@article{VoigtSchroeterJuergenetal.2013,
  author    = {Voigt, Birgit and Schroeter, Rebecca and J{\"u}rgen, Britta and Albrecht, Dirk and Evers, Stefan and Bongaerts, Johannes and Maurer, Karl-Heinz and Schweder, Thomas and Hecker, Michael},
  title     = {The response of Bacillus licheniformis to heat and ethanol stress and the role of the SigB regulon},
  series = {Proteomics},
  volume    = {Vol. 13},
  journal   = {Proteomics},
  number    = {Iss. 14},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1615-9861 (E-Journal); 1615-9853 (Print)},
  pages     = {2140 -- 2146},
  year      = {2013},
  language  = {en}
}
@article{SchmitzHirschBongaertsetal.2002,
  author    = {Schmitz, M. and Hirsch, E. and Bongaerts, Johannes and Takors, Ralf},
  title     = {Pulse experiments as a prerequisite for the quantification of in vivo enzyme kinetics in aromatic amino acid pathway of Eschericia coli},
  series = {Biotechnology progress},
  volume    = {Vol. 18},
  journal   = {Biotechnology progress},
  number    = {Iss. 5},
  issn      = {1520-6033 (E-Journal); 8756-7938 (Print)},
  pages     = {935 -- 941},
  year      = {2002},
  language  = {en}
}
@article{MuellerBongaertsBovenbergetal.2001,
  author    = {M{\"u}ller, Ulrike and Bongaerts, Johannes and Bovenberg, Roel and Jossek, Ralf and Kr{\"a}mer, Marco and Linnemann, J. and M{\"u}schen, S. and Ritterbecks, S. and Sprenger, G. and Wubbolts, Marcel},
  title     = {Metabolic engineering to produce fine chemicals in Escherichia coli},
  series = {Mededelingen van de Faculteit Landbouwwetenschappen, Rijksuniversiteit Gent},
  volume    = {66 (3a)},
  journal   = {Mededelingen van de Faculteit Landbouwwetenschappen, Rijksuniversiteit Gent},
  issn      = {0035-533x},
  pages     = {215 -- 217},
  year      = {2001},
  language  = {en}
}
@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{TippkoetterRoth2020,
  author    = {Tippk{\"o}tter, Nils and Roth, Jasmine},
  title     = {Purified Butanol from Lignocellulose - Solvent-Impregnated Resins for an Integrated Selective Removal},
  series = {Chemie Ingenieur Technik},
  volume    = {92},
  journal   = {Chemie Ingenieur Technik},
  number    = {11},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1522-2640},
  doi       = {10.1002/cite.202000200},
  pages     = {1741 -- 1751},
  year      = {2020},
  abstract  = {In traditional microbial biobutanol production, the solvent must be recovered during fermentation process for a sufficient space-time yield. Thermal separation is not feasible due to the boiling point of n-butanol. As an integrated and selective solid-liquid separation alternative, solvent impregnated resins (SIRs) were applied. Two polymeric resins were evaluated and an extractant screening was conducted. Vacuum application with vapor collection in fixed-bed column as bioreactor bypass was successfully implemented as butanol desorption step. In course of further increasing process economics, fermentation with renewable lignocellulosic substrates was conducted using Clostridium acetobutylicum. Utilization of SIR was shown to be a potential strategy for solvent removal from fermentation broth, while application of a bypass column allows for product removal and recovery at once.},
  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}
}
@inproceedings{HeringUlberTippkoetter2016,
  author    = {Hering, T. and Ulber, Roland and Tippk{\"o}tter, Nils},
  title     = {Development of a screening system for antimicrobial surfaces},
  series = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  booktitle = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  publisher = {DECHEMA},
  address   = {Frankfurt am Main},
  pages     = {129},
  year      = {2016},
  language  = {en}
}
@inproceedings{CapitainHeringTippkoetteretal.2016,
  author    = {Capitain, C. and Hering, T. and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Enzymatic polymerization of lignin model compounds and solubilized lignin in an aqueous ethanol extract},
  series = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  booktitle = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  publisher = {DECHEMA},
  address   = {Frankfurt am Main},
  pages     = {151 -- 152},
  year      = {2016},
  language  = {en}
}