@article{HandtkeVollandMethlingetal.2014,
  author    = {Handtke, Stefan and Volland, Sonja and Methling, Karen and Albrecht, Dirk and Becher, D{\"o}rte and Nehls, Jenny and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Liesegang, Heiko and Voigt, Birgit and Daniel, Rolf and Hecker, Michael},
  title     = {Cell physiology of the biotechnological relevant bacterium Bacillus pumilus - An omics-based approach},
  series = {Journal of Biotechnology},
  journal   = {Journal of Biotechnology},
  number    = {192(A)},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2014.08.028},
  pages     = {204 -- 214},
  year      = {2014},
  abstract  = {Members of the species Bacillus pumilus get more and more in focus of the biotechnological industry as potential new production strains. Based on exoproteome analysis, B. pumilus strain Jo2, possessing a high secretion capability, was chosen for an omics-based investigation. The proteome and metabolome of B. pumilus cells growing either in minimal or complex medium was analyzed. In total, 1542 proteins were identified in growing B. pumilus cells, among them 1182 cytosolic proteins, 297 membrane and lipoproteins and 63 secreted proteins. This accounts for about 43\% of the 3616 proteins encoded in the B. pumilus Jo2 genome sequence. By using GC-MS, IP-LC/MS and H NMR methods numerous metabolites were analyzed and assigned to reconstructed metabolic pathways. In the genome sequence a functional secretion system including the components of the Sec- and Tat-secretion machinery was found. Analysis of the exoproteome revealed secretion of about 70 proteins with predicted secretion signals. In addition, selected production-relevant genome features such as restriction modification systems and NRPS clusters of B. pumilus Jo2 are discussed.},
  language  = {en}
}
@article{WiegandDietrichHerteletal.2013,
  author    = {Wiegand, Sandra and Dietrich, Sascha and Hertel, Robert and Bongaerts, Johannes and Evers, Stefan and Volland, Sonja and Daniel, Rolf and Liesegang, Heiko},
  title     = {RNA-Seq of Bacillus licheniformis: active regulatory RNA features expressed within a productive fermentation},
  series = {BMC genomics},
  volume    = {Vol. 14},
  journal   = {BMC genomics},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1471-2164},
  pages     = {667},
  year      = {2013},
  language  = {en}
}
@article{FalkenbergRahbaFischeretal.2022,
  author    = {Falkenberg, Fabian and Rahba, Jade and Fischer, David and Bott, Michael and Bongaerts, Johannes and Siegert, Petra},
  title     = {Biochemical characterization of a novel oxidatively stable, halotolerant, and high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T},
  series = {FEBS Open Bio},
  volume    = {12},
  journal   = {FEBS Open Bio},
  number    = {10},
  publisher = {Wiley},
  address   = {Hoboken, NJ},
  issn      = {2211-5463},
  doi       = {10.1002/2211-5463.13457},
  pages     = {1729 -- 1746},
  year      = {2022},
  abstract  = {Halophilic and halotolerant microorganisms represent a promising source of salt-tolerant enzymes suitable for various biotechnological applications where high salt concentrations would otherwise limit enzymatic activity. Considering the current growing enzyme market and the need for more efficient and new biocatalysts, the present study aimed at the characterization of a high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T. The protease gene was cloned and expressed in Bacillus subtilis DB104. The recombinant protease SPAO with 269 amino acids belongs to the subfamily of high-alkaline subtilisins. The biochemical characteristics of purified SPAO were analyzed in comparison with subtilisin Carlsberg, Savinase, and BPN'. SPAO, a monomer with a molecular mass of 27.1 kDa, was active over a wide range of pH 6.0-12.0 and temperature 20-80 °C, optimally at pH 9.0-9.5 and 55 °C. The protease is highly oxidatively stable to hydrogen peroxide and retained 58\% of residual activity when incubated at 10 °C with 5\% (v/v) H2O2 for 1 h while stimulated at 1\% (v/v) H2O2. Furthermore, SPAO was very stable and active at NaCl concentrations up to 5.0 m. This study demonstrates the potential of SPAO for biotechnological applications in the future.},
  language  = {en}
}
@article{UndenBongaerts1997,
  author    = {Unden, Gottfried and Bongaerts, Johannes},
  title     = {Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors},
  series = {Biochimica et biophysica acta (BBA) - Bioenergetics},
  volume    = {Vol. 1320},
  journal   = {Biochimica et biophysica acta (BBA) - Bioenergetics},
  number    = {Iss. 3},
  issn      = {1879-2650 (E-Journal); 0005-2728 (Print)},
  pages     = {217 -- 234},
  year      = {1997},
  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{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{WackwitzBongaertsGoodmanetal.1999,
  author    = {Wackwitz, B. and Bongaerts, Johannes and Goodman, S. D. and Unden, Gottfried},
  title     = {Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significance},
  series = {Molecular and general genetics : MGG},
  volume    = {Vol. 262},
  journal   = {Molecular and general genetics : MGG},
  number    = {Iss. 4 - 5},
  issn      = {1617-4623 (E-Journal); 1617-4615 (Print)},
  pages     = {876 -- 883},
  year      = {1999},
  language  = {en}
}
@article{UndenBeckerBongaertsetal.1995,
  author    = {Unden, G. and Becker, S. and Bongaerts, Johannes and Holighaus, G. and Schirawski, J. and Six, S.},
  title     = {O2-sensing and O2-dependent gene regulation in facultatively anaerobic bacteria},
  series = {Archives of microbiology},
  volume    = {Vol. 164},
  journal   = {Archives of microbiology},
  number    = {Iss. 2},
  issn      = {1432-072X (E-Journal); 0003-9276 (Print); 0302-8933 (Print)},
  pages     = {81 -- 90},
  year      = {1995},
  language  = {en}
}
@article{TranBongaertsVladetal.1997,
  author    = {Tran, Quang Hon and Bongaerts, Johannes and Vlad, Dorina and Unden, Gottfried},
  title     = {Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications},
  series = {European journal of biochemistry},
  volume    = {Vol. 244},
  journal   = {European journal of biochemistry},
  number    = {Iss. 1},
  issn      = {0014-2956},
  pages     = {155 -- 160},
  year      = {1997},
  language  = {en}
}
@article{WiegandVoigtAlbrechtetal.2013,
  author    = {Wiegand, Sandra and Voigt, Birgit and Albrecht, Dirk and Bongaerts, Johannes and Evers, Stefan and Hecker, Michael and Daniel, Rolf and Liesegang, Heiko},
  title     = {Fermentation stage-dependent adaptations of Bacillus licheniformis during enzyme production},
  series = {Microbial Cell Factories},
  volume    = {12},
  journal   = {Microbial Cell Factories},
  publisher = {Biomed Central},
  address   = {London},
  issn      = {1475-2859},
  doi       = {10.1186/1475-2859-12-120},
  pages     = {120},
  year      = {2013},
  language  = {en}
}