@article{ScheerWolf2013, author = {Scheer, Nico and Wolf, C. Roland}, title = {Xenobiotic receptor humanized mice and their utility}, series = {Drug Metabolism Reviews}, journal = {Drug Metabolism Reviews}, number = {1}, publisher = {Taylor \& Francis}, address = {London}, issn = {1097-9883}, doi = {10.3109/03602532.2012.738687}, pages = {110 -- 121}, year = {2013}, language = {en} } @article{HuckSchiffelsHerreraetal.2013, author = {Huck, Christina and Schiffels, Johannes and Herrera, Cony N. and Schelden, Maximilian and Selmer, Thorsten and Poghossian, Arshak and Baumann, Marcus and Wagner, Patrick and Sch{\"o}ning, Michael Josef}, title = {Metabolic responses of Escherichia coli upon glucose pulses captured by a capacitive field-effect sensor}, series = {Physica Status Solidi (A)}, volume = {210}, journal = {Physica Status Solidi (A)}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0031-8965}, doi = {10.1002/pssa.201200900}, pages = {926 -- 931}, year = {2013}, abstract = {Living cells are complex biological systems transforming metabolites taken up from the surrounding medium. Monitoring the responses of such cells to certain substrate concentrations is a challenging task and offers possibilities to gain insight into the vitality of a community influenced by the growth environment. Cell-based sensors represent a promising platform for monitoring the metabolic activity and thus, the "welfare" of relevant organisms. In the present study, metabolic responses of the model bacterium Escherichia coli in suspension, layered onto a capacitive field-effect structure, were examined to pulses of glucose in the concentration range between 0.05 and 2 mM. It was found that acidification of the surrounding medium takes place immediately after glucose addition and follows Michaelis-Menten kinetic behavior as a function of the glucose concentration. In future, the presented setup can, therefore, be used to study substrate specificities on the enzymatic level and may as well be used to perform investigations of more complex metabolic responses. Conclusions and perspectives highlighting this system are discussed.}, language = {en} } @article{BaeckerRakowskiPoghossianetal.2013, author = {B{\"a}cker, Matthias and Rakowski, D. and Poghossian, Arshak and Biselli, Manfred and Wagner, Patrick and Sch{\"o}ning, Michael Josef}, title = {Chip-based amperometric enzyme sensor system for monitoring of bioprocesses by flow-injection analysis}, series = {Journal of Biotechnology}, volume = {163}, journal = {Journal of Biotechnology}, number = {4}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0168-1656}, doi = {10.1016/j.jbiotec.2012.03.014}, pages = {371 -- 376}, year = {2013}, abstract = {A microfluidic chip integrating amperometric enzyme sensors for the detection of glucose, glutamate and glutamine in cell-culture fermentation processes has been developed. The enzymes glucose oxidase, glutamate oxidase and glutaminase were immobilized by means of cross-linking with glutaraldehyde on platinum thin-film electrodes integrated within a microfluidic channel. The biosensor chip was coupled to a flow-injection analysis system for electrochemical characterization of the sensors. The sensors have been characterized in terms of sensitivity, linear working range and detection limit. The sensitivity evaluated from the respective peak areas was 1.47, 3.68 and 0.28 μAs/mM for the glucose, glutamate and glutamine sensor, respectively. The calibration curves were linear up to a concentration of 20 mM glucose and glutamine and up to 10 mM for glutamate. The lower detection limit amounted to be 0.05 mM for the glucose and glutamate sensor, respectively, and 0.1 mM for the glutamine sensor. Experiments in cell-culture medium have demonstrated a good correlation between the glutamate, glutamine and glucose concentrations measured with the chip-based biosensors in a differential-mode and the commercially available instrumentation. The obtained results demonstrate the feasibility of the realized microfluidic biosensor chip for monitoring of bioprocesses.}, language = {en} } @article{LeursMezoOehlschlaegeretal.2012, author = {Leurs, Ulrike and Mezo, Gabor and {\"O}hlschl{\"a}ger, Peter and Orban, Erika and Marquard, Andrea and Manea, Marilena}, title = {Design, synthesis, in vitro stability and cytostatic effect of multifunctional anticancer drug-bioconjugates containing GnRH-III as a targeting moiety}, series = {Peptide Science}, volume = {98}, journal = {Peptide Science}, number = {1}, publisher = {Wiley}, address = {New York, NY}, issn = {1097-0282}, doi = {10.1002/bip.21640}, pages = {1 -- 10}, year = {2012}, abstract = {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.}, language = {en} } @article{BaeckerRaueSchusseretal.2012, author = {B{\"a}cker, Matthias and Raue, Markus and Schusser, Sebastian and Jeitner, C. and Breuer, L. and Wagner, P. and Poghossian, Arshak and F{\"o}rster, Arnold and Mang, Thomas and Sch{\"o}ning, Michael Josef}, title = {Microfluidic chip with integrated microvalves based on temperature- and pH-responsive hydrogel thin films}, series = {Physica Status Solidi (a)}, volume = {209}, journal = {Physica Status Solidi (a)}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201100763}, pages = {839 -- 845}, year = {2012}, abstract = {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.}, language = {en} } @article{AggarwalDhimanKumaretal.2012, author = {Aggarwal, P. and Dhiman, S. and Kumar, G. and Scherer, Ulrich W. and Singla, M. L. and Srivastava, A.}, title = {Optical study of poly(ethyleneterephthalate) modified by different ionizing radiation dose}, series = {Indian Journal of Pure and Applied Physics}, volume = {50}, journal = {Indian Journal of Pure and Applied Physics}, number = {2}, issn = {0019-5596}, pages = {129 -- 132}, year = {2012}, abstract = {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.}, language = {en} } @article{WernerGroebelKrumbeetal.2012, author = {Werner, Frederik and Groebel, Simone and Krumbe, Christoph and Wagner, Torsten and Selmer, Thorsten and Yoshinobu, Tatsuo and Baumann, Marcus and Sch{\"o}ning, Michael Josef}, title = {Nutrient concentration-sensitive microorganism-based biosensor}, series = {Physica Status Solidi (a)}, volume = {209}, journal = {Physica Status Solidi (a)}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201100801}, pages = {900 -- 904}, year = {2012}, language = {en} } @inproceedings{FeuerriegelWittenhorstHoffmannetal.2012, author = {Feuerriegel, Uwe and Wittenhorst, Simon and Hoffmann, Ulrich and Pook, Michael}, title = {Simulation von W{\"a}rme{\"u}bertragungsprozessen}, series = {Tagungsband zur AALE-Tagung 2012 : 9. Fachkonferenz}, booktitle = {Tagungsband zur AALE-Tagung 2012 : 9. Fachkonferenz}, publisher = {Oldenbourg Industrieverlag}, address = {M{\"u}nchen}, isbn = {978-3-8356-3305-6}, pages = {127 -- 136}, year = {2012}, language = {de} } @techreport{VaessenOhmeManderscheid2012, author = {Vaeßen, Christiane and Ohme, H. and Manderscheid, D.}, title = {Endbericht Projekt Immotherm : Vorhabensbezeichnung: KMU-innovativ-Verbundvorhaben "Einsatz immobilisierter Mikroorganismen zur Ent{\"o}lung und Entsalzung von Kondensatwasser bei hohen Prozesstemperaturen" : Laufzeit des Vorhabens: 01.03.2009-31.08.2011 : F{\"o}rderkennzeichen: 01LY0816A, 01LY0816B, 01LY0816C}, pages = {71 S. : zahlr. Ill. u. graph. Darst.}, year = {2012}, language = {de} } @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{SchoeningBiselliSelmeretal.2012, author = {Sch{\"o}ning, Michael Josef and Biselli, Manfred and Selmer, Thorsten and {\"O}hlschl{\"a}ger, Peter and Baumann, Marcus and F{\"o}rster, Arnold and Poghossian, Arshak}, title = {Forschung „zwischen" den Disziplinen: das Institut f{\"u}r Nano- und Biotechnologien}, series = {Analytik news : das Online-Labormagazin f{\"u}r Labor und Analytik}, volume = {Publ. online}, journal = {Analytik news : das Online-Labormagazin f{\"u}r Labor und Analytik}, publisher = {Dr. Beyer Internet-Beratung}, address = {Ober-Ramstadt}, pages = {11 Seiten}, year = {2012}, abstract = {"Biologie trifft Mikroelektronik", das Motto des Instituts f{\"u}r Nano- und Biotechnologien (INB) an der FH Aachen, unterstreicht die zunehmende Bedeutung interdisziplin{\"a}r gepr{\"a}gter Forschungsaktivit{\"a}ten. Der thematische Zusammenschluss grundst{\"a}ndiger Disziplinen, wie die Physik, Elektrotechnik, Chemie, Biologie sowie die Materialwissenschaften, l{\"a}sst neue Forschungsgebiete entstehen, ein herausragendes Beispiel hierf{\"u}r ist die Nanotechnologie: Hier werden neue Werkstoffe und Materialien entwickelt, einzelne Nanopartikel oder Molek{\"u}le und deren Wechselwirkung untersucht oder Schichtstrukturen im Nanometerbereich aufgebaut, die neue und vorher nicht bekannte Eigenschaften hervorbringen. Vor diesem Hintergrund b{\"u}ndelt das im Jahre 2006 gegr{\"u}ndete 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 außergew{\"o}hnliches 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 zuk{\"u}nftig unser allt{\"a}gliches Leben ver{\"a}ndern werden. Im Folgenden werden die verschiedenen Forschungsbereiche kurz zusammenfassend vorgestellt und vorhandene Interaktionen anhand von exemplarisch ausgew{\"a}hlten, aktuellen Forschungsprojekten skizziert.}, language = {de} } @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} } @misc{MaurerO'ConnellSiegertetal.2012, author = {Maurer, Karl-Heinz and O'Connell, Timothy and Siegert, Petra and Weber, Thomas and Tondera, Susanne and Hellmuth, Hendrik}, title = {Fl{\"u}ssige Tensidzubereitung enthaltend Lipase und Phosphonat [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 22}, year = {2012}, language = {de} } @misc{SiegertMerkelHellmuthetal.2012, author = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz}, title = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierenden Komponente, die eine Phenylalkyldicarbons{\"a}ure umfasst) [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 15}, year = {2012}, language = {de} } @misc{SiegertMerkelHellmuthetal.2012, author = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz}, title = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (durch den Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine mehrfach substituierte Benzolcarbons{\"a}ure umfasst, die an mindestens zwei Kohlenstoffatomen des Benzolrestes eine Carboxylgruppe aufweist) [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 16}, year = {2012}, language = {de} } @misc{SiegertMerkelHellmuthetal.2012, author = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz}, title = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Phthaloylglutamins{\"a}ure und/oder eine Phthaloylasparagins{\"a}ure umfasst) [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 16}, year = {2012}, language = {de} } @misc{SiegertMerkelHellmuthetal.2012, author = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz}, title = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Aminophthals{\"a}ure umfasst) [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 16}, year = {2012}, language = {de} } @misc{SiegertMerkelHellmuthetal.2012, author = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz}, title = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die eine Oligoamino-biphenyl-oligocarbons{\"a}ure umfasst) [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 16}, year = {2012}, language = {de} } @misc{SiegertMerkelHellmuthetal.2012, author = {Siegert, Petra and Merkel, Marion and Hellmuth, Hendrik and O'Connell, Timothy and Maurer, Karl-Heinz}, title = {Stabilisierte fl{\"u}ssige enzymhaltige Tensidzubereitung (Einsatz einer das hydrolytische Enzym stabilisierende Komponente, die ein Monosaccharidglycerat umfasst) [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 17}, year = {2012}, language = {de} } @misc{SiegertSchwanebergMartinezMoyaetal.2012, author = {Siegert, Petra and Schwaneberg, Ulrich and Martinez Moya, Ronny and Merkel, Marion and Spitz, Astrid and Wieland, Susanne and Hellmuth, Hendrik and Maurer, Karl-Heinz}, title = {Leistungsverbesserte Proteasevariante [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 29}, year = {2012}, language = {de} }