TY - PAT A1 - Siegert, Petra A1 - Spitz, Astrid A1 - Maurer, Karl-Heinz T1 - Wasch- und Reinigungsmittel enthaltend Proteasen aus Bacillus pumilus [Offenlegungsschrift] T1 - Detergents and cleaning agents containing proteases from bacillus pumilus [Europäische Patentschrift / Internationale Patentanmeldung] Y1 - 2010 SP - 1 EP - 20 PB - Deutsches Patentamt / Europäisches Patentamt / WIPO CY - München / Den Hague / Genf ER - TY - PAT A1 - O'Connell, Timothy A1 - Siegert, Petra A1 - Evers, Stefan A1 - Bongaerts, Johannes A1 - Weber, Thomas A1 - Maurer, Karl-Heinz A1 - Bessler, Cornelius T1 - Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft [Offenlegungsschrift] T1 - Method from improving the cleaning action of a detergent of cleaning agent [US Patentanmeldung] Y1 - 2010 SP - 1 EP - 34 PB - Deutsches Patentamt CY - München ER - TY - JOUR A1 - Barbazán, Paula A1 - Hagenbach, Adelheid A1 - Paulßen, Elisabeth A1 - Abram, Ulrich A1 - Carballo, Rosa A1 - Rodriguez-Hermida, Sabina A1 - Vázquez-López, Ezequiel M. T1 - Tricarbonyl Rhenium(I) and Technetium(I) Complexes with Hydrazones Derived from 4,5-Diazafluoren-9-one and 1,10-Phenanthroline-5,6-dione JF - European Journal of Inorganic Chemistry N2 - 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. Y1 - 2010 U6 - http://dx.doi.org/10.1002/ejic.201000522 SN - 1099-0682 IS - 29 SP - 4622 EP - 4630 PB - Wiley-VCH CY - Weinheim ER - TY - CHAP A1 - Seibler, Jost A1 - Schwenk, Frieder T1 - Transgenic RNAi Applications in the Mouse T2 - Methods in Enzymology : Guide to Techniques in Mouse Development, Part B: Mouse Molecular Genetics. 2nd Edition Y1 - 2010 SN - 978-0-12-384880-2 N1 - Methods in Enzymology : Vol. 477 SP - 367 EP - 386 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Paulßen, Elisabeth A1 - Alberto, Roger A1 - Abram, Ulrich T1 - Synthesis, Characterization, and Structures of R3EOTcO3 Complexes (E = C, Si, Ge, Sn, Pb) and Related Compounds JF - Inorganic Chemistry N2 - AgTcO4 reacts with R3ECl compounds (E = C, Si, Ge, Sn, Pb; R = Me, iPr, tBu, Ph), tBu2SnCl2, or PhMgCl under formation of novel trioxotechnetium(VII) derivatives. The carbon and silicon derivatives readily undergo decomposition, which was proven by 99Tc NMR spectroscopy and the isolation of decomposition products such as [TcOCl3(THF)(OH2)]. Compounds [Ph3GeOTcO3], [(THF)Ph3SnOTcO3], [(O3TcO)SntBu2(OH)]2, and [(THF)4Mg(OTcO3)2] are more stable and were isolated in crystalline form and characterized by X-ray diffraction. Y1 - 2010 U6 - http://dx.doi.org/10.1021/ic1001094 SN - 1520-510X VL - 49 IS - 7 SP - 3525 EP - 3530 PB - American Chemical Society CY - Washington ER - TY - BOOK A1 - Tippkötter, Nils T1 - Reaktionssysteme zur Aufarbeitung und Umsetzung nachwachsender Rohstoffe : Einsatz chromatographischer Verfahren sowie Membran- und Festbettreaktoren zur Verarbeitung von Molke, Stärke und Cellulose Y1 - 2010 SN - 978-3-8325-2717-4 N1 - Kaiserslautern, Technische Universität, Dissertation, 2010 PB - Logos-Verlag CY - Berlin ER - TY - JOUR A1 - Paulßen, Elisabeth A1 - Schweighöfer, Philip V. A1 - Abram, Ulrich T1 - Reactions of [ReOX3(PPh3)2] Complexes (X = Cl, Br) with Phenylacetylene and the Structures of the Products JF - Zeitschrift für anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry N2 - Oxorhenium(V) complexes [ReOX3(PPh3)2] (X = Cl, Br) react with phenylacetylene under formation of complexes with ylide-type ligands. Compounds of the compositions [ReOCl3(PPh3){C(Ph)C(H)(PPh3)}] (1), [ReOBr3(OPPh3){C(Ph)C(H)(PPh3)}] (2), and [ReOBr3(OPPh3){C(H)C(Ph)(PPh3)}] (3) were isolated and characterized by X-ray diffraction. They contain a ligand, which was formed by a nucleophilic attack of released PPh3 at coordinated phenylacetylene. The structures of the products show that there is no preferable position for this attack. Cleavage of the Re–C bond in 3 and dimerization of the organic ligand resulted in the formation of the [{(PPh3)(H)CC(Ph)}2]2+ cation, which crystallized as its [(ReOBr4)(OReO3)]2– salt. Y1 - 2010 U6 - http://dx.doi.org/10.1002/zaac.200900478 SN - 1521-3749 VL - 636 IS - 5 SP - 779 EP - 783 PB - Wiley-VCH CY - Weinheim ER - 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 - Tippkötter, Nils A1 - Roikaew, Wipa A1 - Ulber, Roland A1 - Hoffmann, Alexander A1 - Denzler, Hans-Jörg A1 - Buchholz, Heinrich T1 - Paracoccus denitrificans for the effluent recycling during continuous denitrification of liquid food JF - Biotechnology Progress N2 - Nitrate is an undesirable component of several foods. A typical case of contamination with high nitrate contents is whey concentrate, containing nitrate in concentrations up to 25 l. The microbiological removal of nitrate by Paracoccus denitrificans under formation of harmless nitrogen in combination with a cell retention reactor is described here. Focus lies on the resource-conserving design of a microbal denitrification process. Two methods are compared. The application of polyvinyl alcohol-immobilized cells, which can be applied several times in whey feed, is compared with the implementation of a two step denitrification system. First, the whey concentrate's nitrate is removed by ion exchange and subsequently the eluent regenerated by microorganisms under their retention by crossflow filtration. Nitrite and nitrate concentrations were determined by reflectometric color measurement with a commercially available Reflectoquant® device. Correction factors for these media had to be determined. During the pilot development, bioreactors from 4 to 250 mg·L-1 and crossflow units with membrane areas from 0.02 to 0.80 m2 were examined. Based on the results of the pilot plants, a scaling for the exemplary process of denitrifying 1,000 tons per day is discussed. Y1 - 2010 U6 - http://dx.doi.org/10.1002/btpr.384 SN - 8756-7938 VL - 26 IS - 3 SP - 756 EP - 762 PB - Wiley CY - Hoboken, NJ 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 -