@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}
}
@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}
}
@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}
}
@article{SrivastavaSinghAggarwaletal.2010,
  author    = {Srivastava, Alok and Singh, Virendra and Aggarwal, Pranav 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{RieplPettrakFaulstichetal.2010,
  author    = {Riepl, Herbert Matthias and Pettrak, J{\"u}rgen and Faulstich, Martin and Herrmann, Wolfgang Anton},
  title     = {Self metathesis of fatty alcohols and amines to provide monomers for polyester and polyamide products},
  series = {Macromolecular Symposia},
  volume    = {293},
  journal   = {Macromolecular Symposia},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1521-3900 (eISSN)},
  doi       = {10.1002/masy.200900041},
  pages     = {39 -- 42},
  year      = {2010},
  abstract  = {Self metathesis of oleochemicals offers a variety of bifunctional compounds, that can be used as monomer for polymer production. Many precursors are in huge scales available, like oleic acid ester (biodiesel), oleyl alcohol (tensides), oleyl amines (tensides, lubricants). We show several ways to produce and separate and purify C18-α,ω-bifunctional compounds, using Grubbs 2nd Generation catalysts, starting from technical grade educts.},
  language  = {en}
}