@article{KueppersSteffenHellmuthetal.2014,
  author    = {K{\"u}ppers, Tobias and Steffen, Victoria and Hellmuth, Hendrik and O'Connell, Timothy and Bongaerts, Johannes and Maurer, Karl-Heinz and Wiechert, Wolfgang},
  title     = {Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer},
  series = {Microbial cell factories},
  volume    = {13},
  journal   = {Microbial cell factories},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1475-2859 (E-Journal)},
  doi       = {10.1186/1475-2859-13-46},
  pages     = {Article No. 46},
  year      = {2014},
  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}
}
@article{BongaertsEsserLorbachetal.2011,
  author    = {Bongaerts, Johannes and Esser, Simon and Lorbach, Volker and Al-Momani, L{\´o}ay and M{\"u}ller, Michael A. and Franke, Dirk and Grondal, Christoph and Kurutsch, Anja and Bujnicki, Robert and Takors, Ralf and Raeven, Leon and Wubbolts, Marcel and Bovenberg, Roel and Nieger, Martin and Sch{\"u}rmann, Melanie and Trachtmann, Natalie and Kozak, Stefan and Sprenger, Georg A. and M{\"u}ller, Michael},
  title     = {Diversity-oriented production of metabolites derived from chorismate and their use in organic synthesis},
  series = {Angewandte Chemie International Edition},
  volume    = {Vol. 50},
  journal   = {Angewandte Chemie International Edition},
  number    = {Iss. 34},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1521-3773 (E-Journal); 0570-0833 (Print); 1433-7851 (Print)},
  pages     = {7781 -- 7786},
  year      = {2011},
  language  = {en}
}
@article{DeppeBongaertsO'Connelletal.2011,
  author    = {Deppe, Veronika Maria and Bongaerts, Johannes and O'Connell, Timothy and Maurer, Karl-Heinz and Meinhardt, Friedhelm},
  title     = {Enzymatic deglycation of Amadori products in bacteria},
  series = {Applied microbiology and biotechnology},
  volume    = {Vol. 90},
  journal   = {Applied microbiology and biotechnology},
  number    = {Iss. 2},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)},
  pages     = {399 -- 406},
  year      = {2011},
  language  = {en}
}
@article{BorgmeierBongaertsMeinhardt2012,
  author    = {Borgmeier, Claudia and Bongaerts, Johannes and Meinhardt, Friedhelm},
  title     = {Genetic analysis of the Bacillus licheniformis degSU operon and the impact of regulatory mutations on protease production},
  series = {Journal of biotechnology},
  volume    = {159},
  journal   = {Journal of biotechnology},
  number    = {1-2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2012.02.011},
  pages     = {12 -- 20},
  year      = {2012},
  abstract  = {Disruption experiments targeted at the Bacillus licheniformis degSU operon and GFP-reporter analysis provided evidence for promoter activity immediately upstream of degU. pMutin mediated concomitant introduction of the degU32 allele - known to cause hypersecretion in Bacillus subtilis - resulted in a marked increase in protease activity. Application of 5-fluorouracil based counterselection through establishment of a phosphoribosyltransferase deficient Δupp strain eventually facilitated the marker-free introduction of degU32 leading to further protease enhancement achieving levels as for hypersecreting wild strains in which degU was overexpressed. Surprisingly, deletion of rapG - known to interfere with DegU DNA-binding in B. subtilis - did not enhance protease production neither in the wild type nor in the degU32 strain. The combination of degU32 and Δupp counterselection in the type strain is not only equally effective as in hypersecreting wild strains with respect to protease production but furthermore facilitates genetic strain improvement aiming at biological containment and effectiveness of biotechnological processes.},
  language  = {en}
}
@article{DeppeKlatteBongaertsetal.2011,
  author    = {Deppe, Veronika Maria and Klatte, Stephanie and Bongaerts, Johannes and Maurer, Karl-Heinz and O'Connell, Timothy and Meinhardt, Friedhelm},
  title     = {Genetic control of Amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR},
  series = {Applied and environmental microbiology},
  volume    = {Vol. 77},
  journal   = {Applied and environmental microbiology},
  number    = {No. 9},
  publisher = {American Society of Mechanical Engineers (ASME)},
  address   = {New York},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  pages     = {2839 -- 2846},
  year      = {2011},
  language  = {en}
}
@article{VoigtAlbrechtSieversetal.2015,
  author    = {Voigt, Birgit and Albrecht, Dirk and Sievers, Susanne and Becher, D{\"o}rte and Bongaerts, Johannes and Evers, Stefan and Schweder, Thomas and Maurer, Karl-Heinz and Hecker, Michael},
  title     = {High-resolution proteome maps of Bacillus licheniformis cells growing in minimal medium},
  series = {Proteomics},
  volume    = {15},
  journal   = {Proteomics},
  number    = {15},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1615-9861},
  doi       = {10.1002/pmic.201400504},
  pages     = {2629 -- 2633},
  year      = {2015},
  language  = {en}
}
@article{KraemerBongaertsBovenbergetal.2003,
  author    = {Kr{\"a}mer, Marco and Bongaerts, Johannes and Bovenberg, Roel and Kremer, Susanne and M{\"u}ller, Ulrike and Orf, Sonja and Wubbolts, Marcel and Raeven, Leon},
  title     = {Metabolic engineering for microbial production of shikimic acid},
  series = {Metabolic engineering},
  volume    = {Vol. 5},
  journal   = {Metabolic engineering},
  number    = {Iss. 4},
  issn      = {1096-7184 (E-Journal); 1096-7176 (Print)},
  pages     = {277 -- 283},
  year      = {2003},
  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{FalkenbergVossBottetal.2023,
  author    = {Falkenberg, Fabian and Voß, Leonie and Bott, Michael and Bongaerts, Johannes and Siegert, Petra},
  title     = {New robust subtilisins from halotolerant and halophilic Bacillaceae},
  series = {Applied Microbiology and Biotechnology},
  volume    = {107},
  journal   = {Applied Microbiology and Biotechnology},
  publisher = {Springer Nature},
  address   = {Berlin},
  issn      = {1432-0614},
  doi       = {10.1007/s00253-023-12553-w},
  pages     = {3939 -- 3954},
  year      = {2023},
  abstract  = {The aim of the present study was the characterisation of three true subtilisins and one phylogenetically intermediate subtilisin from halotolerant and halophilic microorganisms. Considering the currently growing enzyme market for efficient and novel biocatalysts, data mining is a promising source for novel, as yet uncharacterised enzymes, especially from halophilic or halotolerant Bacillaceae, which offer great potential to meet industrial needs. Both halophilic bacteria Pontibacillus marinus DSM 16465ᵀ and Alkalibacillus haloalkaliphilus DSM 5271ᵀ and both halotolerant bacteria Metabacillus indicus DSM 16189 and Litchfieldia alkalitelluris DSM 16976ᵀ served as a source for the four new subtilisins SPPM, SPAH, SPMI and SPLA. The protease genes were cloned and expressed in Bacillus subtilis DB104. Purification to apparent homogeneity was achieved by ethanol precipitation, desalting and ion-exchange chromatography. Enzyme activity could be observed between pH 5.0-12.0 with an optimum for SPPM, SPMI and SPLA around pH 9.0 and for SPAH at pH 10.0. The optimal temperature for SPMI and SPLA was 70 °C and for SPPM and SPAH 55 °C and 50 °C, respectively. All proteases showed high stability towards 5\% (w/v) SDS and were active even at NaCl concentrations of 5 M. The four proteases demonstrate potential for future biotechnological applications.},
  language  = {en}
}