@misc{O'ConnellSiegertEversetal.2010, author = {O'Connell, Timothy and Siegert, Petra and Evers, Stefan and Bongaerts, Johannes and Weber, Thomas and Maurer, Karl-Heinz and Bessler, Cornelius}, title = {Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft [Offenlegungsschrift]}, publisher = {Deutsches Patentamt}, address = {M{\"u}nchen}, pages = {1 -- 34}, year = {2010}, language = {de} } @article{BongaertsZoschkeWeidneretal.1995, author = {Bongaerts, Johannes and Zoschke, Sascha and Weidner, Uwe and Linden, Gottfried}, title = {Transcriptional regulation of the proton translocating NADH}, series = {Molecular microbiology}, volume = {Vol. 16}, journal = {Molecular microbiology}, number = {Iss. 3}, issn = {1365-2958 (E-Journal); 0950-382x (Print)}, pages = {521 -- 534}, year = {1995}, language = {en} } @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{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{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{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{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{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{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{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{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{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{FalkenbergBottBongaertsetal.2022, author = {Falkenberg, Fabian and Bott, Michael and Bongaerts, Johannes and Siegert, Petra}, title = {Phylogenetic survey of the subtilase family and a data-mining-based search for new subtilisins from Bacillaceae}, series = {Frontiers in Microbiology}, volume = {2022}, journal = {Frontiers in Microbiology}, number = {13}, publisher = {Frontiers}, address = {Lausanne}, issn = {1664-302X}, doi = {10.3389/fmicb.2022.1017978}, pages = {Artikel 13:1017978}, year = {2022}, abstract = {The subtilase family (S8), a member of the clan SB of serine proteases are ubiquitous in all kingdoms of life and fulfil different physiological functions. Subtilases are divided in several groups and especially subtilisins are of interest as they are used in various industrial sectors. Therefore, we searched for new subtilisin sequences of the family Bacillaceae using a data mining approach. The obtained 1,400 sequences were phylogenetically classified in the context of the subtilase family. This required an updated comprehensive overview of the different groups within this family. To fill this gap, we conducted a phylogenetic survey of the S8 family with characterised holotypes derived from the MEROPS database. The analysis revealed the presence of eight previously uncharacterised groups and 13 subgroups within the S8 family. The sequences that emerged from the data mining with the set filter parameters were mainly assigned to the subtilisin subgroups of true subtilisins, high-alkaline subtilisins, and phylogenetically intermediate subtilisins and represent an excellent source for new subtilisin candidates.}, 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} } @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{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{HaegerJolmesOyenetal.2024, author = {Haeger, Gerrit and Jolmes, Tristan and Oyen, Sven and Jaeger, Karl-Erich and Bongaerts, Johannes and Sch{\"o}rken, Ulrich and Siegert, Petra}, title = {Novel recombinant aminoacylase from Paraburkholderia monticola capable of N-acyl-amino acid synthesis}, series = {Applied Microbiology and Biotechnology}, journal = {Applied Microbiology and Biotechnology}, number = {108}, publisher = {Springer}, address = {Berlin}, issn = {1432-0614}, doi = {10.1007/s00253-023-12868-8}, pages = {14 Seiten}, year = {2024}, abstract = {N-Acyl-amino acids can act as mild biobased surfactants, which are used, e.g., in baby shampoos. However, their chemical synthesis needs acyl chlorides and does not meet sustainability criteria. Thus, the identification of biocatalysts to develop greener synthesis routes is desirable. We describe a novel aminoacylase from Paraburkholderia monticola DSM 100849 (PmAcy) which was identified, cloned, and evaluated for its N-acyl-amino acid synthesis potential. Soluble protein was obtained by expression in lactose autoinduction medium and co-expression of molecular chaperones GroEL/S. Strep-tag affinity purification enriched the enzyme 16-fold and yielded 15 mg pure enzyme from 100 mL of culture. Biochemical characterization revealed that PmAcy possesses beneficial traits for industrial application like high temperature and pH-stability. A heat activation of PmAcy was observed upon incubation at temperatures up to 80 °C. Hydrolytic activity of PmAcy was detected with several N-acyl-amino acids as substrates and exhibited the highest conversion rate of 773 U/mg with N-lauroyl-L-alanine at 75 °C. The enzyme preferred long-chain acyl-amino-acids and displayed hardly any activity with acetyl-amino acids. PmAcy was also capable of N-acyl-amino acid synthesis with good conversion rates. The best synthesis results were obtained with the cationic L-amino acids L-arginine and L-lysine as well as with L-leucine and L-phenylalanine. Exemplarily, L-phenylalanine was acylated with fatty acids of chain lengths from C8 to C18 with conversion rates of up to 75\%. N-lauroyl-L-phenylalanine was purified by precipitation, and the structure of the reaction product was verified by LC-MS and NMR.}, language = {en} } @article{HaegerProbstJaegeretal.2023, author = {Haeger, Gerrit and Probst, Johanna and Jaeger, Karl-Erich and Bongaerts, Johannes and Siegert, Petra}, title = {Novel aminoacylases from Streptomyces griseus DSM 40236 and their recombinant production in Streptomyces lividans}, series = {FEBS Open Bio}, volume = {13}, journal = {FEBS Open Bio}, number = {12}, publisher = {Wiley}, address = {Hoboken, NJ}, issn = {2211-5463}, doi = {10.1002/2211-5463.13723}, pages = {2224 -- 2238}, year = {2023}, abstract = {Amino acid-based surfactants are valuable compounds for cosmetic formulations. The chemical synthesis of acyl-amino acids is conventionally performed by the Schotten-Baumann reaction using fatty acyl chlorides, but aminoacylases have also been investigated for use in biocatalytic synthesis with free fatty acids. Aminoacylases and their properties are diverse; they belong to different peptidase families and show differences in substrate specificity and biocatalytic potential. Bacterial aminoacylases capable of synthesis have been isolated from Burkholderia, Mycolicibacterium, and Streptomyces. Although several proteases and peptidases from S. griseus have been described, no aminoacylases from this species have been identified yet. In this study, we investigated two novel enzymes produced by S. griseus DSM 40236ᵀ . We identified and cloned the respective genes and recombinantly expressed an α-aminoacylase (EC 3.5.1.14), designated SgAA, and an ε-lysine acylase (EC 3.5.1.17), designated SgELA, in S. lividans TK23. The purified aminoacylase SgAA was biochemically characterized, focusing on its hydrolytic activity to determine temperature- and pH optima and stabilities. The aminoacylase could hydrolyze various acetyl-amino acids at the Nα -position with a broad specificity regarding the sidechain. Substrates with longer acyl chains, like lauroyl-amino acids, were hydrolyzed to a lesser extent. Purified aminoacylase SgELA specific for the hydrolysis of Nε -acetyl-L-lysine was unstable and lost its enzymatic activity upon storage for a longer period but could initially be characterized. The pH optimum of SgELA was pH 8.0. While synthesis of acyl-amino acids was not observed with SgELA, SgAA catalyzed the synthesis of lauroyl-methionine.}, language = {en} }