@article{Lassonczyk1991, author = {Lassonczyk, Beate}, title = {Bodenentwicklung auf Terrassenschottern im ariden Bereich von NO-Somalia}, series = {Mitteilungen der Deutschen Bodenkundlichen Gesellschaft. 66 (1991), H. 2}, journal = {Mitteilungen der Deutschen Bodenkundlichen Gesellschaft. 66 (1991), H. 2}, isbn = {0343-107x}, pages = {1153 -- 1156}, year = {1991}, language = {de} } @inproceedings{SiegertIdingBaumannetal.2000, author = {Siegert, Petra and Iding, Hans and Baumann, Martin and McLeish, Michael J. and Kenyon, George L. and Pohl, Martina}, title = {Broadening of the substrate spectra of two ThDP-dependent decarboxylases using site-directed-mutagenesis}, series = {Proceedings of the 4th International Congress on Biochemical Engineering : 17 and 18 February 2000, Stuttgart}, booktitle = {Proceedings of the 4th International Congress on Biochemical Engineering : 17 and 18 February 2000, Stuttgart}, organization = {International Congress on Biochemical Engineering <4, 2000, Stuttgart>}, isbn = {3-8167-5570-4}, pages = {38 -- 42}, year = {2000}, language = {en} } @article{AboulnagaPinkenburgSchiffelsetal.2013, author = {Aboulnaga, El-Hussiny and Pinkenburg, Olaf and Schiffels, Johannes and El-Refai, Ahmed and Buckel, Wolfgang and Selmer, Thorsten}, title = {Butyrate production in Escherichia coli: Exploitation of an oxygen tolerant bifurcating butyryl-CoA dehydrogenase/electron transferring flavoprotein complex from Clostridium difficile}, series = {Journal of bacteriology. June 14, 2013}, journal = {Journal of bacteriology. June 14, 2013}, issn = {1098-5530 (E-Journal) ; 0021-9193 (Print)}, pages = {Epub ahead of print}, year = {2013}, language = {de} } @article{RibitschKarlBirnerGruenbergeretal.2010, author = {Ribitsch, D. and Karl, W. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. 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} } @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} } @misc{LauthHagemeyerLautensacketal.1999, author = {Lauth, Jakob and Hagemeyer, Alfred and Lautensack, Thomas and Deimling, Axel}, title = {Catalyst and catalytic oxidative dehydrogenation of alkylaromatics and paraffins : United States Patent ; patent number 5,902,918 ; date of patent: May 11, 1999 / Assignee: BASF Aktiengesellschaft. Inventors: Alfred Hagemeyer ; Gunter Lauth ; Thomas Lautensack ; Axel Deimling}, publisher = {United States Trademark and Patent Office}, address = {[Alexandria, VA]}, pages = {6 S.}, year = {1999}, language = {en} } @incollection{WendorffEggertPohletal.2007, author = {Wendorff, Marion and Eggert, Thorsten and Pohl, Martina and Dresen, Carola and M{\"u}ller, Michael and Jaeger, Karl-Erich and Sprenger, Georg A. and Sch{\"u}rmann, Melanie and Sch{\"u}rmann, Martin and Johnen, Sandra and Sprenger, Gerda and Sahm, Hermann and Inoue, Tomoyuki and Sch{\"o}rken, Ulrich and Breittaupt, Holger and Fr{\"o}lich, Bettina and Heim, Petra and Iding, Hans and Juchem, Bettina and Siegert, Petra and Kula, Maria-Regina and Weckbecker, Andrea and Hummel, Werner and Fessner, Wolf-Dieter and Elling, Lothar and Wolberg, Michael and Bode, Silke and Feldmann, Ralf and Geilenkirchen, Petra and Schubert, Thomas and Walter, Lydia and D{\"u}nnwald, Thomas and Demir, Ayhan S. and Kolter-Jung, Doris and Nitsche, Adam and D{\"u}nkelmann, Pascal and Cosp, Annabel and Lingen, Bettina}, title = {Catalytic asymmetric synthesis : section 2.2}, series = {Asymmetric synthesis with chemical and biological methods / ed. by Dieter Enders ...}, booktitle = {Asymmetric synthesis with chemical and biological methods / ed. by Dieter Enders ...}, publisher = {Wiley-VCH}, address = {Weinheim}, isbn = {978-3-527-31473-7}, pages = {298 -- 413}, year = {2007}, 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{KochWunderlichSeibleretal.2008, author = {Koch, Linda and Wunderlich, F. Thomas and Seibler, Jost and K{\"o}nner, A. Christine and Hampel, Brigitte and Irlenbusch, Sigrid and Brabant, Georg and Kahn, C. Ronald and Schwenk, Frieder and Br{\"u}ning, Jens C.}, title = {Central insulin action regulates peripheral glucose and fat metabolism in mice}, series = {The Journal of Clinical Investigation (JCI)}, volume = {118}, journal = {The Journal of Clinical Investigation (JCI)}, number = {6}, issn = {1558-8238}, doi = {10.1172/JCI31073}, pages = {2132 -- 2147}, year = {2008}, language = {en} } @article{PrielmeierNagatomoFrahm1994, author = {Prielmeier, Franz and Nagatomo, Yasushi and Frahm, Jens}, title = {Cerebral blood oxygenation in rat brain during hypoxic hypoxia. Quantitative MRI of effective transverse relaxation rates}, series = {Magnetic Resonance in Medicine. 31 (1994), H. 6}, journal = {Magnetic Resonance in Medicine. 31 (1994), H. 6}, isbn = {0740-3194}, pages = {678 -- 681}, year = {1994}, language = {en} }