TY - JOUR A1 - Ulber, Roland A1 - Poth, Sebastian A1 - Monzon, Magaly A1 - Tippkötter, Nils T1 - Prozessintegration von Hydrolyse und Fermentation von Cellulose- Faserstoff JF - Chemie Ingenieur Technik N2 - Ein viel versprechender erneuerbarer Rohstoff für die Produktion von Chemikalien und Treibstoffen ist Lignocellulose aus pflanzlicher Biomasse. Die darin enthaltenen Zucker können mittels enzymatischer Hydrolyse freigesetzt und fermentativ zu Ethanol umgesetzt werden. Ein interessanter Ansatz ist dabei die simultane Verzuckerung und Fermentation. Hefen und Enzyme haben mit 30 °C bzw. 50 °C zwar unterschiedliche Temperaturoptima, es konnte aber gezeigt werden, dass auch bei den niedrigeren Temperaturen eine Umsetzung der Cellulose zu Glucose erfolgt, wenn auch langsamer als bei optimalen Bedingungen. Außerdem konnte in Vorversuchen gezeigt werden, dass Ethanol in den zu erwartenden Konzentrationen keinen Einfluss auf die enzymatische Umsetzung hat. Y1 - 2010 U6 - http://dx.doi.org/10.1002/cite.200900103 SN - 1522-2640 N1 - Special Issue "Biokatalyse" VL - 82 IS - 1-2 SP - 135 EP - 139 ER - TY - JOUR A1 - Sieker, Tim A1 - Neuner, Andreas A1 - Dimitrova, Darina A1 - Tippkötter, Nils A1 - Bart, Hans-Jörg A1 - Heinzle, Elmar A1 - Ulber, Roland T1 - Grassilage als Rohstoff für die chemische Industrie JF - Chemie Ingenieur Technik N2 - Grassilage stellt einen nachwachsenden Rohstoff mit großem Potenzial dar. Neben Cellulose und Hemicellulose enthält sie auch organische Säuren, insbesondere Milchsäure. In einem Bioraffinerie-Projekt wird die Milchsäure aus der Silage isoliert und mit gentechnisch optimierten Stämmen zu L-Lysin weiterverarbeitet. Die Lignocellulose wird hydrolysiert und zu Ethanol fermentiert. Ein besonderes Augenmerk liegt auf der Integration der unterschiedlichen Prozesse sowie der einzelnen Prozessschritte zu einem Gesamtprozess, der sämtliche Inhaltsstoffe der Silage verwertet. Y1 - 2010 U6 - http://dx.doi.org/10.1002/cite.201000088 SN - 1522-2640 VL - 82 IS - 8, Special Issue: Industrielle Nutzung nachwachsender Rohstoffe SP - 1153 EP - 1159 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Degering, Christian A1 - Eggert, Thorsten A1 - Puls, Michael A1 - Bongaerts, Johannes A1 - Evers, Stefan A1 - Maurer, Karl-Heinz A1 - Jaeger, Karl-Erich T1 - Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides JF - Applied and environmental microbiology N2 - 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. Y1 - 2010 U6 - http://dx.doi.org/10.1128/AEM.01146-10 SN - 1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print) VL - 76 IS - 19 SP - 6370 EP - 6378 PB - American Society for Microbiology CY - Washington, DC ER - TY - JOUR A1 - Werner, Frederik A1 - Krumbe, Christoph A1 - Schumacher, Katharina A1 - Groebel, Simone A1 - Spelthahn, Heiko A1 - Stellberg, Michael A1 - Wagner, Torsten A1 - Yoshinobu, Tatsuo A1 - Selmer, Thorsten A1 - Keusgen, Michael A1 - Baumann, Marcus A1 - Schöning, Michael Josef T1 - Determination of the extracellular acidification of Escherichia coli by a light-addressable potentiometric sensor JF - Physica status solidi (a) : applications and material science. 208 (2011), H. 6 Y1 - 2011 SN - 1862-6319 SP - 1340 EP - 1344 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Werner, Frederik A1 - Groebel, Simone A1 - Wagner, Torsten A1 - Yoshinobu, Tatsuo A1 - Selmer, Thorsten A1 - Baumann, Marcus A1 - Schöning, Michael Josef T1 - Überwachung der metabolischen Aktivität von Mikroorganismen zur Kontrolle des biologischen Prozesses im Biogasfermenter JF - Biogas 2011 : Energieträger der Zukunft ; 6. Fachtagung, Fachtagung Braunschweig, 08. und 09. Juni 2011 / VDI Energie und Umwelt Y1 - 2011 SN - 978-3-18-092121-1 N1 - Gesellschaft Energie und Umwelt ; Fachtagung Biogas ; (6 : ; 2011.06.08-09 : ; Braunschweig) ; VDI-Berichte ; 2121 SP - 285 EP - 286 PB - VDI-Verl. CY - Düsseldorf ER - TY - JOUR A1 - Martins, Berta M. A1 - Blaser, Martin A1 - Feliks, Mikolaj A1 - Ullmann, Matthias G. A1 - Buckel, Wolfgang A1 - Selmer, Thorsten T1 - Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme JF - Journal of the American Chemical Society Y1 - 2011 N1 - Just accepted manuscript SP - 1 EP - 33 PB - ACS Publications CY - Washington, DC ER - TY - JOUR A1 - Schiffels, Johannes A1 - Baumann, Marcus A1 - Selmer, Thorsten T1 - Facile analysis of short-chain fatty acids as 4-nitrophenyl esters in complex anaerobic fermentation samples by high performance liquid chromatography JF - Journal of Chromatography A. 1218 (2011), H. 34 Y1 - 2011 SN - 0021-9673 SP - 5848 EP - 5851 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Bäcker, Matthias A1 - Delle, L. A1 - Poghossian, Arshak A1 - Biselli, Manfred A1 - Zang, Werner A1 - Wagner, P. A1 - Schöning, Michael Josef T1 - Electrochemical sensor array for bioprocess monitoring JF - Electrochimica Acta (2011) Y1 - 2011 VL - 56 IS - 26 SP - 9673 EP - 9678 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Aggarwal, Prerna A1 - Singh, Virendra A1 - Singh, Arjun A1 - Scherer, Ulrich W. A1 - Singh, Tejvir A1 - Singla, Madan L. A1 - Srivastava, Alok T1 - Physico-chemical transformations in swift heavy ion modified poly(ethyleneterephthalate) JF - Radiation Physics and Chemistry Y1 - 2011 SN - 0969-806X N1 - In Press, Accepted Manuscript SP - 1 EP - 28 PB - Pergamon Press CY - Oxford ER - TY - JOUR A1 - Oosterhuis, Koen A1 - Öhlschläger, Peter A1 - Berg, Joost H. van den A1 - Toebes, Mireille A1 - Gomez, Raquel A1 - Schumacher, Ton N. A1 - Haanen, John B. T1 - Preclinical development of highly effective and safe DNA vaccines directed against HPV 16 E6 and E7 JF - International Journal of Cancer Y1 - 2011 SN - 1097-0215 VL - 129 IS - 2 SP - 397 EP - 406 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Öhlschläger, Peter A1 - Spies, Elmar A1 - Alvarez, Gerardo A1 - Quetting, Michael A1 - Groettrup, Marcus T1 - The combination of TLR-9 adjuvantation and electroporation-mediated delivery enhances in vivo antitumor responses after vaccination with HPV-16 E7 encoding DNA JF - International Journal of Cancer. 128 (2011), H. 2 Y1 - 2011 SN - 1097-0215 SP - 473 EP - 481 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Manea, Marilena A1 - Leurs, Ulrike A1 - Orban, Erika A1 - Baranyai, Zsuzsa A1 - Öhlschläger, Peter A1 - Marquardt, Andreas A1 - Schulcz, Akos A1 - Tejeda, Miguel T1 - Enhanced Enzymatic Stability and Antitumor Activity of Daunorubicin-GnRH-III Bioconjugates Modified in Position 4 JF - Bioconjugate Chemistry Y1 - 2011 SN - 1520-4812 VL - 22 IS - 7 SP - 1320 EP - 1329 PB - ACS CY - Washington, DC ER - TY - JOUR A1 - Spiess, Elmar A1 - Wilfried, Reichardt A1 - Alvarez, Gerardo A1 - Gottrup, Marcus A1 - Öhlschläger, Peter T1 - An Artificial PAP Gene Breaks Self-tolerance and Promotes Tumor Regression in the TRAMP Model for Prostate Carcinoma JF - Molecular Therapy Y1 - 2011 SN - 1525-0016 VL - 20 IS - 3 SP - 555 EP - 564 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Deppe, Veronika Maria A1 - Bongaerts, Johannes A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz A1 - Meinhardt, Friedhelm T1 - Enzymatic deglycation of Amadori products in bacteria JF - Applied microbiology and biotechnology Y1 - 2011 SN - 1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print) VL - Vol. 90 IS - Iss. 2 SP - 399 EP - 406 PB - Springer CY - Berlin ER - TY - JOUR A1 - Deppe, Veronika Maria A1 - Klatte, Stephanie A1 - Bongaerts, Johannes A1 - Maurer, Karl-Heinz A1 - O'Connell, Timothy A1 - Meinhardt, Friedhelm T1 - Genetic control of Amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR JF - Applied and environmental microbiology Y1 - 2011 SN - 1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print) VL - Vol. 77 IS - No. 9 SP - 2839 EP - 2846 PB - American Society of Mechanical Engineers (ASME) CY - New York ER - TY - JOUR A1 - Bongaerts, Johannes A1 - Esser, Simon A1 - Lorbach, Volker A1 - Al-Momani, Lóay A1 - Müller, Michael A. A1 - Franke, Dirk A1 - Grondal, Christoph A1 - Kurutsch, Anja A1 - Bujnicki, Robert A1 - Takors, Ralf A1 - Raeven, Leon A1 - Wubbolts, Marcel A1 - Bovenberg, Roel A1 - Nieger, Martin A1 - Schürmann, Melanie A1 - Trachtmann, Natalie A1 - Kozak, Stefan A1 - Sprenger, Georg A. A1 - Müller, Michael T1 - Diversity-oriented production of metabolites derived from chorismate and their use in organic synthesis JF - Angewandte Chemie International Edition Y1 - 2011 SN - 1521-3773 (E-Journal); 0570-0833 (Print); 1433-7851 (Print) VL - Vol. 50 IS - Iss. 34 SP - 7781 EP - 7786 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Niehaus, F. A1 - Gabor, E. A1 - Wieland, S. A1 - Siegert, Petra A1 - Maurer, Karl-Heinz A1 - Eck, J. T1 - Enzymes for the laundry industries: tapping the vast metagenomic pool of alkaline proteases JF - Microbial biotechnology Y1 - 2011 SN - 1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print) VL - Vol. 4 IS - Iss. 6 SP - 767 EP - 776 PB - Springer CY - Berlin ER - TY - PAT A1 - Siegert, Petra A1 - Evers, Stefan A1 - Marion, Merkel A1 - Mussmann, Nina A1 - Hellmuth, Hendrik A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz A1 - Schwaneberg, Ulrich A1 - Martinez, Ronny A1 - Jakob, Felix T1 - Verfahren zur Anpassung eines hydrolytischen Enzyms an eine das hydrolytische Enzym stabilisierende Komponente [Offenlegungsschrift] T1 - Method for adapting a hydrolytic enzyme to a component that stabilizes the hydrolytic enzyme [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2013 SP - 1 EP - 27 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Merkel, Marion A1 - Kluin, Cornelia A1 - Maurer, Karl-Heinz A1 - O'Connell, Timothy A1 - Wieland, Susanne A1 - Hellmuth, Hendrik T1 - Neue Proteasen und diese enthaltende Mittel [Offenlegungsschrift] T1 - Novel proteases and compositions comprising them [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2011 SP - 1 EP - 21 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Wieland, Susanne A1 - Siegert, Petra A1 - Spitz, Astrid A1 - Maurer, Karl-Heinz A1 - O'Connell, Timothy A1 - Prüser, Inken A1 - Schiedel, Marc-Steffen A1 - Eiting, Thomas A1 - Sendor-Müller, Dorota A1 - Bastigkeit, Thorsten A1 - Benda, Konstantin A1 - Müller, Sven T1 - Lagerstabiles flüssiges Wasch- oder Reinigungsmittel enthaltend Proteasen [Offenlegungsschrift] T1 - Storage-stable liquid washing or cleaning agent containing proteases [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2011 SP - 1 EP - 25 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - JOUR A1 - Raab, Monika A1 - Kappel, Sven A1 - Krämer, Andrea A1 - Sanhaji, Mourad A1 - Matthess, Yves A1 - Kurunci-Csacsko, Elisabeth A1 - Calzada-Wack, Julia A1 - Rathkolb, Birgit A1 - Rosman, Jan A1 - Adler, Thure A1 - Busch, Dirk H. A1 - Esposito, Irene A1 - Fuchs, Helmut A1 - Gailus-Durner, Valérie A1 - Klingenspor, Martin A1 - Wolf, Eckhard A1 - Sänger, Nicole A1 - Prinz, Florian A1 - Hrabe de Angelis, Martin A1 - Seibler, Jost A1 - Yuan, Juping A1 - Bergmann, Martin A1 - Knecht, Rainald A1 - Kreft, Bertolt A1 - Strebhardt, Klaus T1 - Toxicity modelling of Plk1-targeted therapies in genetically engineered mice and cultured primary mammalian cells JF - Nature Communications Y1 - 2011 U6 - http://dx.doi.org/10.1038/ncomms1395 SN - 2041-1723 VL - 2 IS - 395 SP - 1 EP - 11 PB - Nature CY - London ER - TY - JOUR A1 - Hasegawa, Maki A1 - Kapelyukh, Yury A1 - Tahara, Harunobu A1 - Seibler, Jost A1 - Rode, Anja A1 - Krueger, Sylvia A1 - Lee, Dongtao N. A1 - Wolf, C. Roland A1 - Scheer, Nico T1 - Quantitative prediction of human pregnane X receptor and cytochrome P450 3A4 mediated drug-drug interaction in a novel multiple humanized mouse line JF - Molecular Pharmacology Y1 - 2011 U6 - http://dx.doi.org/10.1124/mol.111.071845 SN - 1521-0111 VL - 80 IS - 33 SP - 518 EP - 528 PB - ASPET CY - Bethesda, Md. ER - TY - JOUR A1 - Jordan, Sabine D. A1 - Krüger, Markus A1 - Willmes, Diana M. A1 - Redemann, Nora A1 - Wunderlich, F. Thomas A1 - Brönneke, Hella S. A1 - Merkwirth, Carsten A1 - Kashkar, Hamid A1 - Olkkonen, Vesa M. A1 - Böttger, Thomas A1 - Braun, Thomas A1 - Seibler, Jost A1 - Brüning, Jens C. T1 - Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism JF - Nature Cell Biology N2 - The contribution of altered post-transcriptional gene silencing to the development of insulin resistance and type 2 diabetes mellitus so far remains elusive. Here, we demonstrate that expression of microRNA (miR)-143 and 145 is upregulated in the liver of genetic and dietary mouse models of obesity. Induced transgenic overexpression of miR-143, but not miR-145, impairs insulin-stimulated AKT activation and glucose homeostasis. Conversely, mice deficient for the miR-143–145 cluster are protected from the development of obesity-associated insulin resistance. Quantitative-mass-spectrometry-based analysis of hepatic protein expression in miR-143-overexpressing mice revealed miR-143-dependent downregulation of oxysterol-binding-protein-related protein (ORP) 8. Reduced ORP8 expression in cultured liver cells impairs the ability of insulin to induce AKT activation, revealing an ORP8-dependent mechanism of AKT regulation. Our experiments provide direct evidence that dysregulated post-transcriptional gene silencing contributes to the development of obesity-induced insulin resistance, and characterize the miR-143–ORP8 pathway as a potential target for the treatment of obesity-associated diabetes. Y1 - 2011 U6 - http://dx.doi.org/10.1038/ncb2211 SN - 1465-7392 VL - 13 IS - 4 SP - 434 EP - 446 PB - Nature CY - New York ER - TY - JOUR A1 - Inagaki, Akiko A1 - Sleddens-Linkels, Esther A1 - Wassenaar, Evelyne A1 - Ooms, Marja A1 - Cappellen, Wiggert A. van A1 - Hoeijmakers, Jan H. J. A1 - Seibler, Jost A1 - Vogt, Thomas F. A1 - Shin, Myung K. A1 - Grootegoed, J. Anton A1 - Baarends, Willy M. T1 - Meiotic functions of RAD18 JF - Journal of Cell Science Y1 - 2011 U6 - http://dx.doi.org/10.1242/jcs.081968 SN - 1477-9137 VL - 124 IS - 16 SP - 2837 EP - 2850 PB - Company of Biologists Limited CY - Cambridge ER - TY - JOUR A1 - Sieker, Tim A1 - Neuner, Andreas A1 - Dimitrova, Darina A1 - Tippkötter, Nils A1 - Muffler, Kai A1 - Bart, Hans-Jörg A1 - Heinzle, Elmar A1 - Ulber, Roland T1 - Ethanol production from grass silage by simultaneous pretreatment, saccharification and fermentation: First steps in the process development JF - Engineering in Life Sciences N2 - Grass silage provides a great potential as renewable feedstock. Two fractions of the grass silage, a press juice and the fiber fraction, were evaluated for their possible use for bioethanol production. Direct production of ethanol from press juice is not possible due to high concentrations of organic acids. For the fiber fraction, alkaline peroxide or enzymatic pretreatment was used, which removes the phenolic acids in the cell wall. In this study, we demonstrate the possibility to integrate the enzymatic pretreatment with a simultaneous saccharification and fermentation to achieve ethanol production from grass silage in a one-process step. Achieved yields were about 53 g ethanol per kg silage with the alkaline peroxide pretreatment and 91 g/kg with the enzymatic pretreatment at concentrations of 8.5 and 14.6 g/L, respectively. Furthermore, it was shown that additional supplementation of the fermentation medium with vitamins, trace elements and nutrient salts is not necessary when the press juice is directly used in the fermentation step. Y1 - 2011 U6 - http://dx.doi.org/10.1002/elsc.201000160 N1 - Special Issue "Bioprocess‐oriented plant design" VL - 11 IS - 4 SP - 436 EP - 442 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Poth, Sebastian A1 - Monzon, Magaly A1 - Tippkötter, Nils A1 - Ulber, Roland T1 - Lignocellulosic biorefinery: Process integration of hydrolysis and fermentation (SSF process) JF - Holzforschung N2 - The aim of the present work is the process integration and the optimization of the enzymatic hydrolysis of wood and the following fermentation of the products to ethanol. The substrate is a fiber fraction obtained by organosolv pre-treatment of beech wood. For the ethanol production, a co-fermentation by two different yeasts (Saccharomyces cerevisiae and Pachysolen tannophilus) was carried out to convert glucose as well as xylose. Two approaches has been followed: 1. A two step process, in which the hydrolysis of the fiber fraction and the fermentation to product are separated from each other. 2. A process, in which the hydrolysis and the fermentation are carried out in one single process step as simultaneous saccharification and fermentation (SSF). Following the first approach, a yield of about 0.15 g ethanol per gram substrate can be reached. Based on the SSF, one process step can be saved, and additionally, the gained yield can be raised up to 0.3 g ethanol per gram substrate. Y1 - 2011 N1 - 11th EWLP, Hamburg, Germany, August 16–19, 2010 VL - 65 IS - 5 SP - 633 EP - 637 PB - De Gruyter CY - Berlin ER - TY - CHAP A1 - Hahn, Thomas A1 - Kelly, Svenja A1 - Muffler, Kai A1 - Tippkötter, Nils A1 - Ulber, Roland ED - Hans-Jörg, Bart ED - Pilz, Stephan T1 - Extraction of lignocellulose and algae for the production of bulk and fine chemicals T2 - Industrial scale natural products extraction Y1 - 2011 SN - 978-3-527-32504-7 (Print) SN - 978-3-527-63512-2 (Online) U6 - http://dx.doi.org/10.1002/9783527635122 SP - 221 EP - 245 PB - Wiley-VCH CY - Weinheim ER - TY - CHAP A1 - Muffler, Kai A1 - Poth, Sabastian A1 - Sieker, Tim A1 - Tippkötter, Nils A1 - Ulber, Roland A1 - Sell, Dieter ED - Moo-Young, Murray T1 - Bio-feedstocks T2 - Comprehensive biotechnology : principles and practices in industry, agcriculture, medicine and the environment. Volume 2: Engineering fundamentals of biotechnology Y1 - 2011 SN - 978-0-444-53352-4 U6 - http://dx.doi.org/10.1016/B978-0-08-088504-9.00088-X SP - 93 EP - 101 PB - Elsevier CY - Amsterdam ET - 2. edition ER - TY - JOUR A1 - Tippkötter, Nils A1 - Wollny, S. A1 - Kampeis, P. A1 - Oster, J. A1 - Schneider, H. A1 - Ulber, R. T1 - Magnetseparation von Proteinen : Separation von Zielmolekülen durch hochselektive Aptamere JF - GIT Labor-Fachzeitschrift N2 - Durch die Kombination von Oligonukleotid-Liganden (Aptameren) hoher Bindungsaffinitäten mit hochselektiv abtrennbaren magnetisierbaren Mikropartikeln wird eine einstufige Separation von Zielmolekülen aus mikrobiologischen Produktionsansätzen möglich. Die Aptamere werden hierfür reversibel auf den Partikeloberflächen gebunden und für die spezifische Isolierung von Bioprodukten eingesetzt. Die Abtrennung der beladenen Partikel erfolgt durch einen neuen Rotor-Stator-Separator mit Hochgradient-Magnetfeld. Y1 - 2011 VL - 55 IS - 10 SP - 666 PB - Wiley CY - Weinheim ER - TY - CHAP A1 - Ulber, Roland A1 - Muffler, Kai A1 - Tippkötter, Nils A1 - Hirth, Thomas A1 - Sell, Dieter ED - Ulber, Roland ED - Sell, Dieter ED - Hirth, Thomas T1 - Introduction to Renewable Resources in the Chemical Industry T2 - Renewable raw materials : new feedstocks for the chemical industry Y1 - 2011 SN - 978-3-527-32548-1 SP - 1 EP - 6 PB - Wiley-VCH-Verlag CY - Weinheim ET - 1. Auflage ER - TY - JOUR A1 - Immel, Timo A. A1 - Groth, Ulrich A1 - Huhn, Thomas A1 - Öhlschläger, Peter T1 - Titanium salan complexes displays strong antitumor properties in vitro and in vivo in mice JF - PLoS ONE N2 - The anticancer activity of titanium complexes has been known since the groundbreaking studies of Köpf and Köpf-Maier on titanocen dichloride. Unfortunately, possibly due to their fast hydrolysis, derivatives of titanocen dichloride failed in clinical studies. Recently, the new family of titanium salan complexes containing tetradentate ONNO ligands with anti-cancer properties has been discovered. These salan complexes are much more stabile in aqueous media. In this study we describe the biological activity of two titanium salan complexes in a mouse model of cervical cancer. High efficiency of this promising complex family was demonstrated for the first time in vivo. From these data we conclude that titanium salan complexes display very strong antitumor properties exhibiting only minor side effects. Our results may influence the chemotherapy with metallo therapeutics in the future. Y1 - 2011 U6 - http://dx.doi.org/10.1371/journal.pone.0017869 VL - 6 IS - 3 PB - Plos CY - San Francisco, California, US ER - TY - CHAP A1 - Feuerriegel, Uwe A1 - Pook, Michael A1 - Wersch, Gregor A1 - Wittenhorst, Simon A1 - Becker, Jürgen A1 - Ecker, Markus A1 - Hoffmann, Ulrich A1 - Kunz, Ulrich T1 - Simulation von Wärmeübertragungsprozessen N2 - Mit freundlicher Genehmigung der Autoren und des Oldenbourg Industrieverlags https://www.oldenbourg-industrieverlag.de/de/9783835633223-33223 erschienen als Beitrag im Tagungsband zur AALE-Tagung 2012. 9. Fachkonferenz 4.-5. Mai 2012, Aachen, Fachhochschule. ISBN 9783835633223 S 5-1 S. 127-135 Es werden Ergebnisse unterschiedlicher Projekte aus dem Bereich der Simulation von Wärmeübertragungsprozessen mit Excel-VBA vorgestellt. - Thermische Behandlung hochviskoser Fruchtzubereitungen, verschiedene Projekte und Kooperationen mit der Zentis GmbH & Co. KG, Aachen (J. Becker, U. Feuerriegel, G. Wersch). - Untersuchung des dynamischen Verhaltens von dampfbeheizten Ethylen-Verdampfern. Projekt mit der TGE Gas Engineering GmbH, Bonn (M. Ecker, U. Feuerriegel, U. Hoffmann, S. Wittenhorst). - Dynamische Simulation des axialen Temperaturverlaufs von elektrisch beheizten Rohrreaktoren. Kooperation mit dem Institut für Chemische Verfahrenstechnik, TU Clausthal (U. Feuerriegel, U. Kunz, M. Pook, S. Wittenhorst). KW - Wärmeübertragung Y1 - 2012 ER - TY - JOUR A1 - Leurs, Ulrike A1 - Mezo, Gabor A1 - Öhlschläger, Peter A1 - Orban, Erika A1 - Marquard, Andrea A1 - Manea, Marilena T1 - Design, synthesis, in vitro stability and cytostatic effect of multifunctional anticancer drug-bioconjugates containing GnRH-III as a targeting moiety JF - Peptide Science N2 - Bioconjugates containing the GnRH-III hormone decapeptide as a targeting moiety are able to deliver chemotherapeutic agents specifically to cancer cells expressing GnRH receptors, thereby increasing their local efficacy while limiting the peripheral toxicity. However, the number of GnRH receptors on cancer cells is limited and they desensitize under continuous hormone treatment. A possible approach to increase the receptor mediated tumor targeting and consequently the cytostatic effect of the bioconjugates would be the attachment of more than one chemotherapeutic agent to one GnRH-III molecule. Here we report on the design, synthesis and biochemical characterization of multifunctional bioconjugates containing GnRH-III as a targeting moiety and daunorubicin as a chemotherapeutic agent. Two different drug design approaches were pursued. The first one was based on the bifunctional [4Lys]-GnRH-III (Glp-His-Trp-Lys-His-Asp-Trp-Lys-Pro-Gly-NH2) containing two lysine residues in positions 4 and 8, whose ϵ-amino groups were used for the coupling of daunorubicin. In the second drug design, the native GnRH-III (Glp-His-Trp-Ser-His-Asp-Trp-Lys-Pro-Gly-NH2) was used as a scaffold; an additional lysine residue was coupled to the ϵ-amino group of 8Lys in order to generate two free amino groups available for conjugation of daunorubicin. The in vitro stability/degradation of all synthesized compounds was investigated in human serum, as well as in the presence of rat liver lysosomal homogenate. Their cellular uptake was determined on human breast cancer cells and the cytostatic effect was evaluated on human breast, colon and prostate cancer cell lines. Compared with a monofunctional compound, both drug design approaches resulted in multifunctional bioconjugates with increased cytostatic effect. Y1 - 2012 U6 - http://dx.doi.org/10.1002/bip.21640 SN - 1097-0282 VL - 98 IS - 1 SP - 1 EP - 10 PB - Wiley CY - New York, NY ER - TY - JOUR A1 - Bäcker, Matthias A1 - Raue, Markus A1 - Schusser, Sebastian A1 - Jeitner, C. A1 - Breuer, L. A1 - Wagner, P. A1 - Poghossian, Arshak A1 - Förster, Arnold A1 - Mang, Thomas A1 - Schöning, Michael Josef T1 - Microfluidic chip with integrated microvalves based on temperature- and pH-responsive hydrogel thin films JF - Physica Status Solidi (a) N2 - Two types of microvalves based on temperature-responsive poly(N-isopropylacrylamide) (PNIPAAm) and pH-responsive poly(sodium acrylate) (PSA) hydrogel films have been developed and tested. The PNIPAAm and PSA hydrogel films were prepared by means of in situ photopolymerization directly inside the fluidic channel of a microfluidic chip fabricated by combining Si and SU-8 technologies. The swelling/shrinking properties and height changes of the PNIPAAm and PSA films inside the fluidic channel were studied at temperatures of deionized water from 14 to 36 °C and different pH values (pH 3–12) of Titrisol buffer, respectively. Additionally, in separate experiments, the lower critical solution temperature (LCST) of the PNIPAAm hydrogel was investigated by means of a differential scanning calorimetry (DSC) and a surface plasmon resonance (SPR) method. Mass-flow measurements have shown the feasibility of the prepared hydrogel films to work as an on-chip integrated temperature- or pH-responsive microvalve capable to switch the flow channel on/off. Y1 - 2012 U6 - http://dx.doi.org/10.1002/pssa.201100763 SN - 1862-6319 VL - 209 IS - 5 SP - 839 EP - 845 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Aggarwal, P. A1 - Dhiman, S. A1 - Kumar, G. A1 - Scherer, Ulrich W. A1 - Singla, M. L. A1 - Srivastava, A. T1 - Optical study of poly(ethyleneterephthalate) modified by different ionizing radiation dose JF - Indian Journal of Pure and Applied Physics N2 - Thin films of poly(ethyleneterephthalate) [PET]were exposed to radiation dose ranging from 10 to 30 kGy by using gamma rays in the range 12.8-177.8 MGy using swift light ions of hydrogen. There was no effect of the radiation dose on the optical behaviour of PET as a result of exposure to radiation dose up to 30 kGy brought about by gamma rays but a significant decrease in the optical band gap values was observed when PET was exposed to swift light ions of hydrogen. The data obtained are discussed in terms of optical studies carried out on PET using swift heavy ions. Y1 - 2012 SN - 0019-5596 VL - 50 IS - 2 SP - 129 EP - 132 ER - TY - JOUR A1 - Werner, Frederik A1 - Groebel, Simone A1 - Krumbe, Christoph A1 - Wagner, Torsten A1 - Selmer, Thorsten A1 - Yoshinobu, Tatsuo A1 - Baumann, Marcus A1 - Schöning, Michael Josef T1 - Nutrient concentration-sensitive microorganism-based biosensor JF - Physica Status Solidi (a) Y1 - 2012 U6 - http://dx.doi.org/10.1002/pssa.201100801 SN - 1862-6319 VL - 209 IS - 5 SP - 900 EP - 904 PB - Wiley-VCH CY - Weinheim ER - TY - CHAP A1 - Feuerriegel, Uwe A1 - Wittenhorst, Simon A1 - Hoffmann, Ulrich A1 - Pook, Michael T1 - Simulation von Wärmeübertragungsprozessen T2 - Tagungsband zur AALE-Tagung 2012 : 9. Fachkonferenz Y1 - 2012 SN - 978-3-8356-3305-6 N1 - AALE 2012 SP - 127 EP - 136 PB - Oldenbourg Industrieverlag CY - München ER - TY - RPRT A1 - Vaeßen, Christiane A1 - Ohme, H. A1 - Manderscheid, D. T1 - Endbericht Projekt Immotherm : Vorhabensbezeichnung: KMU-innovativ-Verbundvorhaben "Einsatz immobilisierter Mikroorganismen zur Entölung und Entsalzung von Kondensatwasser bei hohen Prozesstemperaturen" : Laufzeit des Vorhabens: 01.03.2009-31.08.2011 : Förderkennzeichen: 01LY0816A, 01LY0816B, 01LY0816C Y1 - 2012 ER - TY - JOUR A1 - Borgmeier, Claudia A1 - Bongaerts, Johannes A1 - Meinhardt, Friedhelm T1 - Genetic analysis of the Bacillus licheniformis degSU operon and the impact of regulatory mutations on protease production JF - Journal of biotechnology N2 - 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. KW - Marker-free mutagenesis KW - Extracellular enzymes KW - Uracil-phosphoribosyltransferase KW - Hypersecretion Y1 - 2012 U6 - http://dx.doi.org/10.1016/j.jbiotec.2012.02.011 SN - 1873-4863 (E-Journal); 0168-1656 (Print) VL - 159 IS - 1-2 SP - 12 EP - 20 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Schöning, Michael Josef A1 - Biselli, Manfred A1 - Selmer, Thorsten A1 - Öhlschläger, Peter A1 - Baumann, Marcus A1 - Förster, Arnold A1 - Poghossian, Arshak T1 - Forschung „zwischen“ den Disziplinen: das Institut für Nano- und Biotechnologien JF - Analytik news : das Online-Labormagazin für Labor und Analytik N2 - "Biologie trifft Mikroelektronik", das Motto des Instituts für Nano- und Biotechnologien (INB) an der FH Aachen, unterstreicht die zunehmende Bedeutung interdisziplinär geprägter Forschungsaktivitäten. Der thematische Zusammenschluss grundständiger Disziplinen, wie die Physik, Elektrotechnik, Chemie, Biologie sowie die Materialwissenschaften, lässt neue Forschungsgebiete entstehen, ein herausragendes Beispiel hierfür ist die Nanotechnologie: Hier werden neue Werkstoffe und Materialien entwickelt, einzelne Nanopartikel oder Moleküle und deren Wechselwirkung untersucht oder Schichtstrukturen im Nanometerbereich aufgebaut, die neue und vorher nicht bekannte Eigenschaften hervorbringen. Vor diesem Hintergrund bündelt das im Jahre 2006 gegründete INB die an der FH Aachen vorhandenen Kompetenzen von derzeit insgesamt sieben Laboratorien auf den Gebieten der Halbleitertechnik und Nanoelektronik, Nanostrukturen und DNA-Sensorik, der Chemo- und Biosensorik, der Enzymtechnologie, der Mikrobiologie und Pflanzenbiotechnologie, der Zellkulturtechnik, sowie der Roten Biotechnologie synergetisch. In der Nano- und Biotechnologie steckt außergewöhnliches Potenzial! Nicht zuletzt deshalb stellen sich die Forscher der Herausforderung, in diesem Bereich gemeinsam zu forschen und Schnittstellen zu nutzen, um so bei der Gestaltung neuartiger Ideen und Produkte mitzuwirken, die zukünftig unser alltägliches Leben verändern werden. Im Folgenden werden die verschiedenen Forschungsbereiche kurz zusammenfassend vorgestellt und vorhandene Interaktionen anhand von exemplarisch ausgewählten, aktuellen Forschungsprojekten skizziert. Y1 - 2012 VL - Publ. online PB - Dr. Beyer Internet-Beratung CY - Ober-Ramstadt ER - TY - JOUR A1 - Ribitsch, D. A1 - Heumann, S. A1 - Karl, W. A1 - Gerlach, J. A1 - Leber, R. A1 - Birner-Gruenberger, R. A1 - Gruber, K. A1 - Eiteljoerg, I. A1 - Remler, P. A1 - Siegert, Petra A1 - Lange, J. A1 - Maurer, Karl-Heinz A1 - Berg, G. A1 - Guebitz, G. M. A1 - Schwab, H. T1 - Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli JF - Journal of biotechnology N2 - 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. KW - Alginate beads KW - Stenotrophomonas maltophilia KW - Detergent protease Y1 - 2012 U6 - http://dx.doi.org/10.1016/j.jbiotec.2011.09.025 SN - 1873-4863 (E-Journal); 0168-1656 (Print) VL - 157 IS - 1 SP - 140 EP - 147 PB - Elsevier CY - Amsterdam ER - TY - PAT A1 - Maurer, Karl-Heinz A1 - O'Connell, Timothy A1 - Siegert, Petra A1 - Weber, Thomas A1 - Tondera, Susanne A1 - Hellmuth, Hendrik T1 - Flüssige Tensidzubereitung enthaltend Lipase und Phosphonat [Offenlegungsschrift] T1 - Liquid surfactant preparation containing lipase and phosphonate [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 22 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Merkel, Marion A1 - Hellmuth, Hendrik A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz T1 - Stabilisierte flüssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierenden Komponente, die eine Phenylalkyldicarbonsäure umfasst) [Offenlegungsschrift] T1 - Stabilized liquid tenside preparation comprising enzymes (using a component that stabilizes the hydrolytic enzyme and includes a phenylalkyldicarboxylic acid) [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 15 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Merkel, Marion A1 - Hellmuth, Hendrik A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz T1 - Stabilisierte flüssige enzymhaltige Tensidzubereitung (durch den Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine mehrfach substituierte Benzolcarbonsäure umfasst, die an mindestens zwei Kohlenstoffatomen des Benzolrestes eine Carboxylgruppe aufweist) [Offenlegungsschrift] T1 - Stabilized liquid tenside preparation comprising enzymes (a component comprising a multiply substituted benzyl carboxylic acid comprising a carboxyl group on at least two carbon atoms of the benzyl radical is used for stabilizing the hydrolytic enzyme) [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 16 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Merkel, Marion A1 - Hellmuth, Hendrik A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz T1 - Stabilisierte flüssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Phthaloylglutaminsäure und/oder eine Phthaloylasparaginsäure umfasst) [Offenlegungsschrift] T1 - Stabilized liquid tenside preparation comprising enzymes (a component comprising a phthaloyl glutamine acid and/or a phthaloyl asparagine acid is used for stablizing the hydrolytic enzyme) [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 16 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Merkel, Marion A1 - Hellmuth, Hendrik A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz T1 - Stabilisierte flüssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Aminophthalsäure umfasst) [Offenlegungsschrift] T1 - Stabilized liquid tenside preparation comprising enzymes (a component comprising an aminophthalic acid is used for stabilizing the hydrolytic enzyme) [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 16 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Merkel, Marion A1 - Hellmuth, Hendrik A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz T1 - Stabilisierte flüssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Oligoamino-biphenyl-oligocarbonsäure umfasst) [Offenlegungsschrift] T1 - Stabilized liquid tenside preparation comprising enzymes (a component comprising an oligoamino-biphenyl-oligocarboxylic acid is used for stabilizing the hydrolytic enzyme) [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 16 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Merkel, Marion A1 - Hellmuth, Hendrik A1 - O'Connell, Timothy A1 - Maurer, Karl-Heinz T1 - Stabilisierte flüssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die ein Monosaccharidglycerat umfasst) [Offenlegungsschrift] T1 - Stabilized liquid enzyme-containing surfactant preparation (using a component which comprises a monosaccharide glycerate and which stabilizes the hydrolytic enzyme) [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 17 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - Siegert, Petra A1 - Schwaneberg, Ulrich A1 - Martinez Moya, Ronny A1 - Merkel, Marion A1 - Spitz, Astrid A1 - Wieland, Susanne A1 - Hellmuth, Hendrik A1 - Maurer, Karl-Heinz T1 - Leistungsverbesserte Proteasevariante [Offenlegungsschrift] T1 - Performance-enhanced protease variant [Europäische Patentanmeldung / Internationale Patentanmeldung] Y1 - 2012 SP - 1 EP - 29 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - JOUR A1 - Henken, F. E. A1 - Oosterhuis, K. A1 - Öhlschläger, Peter A1 - Bosch, L. A1 - Hooijberg, E. A1 - Haanen, J. B. A. G. A1 - Steenbergen, R. D. M. T1 - Preclinical safety evaluation of DNA vaccines encoding modified HPV16 E6 and E7 JF - Vaccine N2 - Persistent infection with high-risk human papillomaviruses (hrHPV) can result in the formation of anogenital cancers. As hrHPV proteins E6 and E7 are required for cancer initiation and maintenance, they are ideal targets for immunotherapeutic interventions. Previously, we have described the development of DNA vaccines for the induction of HPV16 E6 and E7 specific T cell immunity. These vaccines consist of ‘gene-shuffled’ (SH) versions of HPV16 E6 and E7 that were fused to Tetanus Toxin Fragment C domain 1 (TTFC) and were named TTFC-E6SH and TTFC-E7SH. Gene-shuffling was performed to avoid the risk of inducing malignant transformation at the vaccination site. Here, we describe the preclinical safety evaluation of these candidate vaccines by analysis of their transforming capacity in vitro using established murine fibroblasts (NIH 3T3 cells) and primary human foreskin keratinocytes (HFKs). We demonstrate that neither ectopic expression of TTFC-E6SH and TTFC-E7SH alone or in combination enabled NIH 3T3 cells to form colonies in soft agar. In contrast, expression of HPV16 E6WT and E7WT alone or in combination resulted in effective transformation. Similarly, retroviral transduction of HFKs from three independent donors with both TTFC-E6SH and TTFC-E7SH alone or in combination did not show any signs of immortalization. In contrast, the combined expression of E6WT and E7WT induced immortalization in HFKs from all donors. Based on these results we consider it justified to proceed to clinical evaluation of DNA vaccines encoding TTFC-E6SH and TTFC-E7SH in patients with HPV16 associated (pre)malignancies. Y1 - 2012 U6 - http://dx.doi.org/10.1016/j.vaccine.2012.04.013 SN - 0264-410X VL - 30 IS - 28 SP - 4259 EP - 4266 PB - Elsevier CY - Amsterdam ER -