@misc{WiesenTippkoetterMuffleretal.2012, author = {Wiesen, S. and Tippk{\"o}tter, Nils and Muffler, K. and Sohling, U. and Ruf, F. and Ulber, Roland}, title = {Nutzung von Rohglycerin: Rohglycerin-Aufarbeitung, Herstellung von 1, 3-Propandiol und R{\"u}ckgewinnung von Fetts{\"a}uren}, series = {Chemie Ingenieur Technik}, volume = {84}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.201250265}, pages = {1296}, year = {2012}, abstract = {Die fermentative Verwertung von Rohglycerin setzt je nach Herstellungsmethode und Produktionsorganismus eine Vorbehandlung des Glycerins zur Entfernung von Produktinhibitoren voraus. Durch den Einsatz von Hydrotalcit-Adsorbern k{\"o}nnen die im Rohglycerin enthaltenen Fetts{\"a}uren entfernt werden. Durch diese einfache Aufarbeitungsmethode ist ein mit reinem Glycerin vergleichbarer Umsatz von stark mit Fetts{\"a}uren verunreinigtem Rohglycerin zu 1,3-Propandiol (PDO) m{\"o}glich. Die durch den Hydrotalcit gebundenen Fetts{\"a}uren lassen sich mit einem Ethanol-Wasser-Gemisch eluieren. Somit kann der Adsorber regeneriert und die Fetts{\"a}uren wieder der Wertsch{\"o}pfungskette zugef{\"u}hrt werden. Im Fed-Batch-Experiment kann mit C. diolis eine PDO-Konzentration von {\"u}ber 50 g L⁻¹ unter Verwendung des aufgereinigten Rohglycerins erzielt werden. In der industriellen Produktion wird PDO momentan destillativ aufgearbeitet. Ein adsorptives Aufarbeitungsverfahren kann den Energiebedarf des Herstellungsprozesses drastisch senken. Auf der Suche nach einem geeigneten Material wurde ein Adsorberscreening in Bezug auf die Bindungseigenschaften durchgef{\"u}hrt. Mit einem b-Zeolith der Firma S{\"u}d ChemieAG konnte bisher die h{\"o}chste Beladung im Modellsystem von 120 mg PDO/gAdsorber erreicht werden.}, language = {de} } @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}, publisher = {Council Of Scientific And Industrial Research (CSIR), National Institute Of Science Communication and Policy Research (NIScPR)}, address = {New Delhi}, 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{RibitschKarlBirnerGruenbergeretal.2010, author = {Ribitsch, D. and Karl, W. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Schwab, H.}, title = {C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli}, series = {Journal of biotechnology}, volume = {150}, journal = {Journal of biotechnology}, number = {3}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, doi = {10.1016/j.jbiotec.2010.09.947}, pages = {408 -- 416}, year = {2010}, abstract = {Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477. This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7-11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.}, language = {en} } @article{BarbazanHagenbachPaulssenetal.2010, author = {Barbaz{\´a}n, Paula and Hagenbach, Adelheid and Paulßen, Elisabeth and Abram, Ulrich and Carballo, Rosa and Rodriguez-Hermida, Sabina and V{\´a}zquez-L{\´o}pez, Ezequiel M.}, title = {Tricarbonyl Rhenium(I) and Technetium(I) Complexes with Hydrazones Derived from 4,5-Diazafluoren-9-one and 1,10-Phenanthroline-5,6-dione}, series = {European Journal of Inorganic Chemistry}, journal = {European Journal of Inorganic Chemistry}, number = {29}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1099-0682}, doi = {10.1002/ejic.201000522}, pages = {4622 -- 4630}, year = {2010}, abstract = {Tricarbonylrhenium(I) and -technetium(I) halide (halide = Cl and Br) complexes of ligands derived from 4,5-diazafluoren-9-one (df) and 1,10-phenanthroline-5,6-dione (phen) derivatives of benzoic and 2-hydroxybenzoic acid hydrazides have been prepared. The complexes have been characterized by elemental analysis, MS, IR, 1H NMR and absorption and emission UV/Vis spectroscopic methods. The metal centres (ReI and TcI) are coordinated through the nitrogen imine atoms and establish five-membered chelate rings, whereas the hydrazone groups stand uncoordinated. The 1H NMR spectra suggest the same behaviour in solution on the basis of only marginal variations in the chemical shifts of the hydrazine protons.}, language = {en} } @article{UlberPothMonzonetal.2010, author = {Ulber, Roland and Poth, Sebastian and Monzon, Magaly and Tippk{\"o}tter, Nils}, title = {Prozessintegration von Hydrolyse und Fermentation von Cellulose- Faserstoff}, series = {Chemie Ingenieur Technik}, volume = {82}, journal = {Chemie Ingenieur Technik}, number = {1-2}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1522-2640}, doi = {10.1002/cite.200900103}, pages = {135 -- 139}, year = {2010}, abstract = {Ein viel versprechender erneuerbarer Rohstoff f{\"u}r die Produktion von Chemikalien und Treibstoffen ist Lignocellulose aus pflanzlicher Biomasse. Die darin enthaltenen Zucker k{\"o}nnen 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.}, language = {de} } @article{SiekerNeunerDimitrovaetal.2010, author = {Sieker, Tim and Neuner, Andreas and Dimitrova, Darina and Tippk{\"o}tter, Nils and Bart, Hans-J{\"o}rg and Heinzle, Elmar and Ulber, Roland}, title = {Grassilage als Rohstoff f{\"u}r die chemische Industrie}, series = {Chemie Ingenieur Technik}, volume = {82}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1522-2640}, doi = {10.1002/cite.201000088}, pages = {1153 -- 1159}, year = {2010}, abstract = {Grassilage stellt einen nachwachsenden Rohstoff mit großem Potenzial dar. Neben Cellulose und Hemicellulose enth{\"a}lt sie auch organische S{\"a}uren, insbesondere Milchs{\"a}ure. In einem Bioraffinerie-Projekt wird die Milchs{\"a}ure aus der Silage isoliert und mit gentechnisch optimierten St{\"a}mmen 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 s{\"a}mtliche Inhaltsstoffe der Silage verwertet.}, 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} } @article{BaumannLaraHubbertenetal.1997, author = {Baumann, Marcus and Lara, R.J. and Hubberten, D.N. and Thomas, D. N.}, title = {Dissolved organic matter studies in enclosed systems: Application of hydophobic fractionation for the assessment of organic nitrogen dynamics / Lara, R.J. ; Hubberten, U. ; Thomas, D.N. ; Baumann, M.E.M. ; Kattner, G.}, series = {Journal of Marine Systems. 13 (1997), H. 1-4}, journal = {Journal of Marine Systems. 13 (1997), H. 1-4}, isbn = {0924-7963}, pages = {155 -- 161}, year = {1997}, language = {en} } @article{BaumannThomasGleitz1992, author = {Baumann, Marcus and Thomas, D. N. and Gleitz, M.}, title = {Efficiency of carbon assimilation and photoacclimation in a small unicellular Chaetoceros species from the Weddel Sea (Antarctica): Influence of temperature and irridiance / Thomas, D. ; Baumann, M.E.M. ; Gleitz, M.}, series = {Journal of Experimental Marine Biology and Ecology. 157 (1992), H. 2}, journal = {Journal of Experimental Marine Biology and Ecology. 157 (1992), H. 2}, isbn = {0022-0981}, pages = {195 -- 209}, year = {1992}, language = {en} } @book{Pettrak2014, author = {Pettrak, J{\"u}rgen}, title = {Nutzung nachwachsender Rohstoffe bei der Herstellung thermoplastischer Elastomere aus Folgeprodukten der Olefinmetathese}, publisher = {Attenkofer}, address = {Straubing}, isbn = {978-3-942742-35-1}, pages = {147 Seiten}, year = {2014}, language = {de} }