@misc{EngelBayerUlberetal.2018,
  author    = {Engel, Mareike and Bayer, Hendrik and Ulber, Roland and Tippk{\"o}tter, Nils},
  title     = {Kommt es in Elektrofermentationen mit Clostridium acetobutylicum zu einer Eisenlimitierung?},
  series = {Chemie Ingenieur Technik},
  volume    = {90},
  journal   = {Chemie Ingenieur Technik},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0009-286X},
  doi       = {10.1002/cite.201855047},
  pages     = {1154},
  year      = {2018},
  abstract  = {Das strikt anaerobe Bakterium Clostridium acetobutylicum bildet die L{\"o}semittel Aceton, Butanol und Ethanol (ABE-Fermentation). Im Fall einer Eisenlimitierung kommt es zus{\"a}tzlich zu einer Riboflavinsekretion (RF), was durch die gelbe F{\"a}rbung des Kultur{\"u}berstands erkennbar ist. In dieser Arbeit wurde beobachtet, dass w{\"a}hrend Elektrofermentationen mit C. acetobutylicum bei -600 mV eine gelbe F{\"a}rbung auftritt. Es wurde deshalb untersucht, ob eine Eisenlimitierung im bio-elektrochemischen System (BES) vorliegt. Hierzu wurden die Flavinspezien bei Kultivierungen in Medien mit einer Eisenlimitierung bzw. mit ausreichend Eisen in Serumflaschen sowie im BES mit und ohne angelegtem Potenzial verglichen. In den Serumflaschenversuchen wurden RF und Flavinadenindinukleotid (FAD)-Konzentrationen von ‡ 20 mg L⁻¹ sowie Flavinmononukleotid (FMN)-Konzentrationen von ca. 5 mg L⁻¹ detektiert. Bei ausreichender Eisenverf{\"u}gbarkeit hingegen wurden in den Serumflaschen fast keine Flavine sekretiert. Im BES bei -600 mV hingegen wurde auch in diesen Kultur{\"u}berst{\"a}nden FMN und FAD (1-5 mg L⁻¹ ),jedoch kein RF gemessen. Diese Ergebnisse zeigen, dass die Flavinbildung im BES mit angelegtem Potenzial nicht mit der Flavinbildung unter Eisenlimitierung in Serumflaschen korreliert. Andere Faktoren f{\"u}r eine m{\"o}gliche Flavinbildung werden aktuell n{\"a}her betrachtet.},
  language  = {de}
}
@article{VarrialeHengsbachGuoetal.2024,
  author    = {Varriale, Ludovica and Hengsbach, Jan-Niklas and Guo, Tianyi and Kuka, Katrin and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Sustainable production of lactic acid using a perennial ryegrass as feedstock—a comparative study of fermentation at the bench- and reactor-scale, and ensiling},
  series = {Sustainability},
  volume    = {16},
  journal   = {Sustainability},
  number    = {18},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2071-1050},
  doi       = {10.3390/su16188054},
  year      = {2024},
  abstract  = {Perennial ryegrass (Lolium perenne) is an underutilized lignocellulosic biomass that has several benefits such as high availability, renewability, and biomass yield. The grass press-juice obtained from the mechanical pretreatment can be used for the bio-based production of chemicals. Lactic acid is a platform chemical that has attracted consideration due to its broad area of applications. For this reason, the more sustainable production of lactic acid is expected to increase. In this work, lactic acid was produced using complex medium at the bench- and reactor scale, and the results were compared to those obtained using an optimized press-juice medium. Bench-scale fermentations were carried out in a pH-control system and lactic acid production reached approximately 21.84 ± 0.95 g/L in complex medium, and 26.61 ± 1.2 g/L in press-juice medium. In the bioreactor, the production yield was 0.91 ± 0.07 g/g, corresponding to a 1.4-fold increase with respect to the complex medium with fructose. As a comparison to the traditional ensiling process, the ensiling of whole grass fractions of different varieties harvested in summer and autumn was performed. Ensiling showed variations in lactic acid yields, with a yield up to 15.2\% dry mass for the late-harvested samples, surpassing typical silage yields of 6-10\% dry mass.},
  language  = {en}
}
@article{UndenBeckerBongaertsetal.1995,
  author    = {Unden, Gottfried and Becker, S. and Bongaerts, Johannes and Holighaus, G. and Schirawski, Jan and Six, Simon},
  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, Gottfried and Becker, S. and Bongaerts, Johannes and Schirawski, Jan and Six, Simon},
  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{ElbersPfefferFrieseletal.1993,
  author    = {Elbers, Gereon and Pfeffer, H.-U. and Friesel, J. and Beier, Reinhold},
  title     = {Pilotuntersuchungen gem{\"a}ß dem Verordnungsentwurf nach \S 40, Abs. 2 des Bundesimmissionsschutzgesetzes / H.-U. Pfeffer, J. Friesel, G. Elbers, R. Beier, K. Ellermann},
  series = {Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung : Vortr{\"a}ge und Berichte zum Kolloquium "Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung - Bilanz und Perspektiven" am 11. November 1993 in Essen / [Hrsg.: Landesanstalt f{\"u}r Immissionsschutz Nordrhein-Westfalen. Red. Bearb.: Robert Niesenhaus]},
  journal   = {Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung : Vortr{\"a}ge und Berichte zum Kolloquium "Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung - Bilanz und Perspektiven" am 11. November 1993 in Essen / [Hrsg.: Landesanstalt f{\"u}r Immissionsschutz Nordrhein-Westfalen. Red. Bearb.: Robert Niesenhaus]},
  address   = {Essen},
  pages     = {117},
  year      = {1993},
  language  = {de}
}
@article{RibitschHeumannKarletal.2012,
  author    = {Ribitsch, Doris and Heumann, Sonja and Karl, Wolfgang and Gerlach, Jochen and Leber, R. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, Peter and Siegert, Petra and Lange, J. and Maurer, Karl-Heinz and Berg, G. and Guebitz, G. M. and Schwab, H.},
  title     = {Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli},
  series = {Journal of biotechnology},
  volume    = {157},
  journal   = {Journal of biotechnology},
  number    = {1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2011.09.025},
  pages     = {140 -- 147},
  year      = {2012},
  abstract  = {A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3. From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.},
  language  = {en}
}
@article{RibitschKarlBirnerGruenbergeretal.2010,
  author    = {Ribitsch, Doris and Karl, Wolfgang and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, Peter and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Schwab, H.},
  title     = {C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli},
  series = {Journal of biotechnology},
  volume    = {150},
  journal   = {Journal of biotechnology},
  number    = {3},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2010.09.947},
  pages     = {408 -- 416},
  year      = {2010},
  abstract  = {Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477. This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7-11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.},
  language  = {en}
}
@misc{BergBesslerGerlachetal.2009,
  author    = {Berg, Gabriele and Bessler, Cornelius and Gerlach, Jochen and G{\"u}bitz, Georg and Heumann, Sonja and Karl, Wolfgang and Maurer, Karl-Heinz and Remler, Peter and Ribitsch, Doris and Schwab, Helmut and Siegert, Petra and Wieland, Susanne},
  title     = {Mittel enthaltend Proteasen aus Stenotrophomonas maltophilia [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / USPTO / WIPO},
  address   = {M{\"u}nchen / Den Hague / Washington / Genf},
  pages     = {1 -- 47},
  year      = {2009},
  language  = {de}
}