@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{JablonskiMuenstermannNorketal.2021,
  author    = {Jablonski, Melanie and M{\"u}nstermann, Felix and Nork, Jasmina and Molinnus, Denise and Muschallik, Lukas and Bongaerts, Johannes and Wagner, Torsten and Keusgen, Michael and Siegert, Petra and Sch{\"o}ning, Michael Josef},
  title     = {Capacitive field-effect biosensor applied for the detection of acetoin in alcoholic beverages and fermentation broths},
  series = {physica status solidi (a) applications and materials science},
  volume    = {218},
  journal   = {physica status solidi (a) applications and materials science},
  number    = {13},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.202000765},
  pages     = {7 Seiten},
  year      = {2021},
  abstract  = {An acetoin biosensor based on a capacitive electrolyte-insulator-semiconductor (EIS) structure modified with the enzyme acetoin reductase, also known as butane-2,3-diol dehydrogenase (Bacillus clausii DSM 8716ᵀ), is applied for acetoin detection in beer, red wine, and fermentation broth samples for the first time. The EIS sensor consists of an Al/p-Si/SiO₂/Ta₂O₅ layer structure with immobilized acetoin reductase on top of the Ta₂O₅ transducer layer by means of crosslinking via glutaraldehyde. The unmodified and enzyme-modified sensors are electrochemically characterized by means of leakage current, capacitance-voltage, and constant capacitance methods, respectively.},
  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{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{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{MuschallikKippReckeretal.2020,
  author    = {Muschallik, Lukas and Kipp, Carina Ronja and Recker, Inga and Bongaerts, Johannes and Pohl, Martina and Gelissen, Melanie and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra},
  title     = {Synthesis of α-hydroxy ketones and vicinal diols with the Bacillus licheniformis DSM 13T butane-2, 3-diol dehydrogenase},
  series = {Journal of Biotechnology},
  volume    = {202},
  journal   = {Journal of Biotechnology},
  number    = {Vol. 324},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {2590-1559},
  doi       = {10.1016/j.jbiotec.2020.09.016},
  pages     = {61 -- 70},
  year      = {2020},
  abstract  = {The enantioselective synthesis of α-hydroxy ketones and vicinal diols is an intriguing field because of the broad applicability of these molecules. Although, butandiol dehydrogenases are known to play a key role in the production of 2,3-butandiol, their potential as biocatalysts is still not well studied. Here, we investigate the biocatalytic properties of the meso-butanediol dehydrogenase from Bacillus licheniformis DSM 13T (BlBDH). The encoding gene was cloned with an N-terminal StrepII-tag and recombinantly overexpressed in E. coli. BlBDH is highly active towards several non-physiological diketones and α-hydroxyketones with varying aliphatic chain lengths or even containing phenyl moieties. By adjusting the reaction parameters in biotransformations the formation of either the α-hydroxyketone intermediate or the diol can be controlled.},
  language  = {en}
}
@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{MuschallikMolinnusJablonskietal.2020,
  author    = {Muschallik, Lukas and Molinnus, Denise and Jablonski, Melanie and Kipp, Carina Ronja and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra},
  title     = {Synthesis of α-hydroxy ketones and vicinal (R, R)-diols by Bacillus clausii DSM 8716ᵀ butanediol dehydrogenase},
  series = {RSC Advances},
  volume    = {10},
  journal   = {RSC Advances},
  publisher = {Royal Society of Chemistry (RSC)},
  address   = {Cambridge},
  issn      = {2046-2069},
  doi       = {10.1039/D0RA02066D},
  pages     = {12206 -- 12216},
  year      = {2020},
  abstract  = {α-hydroxy ketones (HK) and 1,2-diols are important building blocks for fine chemical synthesis. Here, we describe the R-selective 2,3-butanediol dehydrogenase from B. clausii DSM 8716ᵀ (BcBDH) that belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR) and catalyzes the selective asymmetric reduction of prochiral 1,2-diketones to the corresponding HK and, in some cases, the reduction of the same to the corresponding 1,2-diols. Aliphatic diketones, like 2,3-pentanedione, 2,3-hexanedione, 5-methyl-2,3-hexanedione, 3,4-hexanedione and 2,3-heptanedione are well transformed. In addition, surprisingly alkyl phenyl dicarbonyls, like 2-hydroxy-1-phenylpropan-1-one and phenylglyoxal are accepted, whereas their derivatives with two phenyl groups are not substrates. Supplementation of Mn²⁺ (1 mM) increases BcBDH's activity in biotransformations. Furthermore, the biocatalytic reduction of 5-methyl-2,3-hexanedione to mainly 5-methyl-3-hydroxy-2-hexanone with only small amounts of 5-methyl-2-hydroxy-3-hexanone within an enzyme membrane reactor is demonstrated.},
  language  = {en}
}
@article{MuellerBeckersMussmannetal.2018,
  author    = {M{\"u}ller, Janina and Beckers, Mario and Mußmann, Nina and Bongaerts, Johannes and B{\"u}chs, Jochen},
  title     = {Elucidation of auxotrophic deficiencies of Bacillus pumilus DSM 18097 to develop a defined minimal medium},
  series = {Microbial Cell Factories},
  volume    = {17},
  journal   = {Microbial Cell Factories},
  number    = {1},
  publisher = {BioMed Central},
  issn      = {1475-2859},
  doi       = {10.1186/s12934-018-0956-1},
  pages     = {Article No. 106},
  year      = {2018},
  abstract  = {Background Culture media containing complex compounds like yeast extract or peptone show numerous disadvantages. The chemical composition of the complex compounds is prone to significant variations from batch to batch and quality control is difficult. Therefore, the use of chemically defined media receives more and more attention in commercial fermentations. This concept results in better reproducibility, it simplifies downstream processing of secreted products and enable rapid scale-up. Culturing bacteria with unknown auxotrophies in chemically defined media is challenging and often not possible without an extensive trial-and-error approach. In this study, a respiration activity monitoring system for shake flasks and its recent version for microtiter plates were used to clarify unknown auxotrophic deficiencies in the model organism Bacillus pumilus DSM 18097. Results Bacillus pumilus DSM 18097 was unable to grow in a mineral medium without the addition of complex compounds. Therefore, a rich chemically defined minimal medium was tested containing basically all vitamins, amino acids and nucleobases, which are essential ingredients of complex components. The strain was successfully cultivated in this medium. By monitoring of the respiration activity, nutrients were supplemented to and omitted from the rich chemically defined medium in a rational way, thus enabling a systematic and fast determination of the auxotrophic deficiencies. Experiments have shown that the investigated strain requires amino acids, especially cysteine or histidine and the vitamin biotin for growth. Conclusions The introduced method allows an efficient and rapid identification of unknown auxotrophic deficiencies and can be used to develop a simple chemically defined tailor-made medium. B. pumilus DSM 18097 was chosen as a model organism to demonstrate the method. However, the method is generally suitable for a wide range of microorganisms. By combining a systematic combinatorial approach based on monitoring the respiration activity with cultivation in microtiter plates, high throughput experiments with high information content can be conducted. This approach facilitates media development, strain characterization and cultivation of fastidious microorganisms in chemically defined minimal media while simultaneously reducing the experimental effort.},
  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{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{RachingerBauchStrittmatteretal.2013,
  author    = {Rachinger, Michael and Bauch, Melanie and Strittmatter, Axel and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Daniel, Rolf and Liebl, Wolfgang and Liesegang, Heiko and Ehrenreich, Armin},
  title     = {Size unlimited markerless deletions by a transconjugative plasmid-system in Bacillus licheniformis},
  series = {Journal of biotechnology},
  volume    = {Vol. 164},
  journal   = {Journal of biotechnology},
  number    = {Iss. 4},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  pages     = {365 -- 369},
  year      = {2013},
  language  = {en}
}
@article{ScheeleBongaertsMaureretal.2009,
  author    = {Scheele, S. and Bongaerts, Johannes and Maurer, K.-H. and Freudl, R.},
  title     = {Sekretion einer Kofaktor-haltigen Oxidase durch Corynebacterium glutamicum},
  series = {Chemie - Ingenieur - Technik (CIT)},
  volume    = {Vol. 81},
  journal   = {Chemie - Ingenieur - Technik (CIT)},
  number    = {Iss. 8},
  issn      = {1522-2640 (E-Journal); 0009-286X (Print)},
  pages     = {1309},
  year      = {2009},
  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}
}
@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{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}
}
@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{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{UndenBeckerBongaertsetal.1994,
  author    = {Unden, G. and Becker, S. and Bongaerts, Johannes and Schirawski, J. and Six, S.},
  title     = {Oxygen regulated gene expression in facultatively anaerobic bacteria},
  series = {Antonie van Leeuwenhoek},
  volume    = {Vol. 66},
  journal   = {Antonie van Leeuwenhoek},
  number    = {Iss. 1-3},
  issn      = {0003-6072 (Print) ; 1572-9699 (online)},
  pages     = {3 -- 22},
  year      = {1994},
  language  = {en}
}