@misc{PothMonzonTippkoetteretal.2010, author = {Poth, S. and Monzon, M. and Tippk{\"o}tter, Nils and Ulber, Roland}, title = {Lignocellulose-Bioraffinerie: Simultane Verzuckerung und Fermentation}, series = {Chemie Ingenieur Technik}, volume = {82}, journal = {Chemie Ingenieur Technik}, number = {9}, publisher = {Wiley-VCH}, address = {Weinheim}, doi = {10.1002/cite.201050360}, pages = {1568}, year = {2010}, abstract = {Die am h{\"a}ufigsten genutzten Rohstoffe f{\"u}r die Produktion von Treibstoffen und Chemikalien sind fossilen Ursprungs. Da diese limitiert sind, werden im Hinblick auf die Nachhaltigkeit alternative, erneuerbare Rohstoffquellen intensiv untersucht. Vielversprechend in diesem Kontext sind die in Lignocellulose enthaltenen Zucker, die beispielsweise zur Produktion von Ethanol genutzt werden k{\"o}nnen. In der Regel sind f{\"u}r eine Lig-nocellulose-Bioraffinerie mehrere Prozessschritte notwendig: Vorbehandlung, Verzuckerung und Fermentation. Um diesen Prozess einfacher zu gestalten, ist es m{\"o}glich, die Verzuckerung und die Fermentation in einem Schritt durchzuf{\"u}hren (SSF). Als Substrat wird hier Cellulose-Faserstoff verwendet, der durch das Organosolv-Verfahren aufgeschlossen wurde. Die Hydrolyse erfolgt mit kommerziell erh{\"a}ltlichen Enzymen und f{\"u}r die Fermentation zu Ethanol werden zwei Hefen verwendet. Beim SSF-Verfahren konnte, im Vergleich zur entkoppelten Verfahrensweise, trotz bestehender Unterschiede in den Temperatur-Optima von Enzymen und Hefen eine Steigerung in der Ethanol-Ausbeute von 0,15 auf 0,2 gg⁻¹ beobachtet werden. Um wirtschaftliche Ausbeuten und Konzentrationen des Produkts erzielen zu k{\"o}nnen, ist es notwendig den Prozess weiter zu optimieren. Im Einzelfall muss {\"u}berpr{\"u}ft werden, ob diese Verfahrensweise auch f{\"u}r die Produktion anderer interessanter Stoffe (wie Itacons{\"a}ure, Bernsteins{\"a}ure) geeignet ist.}, language = {de} } @misc{PothMonzonTippkoetteretal.2009, author = {Poth, S. and Monzon, M. and Tippk{\"o}tter, Nils and Ulber, Roland}, title = {Enzymatische Hydrolyse von vorbehandelter Lignocellulose}, series = {Chemie Ingenieur Technik}, volume = {81}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.200950244}, pages = {1049}, year = {2009}, abstract = {Die {\"o}konomische Abh{\"a}ngigkeit von fossilen Brennstoffen und der klimatische Wandel durch die Nutzung dieser haben zu einer intensiven Suche nach erneuerbaren Rohstoffen f{\"u}r die Produktion von Chemikalien und Treibstoffen gef{\"u}hrt. Ein viel versprechender Rohstoff in diesem Zusammenhang sind Zucker, die mittels enzymatischer Hydrolyse aus Lignocellulose gewonnen und beispielsweise zu Ethanol umgesetzt werden k{\"o}nnen. Dabei ist es notwendig die Hydrolyse in Hinsicht auf das verwendete Substrat und die Verwendung der entstehenden Hydrolysate f{\"u}r die Fermentation von Alkohol zu optimieren. Als Substrat dienen Cellulose- und Hemicellulose-Fraktionen, die durch thermo-chemische Vorbehandlung von Holz gewonnen werden. Die Vorbehandlung erfolgt bei unserem Projektpartner am Johann Heinrich von Th{\"u}nen Institut in Hamburg. Verschiedene kommerziell erh{\"a}ltliche Enzyme, thermostabile eingeschlossen, wurden auf ihre F{\"a}higkeit hin untersucht, diese Fraktionen zu den entsprechenden Zuckern umsetzen zu k{\"o}nnen. Um die Konzentration an fermentierbaren Zuckern zu steigern werden verschiedene Optimierungen durchgef{\"u}hrt, z. B. die Erh{\"o}hung der Substrat- bzw. Enzymkonzentrationen. Ein weiterer interessanter Ansatz, welcher ebenfalls verfolgt wird, ist es die Hydrolyse und die Fermentation in einem Schritt durchzuf{\"u}hren.}, language = {de} } @article{PolenKraemerBongaertsetal.2005, author = {Polen, T. and Kr{\"a}mer, Marco and Bongaerts, Johannes and Wubbolts, Marcel and Wendisch, V. F.}, title = {The global gene expression response of Escherichia coli to L-phenylalanine}, series = {Journal of biotechnology}, volume = {Vol. 115}, journal = {Journal of biotechnology}, number = {Iss. 3}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, pages = {221 -- 237}, year = {2005}, language = {en} } @article{PohlSiegertMeschetal.1998, author = {Pohl, Martina and Siegert, Petra and Mesch, K. and Bruhn, H. and Gr{\"o}tzinger, Joachim}, title = {Active site mutants of pyruvate decarboxylase from Zymomonas mobilis : a site-directed mutagenesis study of L112, I472, I476, E473 and N482}, series = {European journal of biochemistry}, volume = {Vol. 257}, journal = {European journal of biochemistry}, number = {Iss. 3}, issn = {1432-1033 (E-Journal); 1742-4658 (E-Journal); 0014-2956 (Print); 1742-464X (Print)}, pages = {538 -- 546}, year = {1998}, language = {en} } @article{PlumMaHampeletal.2006, author = {Plum, Leona and Ma, Xiaosong and Hampel, Brigitte and Balthasar, Nina and Coppari, Roberto and M{\"u}nzberg, Heike and Shanabrough, Marya and Burdakov, Denis and Rother, Eva and Janoschek, Ruth and Alber, Jens and Belgardt, Bengt F. and Koch, Linda and Seibler, Jost and Schenk, Frieder and Fekete, Csaba and Suzuki, Akira and Mak, Tak W. and Krone, Wilhelm and Horvath, Tamas L. and Ashcroft, Frances M. and Br{\"u}ning, Jens C.}, title = {Enhanced PIP3 signaling in POMC neurons causes KATP channel activation and leads to diet-sensitive obesity}, series = {The Journal of Clinical Investigation (JCI)}, volume = {116}, journal = {The Journal of Clinical Investigation (JCI)}, number = {7}, issn = {1558-8238}, doi = {10.1172/JCI27123}, pages = {1886 -- 1901}, year = {2006}, language = {en} } @article{PinkenburgSchiffelsSelmer2016, author = {Pinkenburg, Olaf and Schiffels, Johannes and Selmer, Thorsten}, title = {Das CoLibry-Konzept - ein Werkzeugkasten f{\"u}r die Synthetische Biologie: Bioproduktion}, series = {BIOspektrum}, volume = {22}, journal = {BIOspektrum}, number = {6}, publisher = {Springer}, address = {Berlin}, doi = {10.1007/s12268-016-0734-8}, pages = {593 -- 595}, year = {2016}, abstract = {Regardless of size or destination, synthetic biology starts with com-parably small information units, which need to be combined and properly arranged in order to achieve a certain goal. This may be the de novo synthesis of individual genes from oligonucleotides, a shuffling of protein domains in order to create novel biocatalysts, the assembly of multiple enzyme encoding genes in metabolic pathway design, or strain development at the production stage. The CoLibry concept has been designed in order to close the gap between recombinant production of individual genes and genome editing.}, language = {de} } @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{PilasYaziciSelmeretal.2018, author = {Pilas, Johanna and Yazici, Y. and Selmer, Thorsten and Keusgen, M. and Sch{\"o}ning, Michael Josef}, title = {Application of a portable multi-analyte biosensor for organic acid determination in silage}, series = {Sensors}, volume = {18}, journal = {Sensors}, number = {5}, publisher = {MDPI}, address = {Basel}, issn = {1424-8220}, doi = {10.3390/s18051470}, pages = {12 Seiten}, year = {2018}, abstract = {Multi-analyte biosensors may offer the opportunity to perform cost-effective and rapid analysis with reduced sample volume, as compared to electrochemical biosensing of each analyte individually. This work describes the development of an enzyme-based biosensor system for multi-parametric determination of four different organic acids. The biosensor array comprises five working electrodes for simultaneous sensing of ethanol, formate, d-lactate, and l-lactate, and an integrated counter electrode. Storage stability of the biosensor was evaluated under different conditions (stored at +4 °C in buffer solution and dry at -21 °C, +4 °C, and room temperature) over a period of 140 days. After repeated and regular application, the individual sensing electrodes exhibited the best stability when stored at -21 °C. Furthermore, measurements in silage samples (maize and sugarcane silage) were conducted with the portable biosensor system. Comparison with a conventional photometric technique demonstrated successful employment for rapid monitoring of complex media.}, 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{PilasIkenSelmeretal.2015, author = {Pilas, Johanna and Iken, Heiko and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Development of a multi-parameter sensor chip for the simultaneous detection of organic compounds in biogas processes}, series = {Physica status solidi (a)}, volume = {212}, journal = {Physica status solidi (a)}, number = {6}, publisher = {Wiley}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201431894}, pages = {1306 -- 1312}, year = {2015}, abstract = {An enzyme-based multi-parameter biosensor is developed for monitoring the concentration of formate, d-lactate, and l-lactate in biological samples. The sensor is based on the specific dehydrogenation by an oxidized β-nicotinamide adenine dinucleotide (NAD+)-dependent dehydrogenase (formate dehydrogenase, d-lactic dehydrogenase, and l-lactic dehydrogenase, respectively) in combination with a diaphorase from Clostridium kluyveri (EC 1.8.1.4). The enzymes are immobilized on a platinum working electrode by cross-linking with glutaraldehyde (GA). The principle of the determination scheme in case of l-lactate is as follows: l-lactic dehydrogenase (l-LDH) converts l-lactate into pyruvate by reaction with NAD+. In the presence of hexacyanoferrate(III), the resulting reduced β-nicotinamide adenine dinucleotide (NADH) is then regenerated enzymatically by diaphorase. The electrochemical detection is based on the current generated by oxidation of hexacyanoferrate(II) at an applied potential of +0.3 V vs. an Ag/AgCl reference electrode. The biosensor will be electrochemically characterized in terms of linear working range and sensitivity. Additionally, the successful practical application of the sensor is demonstrated in an extract from maize silage.}, language = {en} }