@misc{SiekerTippkoetterUlberetal.2009,
  author    = {Sieker, T. and Tippk{\"o}tter, Nils and Ulber, Roland and Bart, H.-J. 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}
}
@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}
}
@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}
}
@article{ClaessenGrefenMangetal.2010,
  author    = {Claessen, O. and Grefen, Dana and Mang, Thomas and Dikland, H. G. and Dikland, H. G. and Duin, M. van},
  title     = {Helle Fensterprofilmaterialien : Alterungsverhalten auf Basis von peroxidisch vernetztem EPDM},
  series = {Kautschuk, Gummi, Kunststoffe : KGK},
  volume    = {63},
  journal   = {Kautschuk, Gummi, Kunststoffe : KGK},
  number    = {9},
  isbn      = {0948-3276},
  pages     = {350 -- 360},
  year      = {2010},
  language  = {de}
}
@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}
}
@article{SrivastavaSinghAggarwaletal.2010,
  author    = {Srivastava, A. and Singh, V. and Aggarwal, P. 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{KowollikSchnitzlerBisellietal.2010,
  author    = {Kowollik, S. and Schnitzler, Thomas and Biselli, Manfred and Krueger, R. and Zang, Werner and Peuscher, A. and Schillberg, S. and Fischer, R.},
  title     = {Die Rolle des Respirationsquotienten in der Zellkulturfermentation},
  series = {Chemie Ingenieur Technik},
  volume    = {82},
  journal   = {Chemie Ingenieur Technik},
  number    = {9},
  isbn      = {Chemie Ingenieur Tec},
  pages     = {1505 -- 1506},
  year      = {2010},
  language  = {de}
}
@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}
}
@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{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, Special Issue: Industrielle Nutzung nachwachsender Rohstoffe},
  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{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}
}