@article{MangHodeniusSchmitzRodeetal.2009, author = {Mang, Thomas and Hodenius, M. A. J. and Schmitz-Rode, T. and Baumann, M.}, title = {Absorption of 10-hydroxycamptothecin into the coat of magnetoliposomes / Hodenius, M. A. J. ; Schmitz-Rode, T. ; Baumann, M. ; Ivoanova, G. ; Wong, J. E. ; Mang, T. ; Haulena, F. ; Soenen, S. J. H. ; De Cuyper, M.}, series = {Colloids and Surfaces A: Physicochemical and Engineering Aspects. 343 (2009), H. 1-3}, journal = {Colloids and Surfaces A: Physicochemical and Engineering Aspects. 343 (2009), H. 1-3}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {0927-7757}, pages = {20 -- 23}, year = {2009}, language = {en} } @article{BaeckerBegingBisellietal.2009, author = {B{\"a}cker, Matthias and Beging, Stefan and Biselli, Manfred and Poghossian, Arshak and Wang, J. and Zang, Werner and Wagner, Patrick and Sch{\"o}ning, Michael Josef}, title = {Concept for a solid-state multi-parameter sensor system for cell-culture monitoring}, series = {Electrochimica Acta. 54 (2009), H. 25 Sp. Iss. SI}, journal = {Electrochimica Acta. 54 (2009), H. 25 Sp. Iss. SI}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {0013-4686}, pages = {6107 -- 6112}, year = {2009}, language = {en} } @article{SchiffelsBaumannSelmer2011, author = {Schiffels, Johannes and Baumann, Marcus and Selmer, Thorsten}, title = {Facile analysis of short-chain fatty acids as 4-nitrophenyl esters in complex anaerobic fermentation samples by high performance liquid chromatography}, series = {Journal of Chromatography A. 1218 (2011), H. 34}, journal = {Journal of Chromatography A. 1218 (2011), H. 34}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {0021-9673}, pages = {5848 -- 5851}, year = {2011}, language = {en} } @article{BaeckerDellePoghossianetal.2011, author = {B{\"a}cker, Matthias and Delle, L. and Poghossian, Arshak and Biselli, Manfred and Zang, Werner and Wagner, P. and Sch{\"o}ning, Michael Josef}, title = {Electrochemical sensor array for bioprocess monitoring}, series = {Electrochimica Acta (2011)}, volume = {56}, journal = {Electrochimica Acta (2011)}, number = {26}, publisher = {Elsevier}, address = {Amsterdam}, pages = {9673 -- 9678}, year = {2011}, language = {en} } @article{SpiessWilfriedAlvarezetal.2011, author = {Spiess, Elmar and Wilfried, Reichardt and Alvarez, Gerardo and Gottrup, Marcus and {\"O}hlschl{\"a}ger, Peter}, title = {An Artificial PAP Gene Breaks Self-tolerance and Promotes Tumor Regression in the TRAMP Model for Prostate Carcinoma}, series = {Molecular Therapy}, volume = {20}, journal = {Molecular Therapy}, number = {3}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {1525-0016}, pages = {555 -- 564}, year = {2011}, language = {en} } @article{BorgmeierBongaertsMeinhardt2012, author = {Borgmeier, Claudia and Bongaerts, Johannes and Meinhardt, Friedhelm}, title = {Genetic analysis of the Bacillus licheniformis degSU operon and the impact of regulatory mutations on protease production}, series = {Journal of biotechnology}, volume = {159}, journal = {Journal of biotechnology}, number = {1-2}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, doi = {10.1016/j.jbiotec.2012.02.011}, pages = {12 -- 20}, year = {2012}, abstract = {Disruption experiments targeted at the Bacillus licheniformis degSU operon and GFP-reporter analysis provided evidence for promoter activity immediately upstream of degU. pMutin mediated concomitant introduction of the degU32 allele - known to cause hypersecretion in Bacillus subtilis - resulted in a marked increase in protease activity. Application of 5-fluorouracil based counterselection through establishment of a phosphoribosyltransferase deficient Δupp strain eventually facilitated the marker-free introduction of degU32 leading to further protease enhancement achieving levels as for hypersecreting wild strains in which degU was overexpressed. Surprisingly, deletion of rapG - known to interfere with DegU DNA-binding in B. subtilis - did not enhance protease production neither in the wild type nor in the degU32 strain. The combination of degU32 and Δupp counterselection in the type strain is not only equally effective as in hypersecreting wild strains with respect to protease production but furthermore facilitates genetic strain improvement aiming at biological containment and effectiveness of biotechnological processes.}, language = {en} } @article{WilmingBegemannKuhneetal.2013, author = {Wilming, Anja and Begemann, Jens and Kuhne, Stefan and Regestein, Lars and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and B{\"u}chs, Jochen}, title = {Metabolic studies of γ-polyglutamic acid production in Bacillus licheniformis by small-scale continuous cultivations}, series = {Biochemical engineering journal}, volume = {Vol. 73}, journal = {Biochemical engineering journal}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-295X (E-Journal); 1369-703X (Print)}, pages = {29 -- 37}, year = {2013}, 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{DuttaHartkopfFroederWitteetal.2013, author = {Dutta, Suryendu and Hartkopf-Fr{\"o}der, Christoph and Witte, Karin and Brocke, Rainer and Mann, Ulrich}, title = {Molecular characterization of fossil palynomorphs by transmission micro-FTIR spectroscopy: implications for hydrocarbon source evaluation}, series = {International journal of coal geology}, volume = {Vol. 115}, journal = {International journal of coal geology}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1872-7840 (E-Journal); 0166-5162 (Print)}, pages = {13 -- 23}, year = {2013}, language = {en} } @article{RibitschHeumannKarletal.2012, author = {Ribitsch, D. and Heumann, S. and Karl, W. and Gerlach, J. and Leber, R. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. 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} }