@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{DegeringEggertPulsetal.2010,
  author    = {Degering, Christian and Eggert, Thorsten and Puls, Michael and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Jaeger, Karl-Erich},
  title     = {Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides},
  series = {Applied and environmental microbiology},
  volume    = {76},
  journal   = {Applied and environmental microbiology},
  number    = {19},
  publisher = {American Society for Microbiology},
  address   = {Washington, DC},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  doi       = {10.1128/AEM.01146-10},
  pages     = {6370 -- 6378},
  year      = {2010},
  abstract  = {Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.},
  language  = {en}
}
@article{PolenKraemerBongaertsetal.2005,
  author    = {Polen, T. and Kr{\"a}mer, Marco and Bongaerts, Johannes and Wubbolts, Marcel and Wendisch, V. F.},
  title     = {The global gene expression response of Escherichia coli to L-phenylalanine},
  series = {Journal of biotechnology},
  volume    = {Vol. 115},
  journal   = {Journal of biotechnology},
  number    = {Iss. 3},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  pages     = {221 -- 237},
  year      = {2005},
  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{GerigkMaassKreutzeretal.2002,
  author    = {Gerigk, M. and Maaß, D. and Kreutzer, A. and Sprenger, G. and Bongaerts, Johannes and Wubbolts, Marcel and Takors, Ralf},
  title     = {Enhanced pilot-scale fed-batch L-phenylalanine production with recombinant Escherichia coli by fully integrated reactive extraction},
  series = {Bioprocess and biosystems engineering},
  volume    = {Vol. 25},
  journal   = {Bioprocess and biosystems engineering},
  number    = {Iss. 1},
  issn      = {1432-0797 (E-Journal); 1615-7605 (E-Journal); 0178-515X (Print); 1615-7591 (Print)},
  pages     = {43 -- 52},
  year      = {2002},
  language  = {en}
}
@article{GerigkBujnickiGanpoNkwenkwaetal.2002,
  author    = {Gerigk, M. and Bujnicki, R. and Ganpo-Nkwenkwa, E. and Bongaerts, Johannes and Sprenger, G. and Takors, Ralf},
  title     = {Process control for enhanced L-phenylalanine production using different recombinant Escherichia coli strains},
  series = {Biotechnology and bioengineering},
  volume    = {Vol. 80},
  journal   = {Biotechnology and bioengineering},
  number    = {Iss. 7},
  issn      = {1097-0290 (E-Journal); 0006-3592 (Print)},
  pages     = {746 -- 754},
  year      = {2002},
  language  = {en}
}
@article{BongaertsBovenbergKraemeretal.2002,
  author    = {Bongaerts, Johannes and Bovenberg, Roel and Kr{\"a}mer, Marco and M{\"u}ller, Ulrike and Raeven, Leon and Wubbolts, Marcel},
  title     = {Metabolic engineering to produce fine chemicals in Escherichia coli},
  series = {Chemie - Ingenieur - Technik (CIT)},
  volume    = {Vol. 74},
  journal   = {Chemie - Ingenieur - Technik (CIT)},
  number    = {Iss. 5},
  issn      = {1522-2640 (E-Journal); 0009-286X (Print)},
  pages     = {694},
  year      = {2002},
  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{BongaertsKraemerMuelleretal.2001,
  author    = {Bongaerts, Johannes and Kr{\"a}mer, Marco and M{\"u}ller, Ulrike and Raeven, Leon and Wubbolts, Marcel},
  title     = {Metabolic engineering for microbial production of aromatic amino acids and derived compounds},
  series = {Metabolic engineering},
  volume    = {Vol. 3},
  journal   = {Metabolic engineering},
  number    = {Iss. 4},
  issn      = {1096-7184 (E-Journal); 1096-7176 (Print)},
  pages     = {289 -- 300},
  year      = {2001},
  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}
}