@misc{StaubTippkoetterSucketal.2009, author = {Staub, C. and Tippk{\"o}tter, Nils and Suck, K. and Ruf, F. and Sohling, U. and Ulber, Roland}, title = {Aufreinigung von Molkeproteinen mittels nat{\"u}rlicher Adsorbermaterialien}, series = {Chemie Ingenieur Technik}, volume = {81}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.200950310}, pages = {1299}, year = {2009}, abstract = {Molke als Nebenprodukt der K{\"a}seherstellung wurde lange Zeit als Abfall betrachtet. Bedingt durch ihren hohen BOD (biological oxygen demand) war die direkte Einleitung in Gew{\"a}sser, aber auch der mikrobielle Abbau in Kl{\"a}ranlagen bedenklich. Falls eine Weiterverarbeitung der Molke stattfand, so geschah dies meist zu Molkepulver oder Proteinkonzentrat. Als Untersuchungen der Molkeproteine jedoch unter pharmazeutischen Gesichtspunkten interessante Eigenschaften nahelegten, stieg das Interesse am Bioprodukt Molke und ihren Proteinen an. So stehen beispielsweise f{\"u}r die Molkeproteine a-Lactalbumin (ala) und b-Lactoglobulin (blg) antibakterielle, anticancerogene und diverse andere physiologische Effekte in der Diskussion. Gegenw{\"a}rtig finden meist Membranverfahren zur Aufreinigung von Molkeproteinen Anwendung. Als alternatives Verfahren wurde am Institut f{\"u}r Bioverfahrenstechnik in Kaiserslautern ein chromatographisches Verfahren entwickelt, bei dem nat{\"u}rliche Tonminerale zum Einsatz kamen. Nach chemischer und physikalischer Modifikation des Ausgangsmaterials durch den Hersteller S{\"u}d-Chemie wurden drei der Adsorber f{\"u}r n{\"a}here Untersuchungen zur Auftrennung von Molkeproteinen aus Molkekonzentrat herangezogen. Nach einer Cross-Flow-Filtration des Molkekonzentrats erfolgte die Aufreinigung der Molkeproteine in einem FPLC-System.}, language = {de} } @misc{SiekerTippkoetterUlberetal.2009, author = {Sieker, T. and Tippk{\"o}tter, Nils and Ulber, Roland and Bart, Hans-J{\"o}rg and Heinzle, E.}, title = {Nutzung von Silage zur fermentativen Produktion von Grund-und Feinchemikalien}, series = {Chemie Ingenieur Technik}, volume = {81}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.200950271}, pages = {1207}, year = {2009}, abstract = {Grasschnitt hat in Deutschland ein betr{\"a}chtliches Potenzial als nachwachsender Rohstoff. Da frischer Grasschnitt nur in den Sommermonaten zur Verf{\"u}gung steht und Gras bei der Lagerung verrottet, wird er unter anderem durch Silierung konserviert. W{\"a}hrend der Silierung wird ein Teil der wasserl{\"o}slichen Kohlenhydrate unter anaeroben Bedingungen zu Milchs{\"a}ure fermentiert. Die Kombination aus Luftabschluss und Ans{\"a}uerung bewirkt die Konservierung der Silage. Silage als weit verbreitetes landwirtschaftliches Erzeugnis ist somit ein potentieller, in großen Mengen verf{\"u}gbarer Lieferant f{\"u}r eine Vielzahl von Substraten f{\"u}r mikrobielle Fermentationen. Diese k{\"o}nnen entweder durch die Hydrolyse der in den Pflanzen enthaltenen Cellulosen und Hemicellulosen oder durch die Verwendung eines Silagepresssaftes nutzbar gemacht werden. Die zu entwickelnden Prozesse sollen die verbleibenden Kohlenhydrate, inklusive der Cellulose und Hemicellulose, sowie die Milchs{\"a}ure nutzen. Die in der Silage enthaltenen Zucker sollen zu Ethanol, Itakons{\"a}ure und Bernsteins{\"a}ure und die Milchs{\"a}ure zu 1,2-Propandiol umgesetzt werden. Anfallende Reststoffe wie Hydrolyser{\"u}ckst{\"a}nde, Presskuchen und Fermentationsr{\"u}ckst{\"a}nde sollen bei allen zu etablierenden Prozessen entweder als Viehfutter verwendet oder der Biogasproduktion zugef{\"u}hrt werden k{\"o}nnen, wodurch eine vollst{\"a}ndige stoffliche und energetische Nutzung der Silage erreicht wird.}, language = {de} } @article{MangHodeniusSchmitzRodeetal.2009, author = {Mang, Thomas and Hodenius, Michael A. J. and Schmitz-Rode, Thomas and Baumann, Martin and Ivanova, Gergana and Wong, John Erik and Haulena, Friedhelm and Soenen, Stefaan J. H. and de Cuyper, Marcel}, title = {Absorption of 10-hydroxycamptothecin into the coat of magnetoliposomes / Hodenius, M. A. J. ; Schmitz-Rode, T. ; Baumann, M. ; Ivoanova, G. ; Wong, J. E. ; Mang, T. ; Haulena, F. ; Soenen, S. J. H. ; De Cuyper, M.}, series = {Colloids and Surfaces A: Physicochemical and Engineering Aspects. 343 (2009), H. 1-3}, journal = {Colloids and Surfaces A: Physicochemical and Engineering Aspects. 343 (2009), H. 1-3}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {0927-7757}, pages = {20 -- 23}, year = {2009}, language = {en} } @article{BalakrishnanAndreiSelmerSelmeretal.2010, author = {Balakrishnan, Karthikeyan and Andrei-Selmer, Luminita-Cornelia and Selmer, Thorsten and Bacher, Michael and Dodel, Richard}, title = {Comparison of Intravenous Immunoglobulins for Naturally Occurring Autoantibodies against Amyloid-β}, series = {Journal of Alzheimer's Disease}, volume = {20}, journal = {Journal of Alzheimer's Disease}, number = {1}, isbn = {1387-2877}, pages = {135 -- 143}, year = {2010}, language = {en} } @misc{Jeromin2010, author = {Jeromin, G{\"u}nter Erich}, title = {Immobilisierung von Alkoholdehydrogenasen und deren Coenzyme sowie Verwendung des Immobilisats : Offenlegungsschrift : DE 102008038326 A1 Offenlegungstag: 25.02.2010}, publisher = {Deutsches Patent- und Markenamt}, address = {M{\"u}nchen}, pages = {6 S.}, year = {2010}, language = {de} } @misc{SiegertMussmannO'Connelletal.2010, author = {Siegert, Petra and Mussmann, Nina and O'Connell, Timothy and Maurer, Karl-Heinz}, title = {Neue Proteasen und Mittel enthaltend diese Proteasen [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / WIPO}, address = {M{\"u}nchen / Genf}, pages = {1 -- 30}, year = {2010}, language = {de} } @misc{SiegertBaumstarkKluinetal.2010, author = {Siegert, Petra and Baumstark, Rebecca and Kluin, Cornelia and O'Connell, Timothy and Maurer, Karl-Heinz and Hellmuth, Hendrik}, title = {Neue Proteasen und Mittel enthaltend diese Proteasen [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt}, address = {M{\"u}nchen}, pages = {1 -- 30}, year = {2010}, language = {de} } @misc{SiegertSpitzMaurer2010, author = {Siegert, Petra and Spitz, Astrid and Maurer, Karl-Heinz}, title = {Neue Proteasen und Mittel enthaltend diese Proteasen [Offenlegungsschrift]}, publisher = {Deutsches Patentamt / WIPO}, address = {M{\"u}nchen / Genf}, pages = {1 -- 31}, year = {2010}, language = {de} } @misc{SiegertSpitzMaurer2010, author = {Siegert, Petra and Spitz, Astrid and Maurer, Karl-Heinz}, title = {Wasch- und Reinigungsmittel enthaltend Proteasen aus Bacillus pumilus [Offenlegungsschrift]}, publisher = {Deutsches Patentamt / Europ{\"a}isches Patentamt / WIPO}, address = {M{\"u}nchen / Den Hague / Genf}, pages = {1 -- 20}, year = {2010}, language = {de} } @misc{O'ConnellSiegertMaureretal.2010, author = {O'Connell, Timothy and Siegert, Petra and Maurer, Karl-Heinz and Schiedel, Marc-Steffen and Vockenroth, Inga Kerstin}, title = {Method for improving the cleaning action of a detergent or cleaning agent [Internationale Patentanmeldung]}, publisher = {WIPO}, address = {Genf}, pages = {1 -- 15}, year = {2010}, language = {en} } @incollection{SeiblerSchwenk2010, author = {Seibler, Jost and Schwenk, Frieder}, title = {Transgenic RNAi Applications in the Mouse}, series = {Methods in Enzymology : Guide to Techniques in Mouse Development, Part B: Mouse Molecular Genetics. 2nd Edition}, booktitle = {Methods in Enzymology : Guide to Techniques in Mouse Development, Part B: Mouse Molecular Genetics. 2nd Edition}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {978-0-12-384880-2}, pages = {367 -- 386}, year = {2010}, language = {en} } @article{TippkoetterRoikaewUlberetal.2010, author = {Tippk{\"o}tter, Nils and Roikaew, Wipa and Ulber, Roland and Hoffmann, Alexander and Denzler, Hans-J{\"o}rg and Buchholz, Heinrich}, title = {Paracoccus denitrificans for the effluent recycling during continuous denitrification of liquid food}, series = {Biotechnology Progress}, volume = {26}, journal = {Biotechnology Progress}, number = {3}, publisher = {Wiley}, address = {Hoboken, NJ}, issn = {8756-7938}, doi = {10.1002/btpr.384}, pages = {756 -- 762}, year = {2010}, abstract = {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.}, language = {en} } @article{RossPlummerRodeetal.2010, author = {Ross, Jillian and Plummer, Simon M. and Rode, Anja and Scheer, Nico and Bower, Conrad C. and Vogel, Ortwin and Henderson, Colin J. and Wolf, C. Roland and Elcombe, Clifford R.}, title = {Human constitutive androstane receptor (CAR) and pregnane X receptor (PXR) support the hypertrophic but not the hyperplastic response to the murine nongenotoxic hepatocarcinogens phenobarbital and chlordane in vivo}, series = {Toxicological Sciences}, volume = {116}, journal = {Toxicological Sciences}, number = {2}, publisher = {Oxford University Press}, address = {Oxford}, issn = {1096-0929}, doi = {10.1093/toxsci/kfq118}, pages = {452 -- 466}, year = {2010}, abstract = {Mouse nongenotoxic hepatocarcinogens phenobarbital (PB) and chlordane induce hepatomegaly characterized by hypertrophy and hyperplasia. Increased cell proliferation is implicated in the mechanism of tumor induction. The relevance of these tumors to human health is unclear. The xenoreceptors, constitutive androstane receptors (CARs), and pregnane X receptor (PXR) play key roles in these processes. Novel "humanized" and knockout models for both receptors were developed to investigate potential species differences in hepatomegaly. The effects of PB (80 mg/kg/4 days) and chlordane (10 mg/kg/4 days) were investigated in double humanized PXR and CAR (huPXR/huCAR), double knockout PXR and CAR (PXRKO/CARKO), and wild-type (WT) C57BL/6J mice. In WT mice, both compounds caused increased liver weight, hepatocellular hypertrophy, and cell proliferation. Both compounds caused alterations to a number of cell cycle genes consistent with induction of cell proliferation in WT mice. However, these gene expression changes did not occur in PXRKO/CARKO or huPXR/huCAR mice. Liver hypertrophy without hyperplasia was demonstrated in the huPXR/huCAR animals in response to both compounds. Induction of the CAR and PXR target genes, Cyp2b10 and Cyp3a11, was observed in both WT and huPXR/huCAR mouse lines following treatment with PB or chlordane. In the PXRKO/CARKO mice, neither liver growth nor induction of Cyp2b10 and Cyp3a11 was seen following PB or chlordane treatment, indicating that these effects are CAR/PXR dependent. These data suggest that the human receptors are able to support the chemically induced hypertrophic responses but not the hyperplastic (cell proliferation) responses. At this time, we cannot be certain that hCAR and hPXR when expressed in the mouse can function exactly as the genes do when they are expressed in human cells. However, all parameters investigated to date suggest that much of their functionality is maintained.}, language = {en} } @article{ScheerRossKapelyukhetal.2010, author = {Scheer, Nico and Ross, Jillian and Kapelyukh, Yury and Rode, Anja and Wolf, C. Roland}, title = {In vivo responses of the human and murine pregnane X receptor to dexamethasone in mice}, series = {Drug Metabolism and Disposition}, volume = {38}, journal = {Drug Metabolism and Disposition}, number = {7}, publisher = {ASPET}, address = {Bethesda}, issn = {1521-009X}, doi = {10.1124/dmd.109.031872}, pages = {1046 -- 1053}, year = {2010}, abstract = {Dexamethasone (DEX) is a potent and widely used anti-inflammatory and immunosuppressant glucocorticoid. It can bind and activate the pregnane X receptor (PXR), which plays a critical role as xenobiotic sensor in mammals to induce the expression of many enzymes, including cytochromes P450 in the CYP3A family. This induction results in its own metabolism. We have used a series of transgenic mouse lines, including a novel, improved humanized PXR line, to compare the induction profile of PXR-regulated drug-metabolizing enzymes after DEX administration, as well as looking at hepatic responses to rifampicin (RIF). The new humanized PXR model has uncovered further intriguing differences between the human and mouse receptors in that RIF only induced Cyp2b10 in the new humanized model. DEX was found to be a much more potent inducer of Cyp3a proteins in wild-type mice than in mice humanized for PXR. To assess whether PXR is involved in the detoxification of DEX in the liver, we analyzed the consequences of high doses of the glucocorticoid on hepatotoxicity on different PXR genetic backgrounds. We also studied these effects in an additional mouse model in which functional mouse Cyp3a genes have been deleted. These strains exhibited different sensitivities to DEX, indicating a protective role of the PXR and CYP3A proteins against the hepatotoxicity of this compound.}, language = {en} } @article{PaulssenSchweighoeferAbram2010, author = {Paulßen, Elisabeth and Schweigh{\"o}fer, Philip V. and Abram, Ulrich}, title = {Reactions of [ReOX3(PPh3)2] Complexes (X = Cl, Br) with Phenylacetylene and the Structures of the Products}, series = {Zeitschrift f{\"u}r anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry}, volume = {636}, journal = {Zeitschrift f{\"u}r anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1521-3749}, doi = {10.1002/zaac.200900478}, pages = {779 -- 783}, year = {2010}, abstract = {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.}, language = {en} } @article{PaulssenAlbertoAbram2010, author = {Paulßen, Elisabeth and Alberto, Roger and Abram, Ulrich}, title = {Synthesis, Characterization, and Structures of R3EOTcO3 Complexes (E = C, Si, Ge, Sn, Pb) and Related Compounds}, series = {Inorganic Chemistry}, volume = {49}, journal = {Inorganic Chemistry}, number = {7}, publisher = {American Chemical Society}, address = {Washington}, issn = {1520-510X}, doi = {10.1021/ic1001094}, pages = {3525 -- 3530}, year = {2010}, abstract = {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.}, 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} } @misc{O'ConnellSiegertEversetal.2010, author = {O'Connell, Timothy and Siegert, Petra and Evers, Stefan and Bongaerts, Johannes and Weber, Thomas and Maurer, Karl-Heinz and Bessler, Cornelius}, title = {Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft [Offenlegungsschrift]}, publisher = {Deutsches Patentamt}, address = {M{\"u}nchen}, pages = {1 -- 34}, year = {2010}, language = {de} } @incollection{MufflerTippkoetterUlber2010, author = {Muffler, Kai and Tippk{\"o}tter, Nils and Ulber, Roland}, title = {Chemical feedstocks and fine chemicals from other substrates}, series = {Handbook of hydrocarbon and lipid microbiology. Volume 4: Consequences of microbial interactions with hydrocarbons, oils and lipids. - (Springer reference)}, booktitle = {Handbook of hydrocarbon and lipid microbiology. Volume 4: Consequences of microbial interactions with hydrocarbons, oils and lipids. - (Springer reference)}, editor = {Timmis, Kenneth N.}, publisher = {Springer}, address = {Berlin [u.a.]}, isbn = {978-3-540-77588-1}, doi = {10.1007\%2F978-3-540-77587-4_214}, pages = {2891 -- 2902}, year = {2010}, language = {en} } @misc{TippkoetterZhangPothetal.2010, author = {Tippk{\"o}tter, Nils and Zhang, M. and Poth, S. and Ulber, Roland}, title = {Enzymatische Lignindegradierung unter Einsatz eines Optimierungsalgorithmus}, series = {Chemie Ingenieur Technik}, volume = {82}, journal = {Chemie Ingenieur Technik}, number = {9}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.201050707}, pages = {1601 -- 1602}, year = {2010}, abstract = {Lignine bestehen aus einem hochgradig vernetzten Polymer phenolischer Grundeinheiten. Diese Verbindungen sind eine Quelle vielversprechender chemischer Grundbausteine. Auch die enzymatische Modifikation der Materialeigenschaften des Lignins ist f{\"u}r dessen Anwendung von Interesse. Aufgrund der verschiedenen Bindungstypen im Lignin ist eine Auftrennung mit nur einem Enzym unwahrscheinlich. Vielmehr sind verschiedene mediatorgest{\"u}tzte Reaktionen notwendig. Pilze, wie z.B. T. versicolor, nutzen Enzymkombinationen zum Aufschluss des Lignins. Hierbei kommen Laccase, Ligninperoxidase und Manganperoxidase zum Einsatz. Die optimale Kombination der Enzyme und ihrer Mediatoren bzw. Stabilisatoren ist Ziel der Untersuchungen. Aufgrund der großen Parameteranzahl wurde ein genetischer Algorithmus eingesetzt. Als Versuchsparameter wurden gew{\"a}hlt: die Verh{\"a}ltnisse der Enzyme, Ligninmasse, Konzentrationen an Eisen-, Mangan-, Oxalat-Ionen, ABTS, Violurs{\"a}ure und H₂O₂. Somit werden elf Parameter simultan optimiert. Als Algorithmus wurde ein Programm mit variabler Genkodierung entwickelt. Die Umsetzung des Lignins wird dabei {\"u}ber den verfolgt. Zurzeit ist ein enzymatischer Umsatz von 12\% m{\"o}glich. Als Referenz wurde eine chemische Lignindegradierung mit einem Umsatzvon 37\% etabliert. Die sechs Generationen des Algorithmus zeigen eine Kongruenz der Enzymkonzentrationen von LiP, MnP und VeP, w{\"a}hrend Laccase keinen Einfluss hat. Des Weiteren beeinflussen die Konzentrationen von Mangan und Oxalat die Umsetzung, w{\"a}hrend die Variation von ABTS- und H₂O₂ nur eine geringe Auswirkung hat.}, language = {de} }