@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{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}
}
@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}
}
@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{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}
}
@inproceedings{PothMonzonTippkoetteretal.2010,
  author    = {Poth, Sebastian and Monzon, Magaly and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {Lignocellulosic biorefinery : process integration of hydrolysis and fermentation},
  series = {Proceedings / 11th European Workshop on Lignocellulosics and Pulp : August 16 - 19, 2010, Hamburg, Germany},
  booktitle = {Proceedings / 11th European Workshop on Lignocellulosics and Pulp : August 16 - 19, 2010, Hamburg, Germany},
  publisher = {vTi},
  address   = {Hamburg},
  pages     = {65 -- 68},
  year      = {2010},
  language  = {en}
}
@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}
}
@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}
}