J{\"u}rgen, Britta and Albrecht, Dirk and Becher, D{\"o}rte and Lalk, Michael and Evers, Stefan and Bongaerts, Johannes and Maurer, Karl-Heinz and Putzer, Harald and Hecker, Michael and Schweder, Thomas and Bremer, Erhard},
  title     = {Stress responses of the industrial workhorse Bacillus licheniformis to osmotic challenges},
  series = {PLoS ONE},
  volume    = {8},
  journal   = {PLoS ONE},
  number    = {11},
  publisher = {PLOS},
  address   = {San Francisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0080956},
  pages     = {e80956},
  year      = {2014},
  abstract  = {The Gram-positive endospore-forming bacterium Bacillus licheniformis can be found widely in nature and it is exploited in industrial processes for the manufacturing of antibiotics, specialty chemicals, and enzymes. Both in its varied natural habitats and in industrial settings, B. licheniformis cells will be exposed to increases in the external osmolarity, conditions that trigger water efflux, impair turgor, cause the cessation of growth, and negatively affect the productivity of cell factories in biotechnological processes. We have taken here both systems-wide and targeted physiological approaches to unravel the core of the osmostress responses of B. licheniformis. Cells were suddenly subjected to an osmotic upshift of considerable magnitude (with 1 M NaCl), and their transcriptional profile was then recorded in a time-resolved fashion on a genome-wide scale. A bioinformatics cluster analysis was used to group the osmotically up-regulated genes into categories that are functionally associated with the synthesis and import of osmostress-relieving compounds (compatible solutes), the SigB-controlled general stress response, and genes whose functional annotation suggests that salt stress triggers secondary oxidative stress responses in B. licheniformis. The data set focusing on the transcriptional profile of B. licheniformis was enriched by proteomics aimed at identifying those proteins that were accumulated by the cells through increased biosynthesis in response to osmotic stress. Furthermore, these global approaches were augmented by a set of experiments that addressed the synthesis of the compatible solutes proline and glycine betaine and assessed the growth-enhancing effects of various osmoprotectants. Combined, our data provide a blueprint of the cellular adjustment processes of B. licheniformis to both sudden and sustained osmotic stress.},
  language  = {en}
}