@article{BiselliVanderPolJokschetal.1994, author = {Biselli, Manfred and Van der Pol, Jens J. and Joksch, B. and Spohn, U.}, title = {On-line monitoring and control of glucose, glutamine, lactate and ammonium during a high-cell-density cultivation of hybridoma cells / van der Pol, Jens J. ; Joksch, B. ; Spohn, U. ; Biselli, M. ; Wandrey, C.}, series = {Proceedings of the sixth international meeting of the Japanese Association for Animal Cell Technology [JAACT 93]: Nagoya, Japan, November 9 - 12, 1993 / ed. by T. Kobayashi}, journal = {Proceedings of the sixth international meeting of the Japanese Association for Animal Cell Technology [JAACT 93]: Nagoya, Japan, November 9 - 12, 1993 / ed. by T. Kobayashi}, publisher = {Springer Netherland}, address = {Berlin}, isbn = {0-7923-3156-7}, pages = {167 -- 170}, year = {1994}, language = {en} } @article{BiselliVanderPolSpohnetal.1994, author = {Biselli, Manfred and Van der Pol, Jens J. and Spohn, Uwe and Eberhardt, Rolf}, title = {On-line monitoring of an animal cell culture with multi-channel flow injection analysis / van der Pol, Jens J.; Spohn, Uwe ; Eberhardt, Rolf ; G{\"a}tgens, Jochen ; Biselli, Manfred ; Wandrey, Christian ; Tramper, Johannes}, series = {Journal of Biotechnology. 37 (1994), H. 3}, journal = {Journal of Biotechnology. 37 (1994), H. 3}, isbn = {0168-1656}, pages = {253 -- 264}, year = {1994}, language = {en} } @inproceedings{DeterdingTippkoetterUlber2006, author = {Deterding, A. and Tippk{\"o}tter, Nils and Ulber, Roland}, title = {Online-Essigs{\"a}ureanalytik in Fermentationsbr{\"u}hen mittels Fließdiffusionstechnik (FDT)}, series = {Technische Systeme f{\"u}r Biotechnologie und Umwelt : 13. Heiligenst{\"a}dter Kolloquium, Heilbad Heiligenstadt, 25.09. - 27.09.2006}, booktitle = {Technische Systeme f{\"u}r Biotechnologie und Umwelt : 13. Heiligenst{\"a}dter Kolloquium, Heilbad Heiligenstadt, 25.09. - 27.09.2006}, editor = {Beckmann, Dieter}, address = {Heiligenstadt}, organization = {Institut f{\"u}r Bioprozeß- und Analysenmeßtechnik}, isbn = {978-3-00-018621-9}, pages = {273 -- 280}, year = {2006}, language = {de} } @article{BiselliMachnikWandrey1996, author = {Biselli, Manfred and Machnik, M. and Wandrey, C.}, title = {Online-Immunoanalytik bei der kontinuierlichen Fermentation von Hybridomazellen / Machnik, M. ; Biselli, M. ; Wandrey, C.}, series = {BIO WORLD. 1 (1996), H. 3}, journal = {BIO WORLD. 1 (1996), H. 3}, isbn = {1424-8514}, pages = {12 -- 15}, year = {1996}, language = {de} } @article{WagnerBegingRotteretal.2007, author = {Wagner, Torsten and Beging, Stefan and Rotter, L. and Poghossian, Arshak and Biselli, Manfred and Zang, Werner and Sch{\"o}ning, Michael Josef}, title = {Online-Messsysteme f{\"u}r die automatisierte Charakterisierung von feldeffektbasierten Biosensoren}, series = {8. Dresdner Sensor-Symposium : Sensoren f{\"u}r Umwelt, Klima und Sicherheit, Biosensoren und Biosysteme, Sensoren und Sensorsysteme f{\"u}r die Prozesstechnik, Trends in der Sensortechnik, Materialentwicklung f{\"u}r die Sensorik; 8. Dresdner Sensor-Symposium, 10. - 12. Dezember 2007, Dresden / Gerald Gerlach ... (Hg.)}, journal = {8. Dresdner Sensor-Symposium : Sensoren f{\"u}r Umwelt, Klima und Sicherheit, Biosensoren und Biosysteme, Sensoren und Sensorsysteme f{\"u}r die Prozesstechnik, Trends in der Sensortechnik, Materialentwicklung f{\"u}r die Sensorik; 8. Dresdner Sensor-Symposium, 10. - 12. Dezember 2007, Dresden / Gerald Gerlach ... (Hg.)}, publisher = {TUDpress, Verl. der Wissenschaften}, address = {Dresden}, isbn = {978-3-940046-45-1}, pages = {257 -- 260}, year = {2007}, language = {de} } @article{HoughNalwalkDingetal.2015, author = {Hough, Lindsay B. and Nalwalk, Julia W. and Ding, Xinxin and Scheer, Nico}, title = {Opioid Analgesia in P450 Gene Cluster Knockout Mice: A Search for Analgesia-Relevant Isoforms}, series = {Drug Metabolism and Disposition}, volume = {43}, journal = {Drug Metabolism and Disposition}, number = {9}, issn = {1521-009x}, doi = {10.1124/dmd.115.065490}, pages = {1326 -- 1330}, year = {2015}, language = {en} } @article{NiedermeierPennerUsherovichetal.2023, author = {Niedermeier, Jana and Penner, Crystal and Usherovich, Samuel and B{\´e}langer-Champagne, Camille and Paulßen, Elisabeth and Hoehr, Cornelia}, title = {Optical Fibers as Dosimeter Detectors for Mixed Proton/Neutron Fields - A Biological Dosimeter}, series = {electronics}, volume = {12}, journal = {electronics}, number = {2}, publisher = {MDPI}, address = {Basel}, issn = {2079-9292}, doi = {10.3390/electronics12020324}, pages = {11 Seiten}, year = {2023}, abstract = {In recent years, proton therapy has gained importance as a cancer treatment modality due to its conformality with the tumor and the sparing of healthy tissue. However, in the interaction of the protons with the beam line elements and patient tissues, potentially harmful secondary neutrons are always generated. To ensure that this neutron dose is as low as possible, treatment plans could be created to also account for and minimize the neutron dose. To monitor such a treatment plan, a compact, easy to use, and inexpensive dosimeter must be developed that not only measures the physical dose, but which can also distinguish between proton and neutron contributions. To that end, plastic optical fibers with scintillation materials (Gd₂O₂S:Tb, Gd₂O₂S:Eu, and YVO₄:Eu) were irradiated with protons and neutrons. It was confirmed that sensors with different scintillation materials have different sensitivities to protons and neutrons. A combination of these three scintillators can be used to build a detector array to create a biological dosimeter.}, language = {en} } @article{SrivastavaSinghAggarwaletal.2010, author = {Srivastava, Alok and Singh, Virendra and Aggarwal, Pranav and Schneeweiss, F. and Scherer, Ulrich W. and Friedrich, W.}, title = {Optical studies of insulating polymers for radiation dose monitoring}, series = {Indian Journal of Pure \& Applied Physics}, volume = {48}, journal = {Indian Journal of Pure \& Applied Physics}, number = {11}, isbn = {0019-5596}, pages = {782 -- 786}, year = {2010}, language = {en} } @article{AggarwalDhimanKumaretal.2012, author = {Aggarwal, Pranav and Dhiman, Shashi K. and Kumar, G. and Scherer, Ulrich W. and Singla, M. L. and Srivastava, Alok}, 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{JerominAlbertz1992, author = {Jeromin, G{\"u}nter Erich and Albertz, Michael}, title = {Optically active \&\#945;-acetoxycarboxylic acids and \&\#945;-hydroxycarboxylic acids by enzyme-aided syntheses}, series = {Journal f{\"u}r Praktische Chemie / Chemiker-Zeitung. 334 (1992), H. 6}, journal = {Journal f{\"u}r Praktische Chemie / Chemiker-Zeitung. 334 (1992), H. 6}, isbn = {1436-9966}, pages = {526 -- 528}, year = {1992}, language = {en} } @book{KotterLintz1987, author = {Kotter, Michael and Lintz, Hans-G{\"u}nther}, title = {Optimierung der Katalysatorzusammensetzung im Fall der selektiven Reduktion von Stickoxiden durch Ammoniak bei instation{\"a}rer Reaktionsf{\"u}hrung in einem weiten Temperaturbereich. - (Forschungsbericht KfK-PEF ; 33)}, publisher = {Kernforschungszentrum}, address = {Karlsruhe}, pages = {26 S. : graph. Darst.}, year = {1987}, language = {de} } @misc{WollnyStadtmuellerTippkoetteretal.2012, author = {Wollny, S. and Stadtm{\"u}ller, R. and Tippk{\"o}tter, Nils and Oster, J. and Kampeis, P. and Ulber, Roland}, title = {Optimierung der selektiven Aufarbeitung von Proteinen mit Aptamer-funktionalisierten Magnetpartikeln}, series = {Chemie Ingenieur Technik}, volume = {84}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.201250031}, pages = {1203}, year = {2012}, abstract = {Die Herstellung pharmakologisch relevanter Proteine durch Mikroorganismen f{\"u}hrt eine mehrstufige Aufarbeitung mit sich. Durch die Verwendung von Aptameren, kurzen einzelstr{\"a}ngigen DNA- oder RNA-Oligonukleotiden immobilisiert auf funktionalisierten, wiederverwendbaren Magnetpartikeln, k{\"o}nnen mehrere dieser Abtrennungsoperationen kombiniert und damit die Prozesskosten minimiert werden. Aufgrund der definierten dreidimensionalen Struktur k{\"o}nnen Aptamere kleine organische Molek{\"u}le hochspezifisch binden. Im vorgestellten Projekt wird die Aufarbeitung von His6-GFP als Modellprotein mithilfe der mit Aptamer funktionalisierten Magnetpartikel durchgef{\"u}hrt. In bisherigen Versuchen wurde die Bindung von Aptameren auf den magnetischen Partikeln sowie die Bindung des Modellproteins GFP auf den Partikeln optimiert. Des Weiteren wurden mehrere Strategien zur Elution des GFPs von den Partikeln verfolgt, um den Proteinertrag zu maximieren und die Partikel rezyklieren zu k{\"o}nnen. Die Untersuchung unspezifischer Bindungen von Zelltr{\"u}mmern und Proteinen an die Magnetpartikel wurde mithilfe eines konfokalen Laser-Scanning-Mikroskops durchgef{\"u}hrt.}, language = {de} } @misc{ThielTippkoetterMuffleretal.2012, author = {Thiel, A. and Tippk{\"o}tter, Nils and Muffler, K. and Ruf, F. and Sohling, U. and Ulber, Roland}, title = {Optimierung der Wertsch{\"o}pfungskette bei der Aufarbeitung von Rapsschrot mit Zeolithen}, series = {Chemie Ingenieur Technik}, volume = {84}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.201250028}, pages = {1191 -- 1192}, year = {2012}, abstract = {Im vom BMELV/FNR gef{\"o}rderten SynRg-Projekt wurde unter anderem Rapsschrot untersucht, um Polyphenole zu isolieren und aufzureinigen. Diese sollen anschließend als Basisbausteine f{\"u}r Polymere dienen und ihnen neuartige Eigenschaften verleihen. Derzeit wird an der Polyphenolextraktion gearbeitet, da bei organischen oder w{\"a}ssrigen Extraktionsprozessen {\"u}berwiegend Sinapin, ein Cholinester der Sinapins{\"a}ure, vorliegt und dieses nicht f{\"u}r die Polymerbildung eingesetzt werden kann. F{\"u}r die im Fokus stehende Sinapins{\"a}ure wird deshalb eine simultane Extraktion und enzymatische oder chemische Hydrolyse von Sinapin zu Sinapins{\"a}ure durchgef{\"u}hrt. Durch die Hydrolyse konnte die Sinapins{\"a}ureausbeute bereits um den Faktor 6,2 auf 15,8 mg g⁻¹ gegen{\"u}ber einer reinw{\"a}ssrigen Extraktion gesteigert werden. F{\"u}r die Aufreinigung des an Sinapins{\"a}ure reichen Extrakts erfolgt anschließend ein adsorptiver Aufarbeitungsschritt, bei dem Zeolithe zum Einsatz kommen. Mit diesem Material ist es m{\"o}glich, die Sinapins{\"a}ure quantitativ zu adsorbieren und sp{\"a}ter mit 70 \%igem Ethanol bei 60 °C zu desorbieren. Bei den Adsorbern handelt es sich um b-Zeolithe von der S{\"u}d-Chemie AG.}, language = {de} } @misc{TippkoetterDuweRaisetal.2014, author = {Tippk{\"o}tter, Nils and Duwe, Anna and Rais, Dominik and Zibek, Susanne and Zorn, H.}, title = {Optimierung und Scale-up der enzymatischen Hydrolyse inkl. Ligninabbau}, series = {Chemie Ingenieur Technik}, volume = {86}, journal = {Chemie Ingenieur Technik}, number = {9}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.201450287}, pages = {1515}, year = {2014}, abstract = {Prim{\"a}re Ziele der Hydrolyse pflanzlicher nachwachsender Rohstoffe sind m{\"o}glichst hohe Zuckerkonzentrationen f{\"u}r nachfolgende Fermentationen und eine Maximierung der Produktivit{\"a}t. Zur Optimierung dieser Prozesse wird Organosolv-aufgeschlossene Buchenholz-Cellulose verwendet. Die Hydrolyse des Faserstoffes erfolgt mithilfe von Novozymes CTec2-Enzymen. Die Hydrolysen konnten durch neue R{\"u}hrerelemente auf einen Maßstab von 1000 L {\"u}bertragen werden. Dabei konnten maximale Ausbeuten (g Glucose g -1 Glucose im Faserstoff) bis 81 g g - 1 und Konzentrationen von 152 g L -1 erreicht werden. Zurzeit k{\"o}nnen unter Einsatz eines Feststoffreaktors Cellulosefasern in einer Konzentration bis 400 g L -1 enzymatisch hydrolysiert werden. Die cellulolytischen Enzyme stoßen bei hohen Feststoffkonzentrationen an ihre Grenzen. Mit steigendem Feststoffgehalt nimmt die Hydrolyseausbeute ab. Ein Ansatz zur Steigerung der Effizienz ist der Einsatz ligninolytischer Enzyme, die Ligninreste an der Organosolv-Cellulose aufschließen k{\"o}nnen. Eine solche Verbesserung der Zug{\"a}nglichkeit f{\"u}r cellulolytische Enzyme an ihr Substrat wurde durch Kultur{\"u}berst{\"a}nde verschiedener ligninolytischer Pilze erreicht. Mit Kultur{\"u}berst{\"a}nden von Stereum sp. sind Steigerungen der Glucoseausbeuten um bis zu 30 \% m{\"o}glich.}, language = {de} } @inproceedings{TippkoetterStueckmannWinkelmannetal.2007, author = {Tippk{\"o}tter, Nils and St{\"u}ckmann, H. and Winkelmann, G. and Noack, U. and Beutel, S. and Scheper, T. and Ulber, Roland}, title = {Optimisation of antibody-labelling of gold colloids for their application in an immunchromatographic assay for microcystin-LR}, series = {European BioPerspectives : celebrating the 25th DECHEMA annual convention of biotechnologists ; 30 May - 1 June 2007, Cologne, Germany ; book of abstracts ; abstracts, poster programme}, booktitle = {European BioPerspectives : celebrating the 25th DECHEMA annual convention of biotechnologists ; 30 May - 1 June 2007, Cologne, Germany ; book of abstracts ; abstracts, poster programme}, publisher = {Dechema}, address = {Frankfurt am Main}, pages = {126}, year = {2007}, language = {en} } @article{PilasYaziciSelmeretal.2017, author = {Pilas, Johanna and Yazici, Yasemen and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate}, series = {Electrochimica Acta}, volume = {251}, journal = {Electrochimica Acta}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0013-4686}, doi = {10.1016/j.electacta.2017.07.119}, pages = {256 -- 262}, year = {2017}, abstract = {The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4\% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.}, language = {en} } @article{PilasMarianoKeusgenetal.2015, author = {Pilas, Johanna and Mariano, K. and Keusgen, M. and Selmer, Thorsten and Sch{\"o}ning, Michael Josef}, title = {Optimization of an Enzyme-based Multi-parameter Biosensor for Monitoring Biogas Processes}, series = {Procedia Engineering}, volume = {120}, journal = {Procedia Engineering}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1877-7058}, doi = {10.1016/j.proeng.2015.08.702}, pages = {532 -- 535}, year = {2015}, language = {en} } @article{BiselliRolefDunkeretal.1994, author = {Biselli, Manfred and Rolef, G. and Dunker, R. and Wandrey, Christian}, title = {Optimization of antibody production in a fluidized bed bioreactor / Rolef, G. ; Biselli, M. ; Dunker, R. ; Wandrey, C.}, series = {Animal cell technology : products of today, prospects for tomorrow ; ESACT, European Society for Animal Cell Technology, the 12th meeting / Ed. R. E. Spier}, journal = {Animal cell technology : products of today, prospects for tomorrow ; ESACT, European Society for Animal Cell Technology, the 12th meeting / Ed. R. E. Spier}, publisher = {Butterworth-Heinemann}, address = {Oxford}, isbn = {0750618450}, pages = {481 -- 484}, year = {1994}, language = {en} } @article{PasteurTippkoetterKampeisetal.2014, author = {Pasteur, Aline and Tippk{\"o}tter, Nils and Kampeis, Percy and Ulber, Roland}, title = {Optimization of high gradient magnetic separation filter units for the purification of fermentation products}, series = {IEEE TRANSACTIONS ON MAGNETICS}, volume = {50}, journal = {IEEE TRANSACTIONS ON MAGNETICS}, number = {10}, publisher = {IEEE}, address = {New York, NY}, issn = {0018-9464}, doi = {10.1109/TMAG.2014.2325535}, pages = {Artikel 5000607}, year = {2014}, abstract = {High gradient magnetic separation (HGMS) has been established since the early 1970s. A more recent application of these systems is the use in bioprocesses. To integrate the HGMS in a fermentation process, it is necessary to optimize the separation matrix with regard to the magnetic separation characteristics and permeability of the non-magnetizable components of the fermentation broth. As part of the work presented here, a combined fluidic and magnetic force finite element model simulation was created using the software COMSOL Multiphysics and compared with separation experiments. Finally, as optimal lattice orientation of the separation matrix, a transversal rhombohedral arrangement was defined. The high suitability of the new filter matrix has been verified by separation experiments.}, language = {en} } @article{DegeringEggertPulsetal.2010, author = {Degering, Christian and Eggert, Thorsten and Puls, Michael and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Jaeger, Karl-Erich}, title = {Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides}, series = {Applied and environmental microbiology}, volume = {76}, journal = {Applied and environmental microbiology}, number = {19}, publisher = {American Society for Microbiology}, address = {Washington, DC}, issn = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)}, doi = {10.1128/AEM.01146-10}, pages = {6370 -- 6378}, year = {2010}, abstract = {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.}, language = {en} }