@misc{WielandSiegertSpitzetal.2011,
  author    = {Wieland, Susanne and Siegert, Petra and Spitz, Astrid and Maurer, Karl-Heinz and O'Connell, Timothy and Pr{\"u}ser, Inken and Schiedel, Marc-Steffen and Eiting, Thomas and Sendor-M{\"u}ller, Dorota and Bastigkeit, Thorsten and Benda, Konstantin and M{\"u}ller, Sven},
  title     = {Lagerstabiles fl{\"u}ssiges Wasch- oder Reinigungsmittel enthaltend Proteasen [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 25},
  year      = {2011},
  language  = {de}
}
@article{MartinezJakobTuetal.2013,
  author    = {Martinez, Ronny and Jakob, Felix and Tu, Ran and Siegert, Petra and Maurer, Karl-Heinz and Schwaneberg, Ulrich},
  title     = {Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution},
  series = {Biotechnology and bioengineering},
  volume    = {Vol. 110},
  journal   = {Biotechnology and bioengineering},
  number    = {Iss. 3},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1097-0290 (E-Journal); 0006-3592 (Print); 0368-1467 (Print)},
  pages     = {711 -- 720},
  year      = {2013},
  language  = {en}
}
@article{VoigtAlbrechtSieversetal.2015,
  author    = {Voigt, Birgit and Albrecht, Dirk and Sievers, Susanne and Becher, D{\"o}rte and Bongaerts, Johannes and Evers, Stefan and Schweder, Thomas and Maurer, Karl-Heinz and Hecker, Michael},
  title     = {High-resolution proteome maps of Bacillus licheniformis cells growing in minimal medium},
  series = {Proteomics},
  volume    = {15},
  journal   = {Proteomics},
  number    = {15},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1615-9861},
  doi       = {10.1002/pmic.201400504},
  pages     = {2629 -- 2633},
  year      = {2015},
  language  = {en}
}
@article{DeppeKlatteBongaertsetal.2011,
  author    = {Deppe, Veronika Maria and Klatte, Stephanie and Bongaerts, Johannes and Maurer, Karl-Heinz and O'Connell, Timothy and Meinhardt, Friedhelm},
  title     = {Genetic control of Amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR},
  series = {Applied and environmental microbiology},
  volume    = {Vol. 77},
  journal   = {Applied and environmental microbiology},
  number    = {No. 9},
  publisher = {American Society of Mechanical Engineers (ASME)},
  address   = {New York},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  pages     = {2839 -- 2846},
  year      = {2011},
  language  = {en}
}
@misc{MaurerO'ConnellSiegertetal.2012,
  author    = {Maurer, Karl-Heinz and O'Connell, Timothy and Siegert, Petra and Weber, Thomas and Tondera, Susanne and Hellmuth, Hendrik},
  title     = {Fl{\"u}ssige Tensidzubereitung enthaltend Lipase und Phosphonat [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 22},
  year      = {2012},
  language  = {de}
}
@article{RibitschHeumannKarletal.2012,
  author    = {Ribitsch, D. and Heumann, S. and Karl, W. and Gerlach, J. and Leber, R. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Siegert, Petra and Lange, J. and Maurer, Karl-Heinz and Berg, G. and Guebitz, G. M. and Schwab, H.},
  title     = {Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli},
  series = {Journal of biotechnology},
  volume    = {157},
  journal   = {Journal of biotechnology},
  number    = {1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2011.09.025},
  pages     = {140 -- 147},
  year      = {2012},
  abstract  = {A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3. From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.},
  language  = {en}
}
@article{NiehausGaborWielandetal.2011,
  author    = {Niehaus, F. and Gabor, E. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Eck, J.},
  title     = {Enzymes for the laundry industries: tapping the vast metagenomic pool of alkaline proteases},
  series = {Microbial biotechnology},
  volume    = {Vol. 4},
  journal   = {Microbial biotechnology},
  number    = {Iss. 6},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)},
  pages     = {767 -- 776},
  year      = {2011},
  language  = {en}
}
@article{DeppeBongaertsO'Connelletal.2011,
  author    = {Deppe, Veronika Maria and Bongaerts, Johannes and O'Connell, Timothy and Maurer, Karl-Heinz and Meinhardt, Friedhelm},
  title     = {Enzymatic deglycation of Amadori products in bacteria},
  series = {Applied microbiology and biotechnology},
  volume    = {Vol. 90},
  journal   = {Applied microbiology and biotechnology},
  number    = {Iss. 2},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)},
  pages     = {399 -- 406},
  year      = {2011},
  language  = {en}
}
@article{KueppersSteffenHellmuthetal.2014,
  author    = {K{\"u}ppers, Tobias and Steffen, Victoria and Hellmuth, Hendrik and O'Connell, Timothy and Bongaerts, Johannes and Maurer, Karl-Heinz and Wiechert, Wolfgang},
  title     = {Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer},
  series = {Microbial cell factories},
  volume    = {13},
  journal   = {Microbial cell factories},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1475-2859 (E-Journal)},
  doi       = {10.1186/1475-2859-13-46},
  pages     = {Article No. 46},
  year      = {2014},
  language  = {en}
}
@article{HandtkeVollandMethlingetal.2014,
  author    = {Handtke, Stefan and Volland, Sonja and Methling, Karen and Albrecht, Dirk and Becher, D{\"o}rte and Nehls, Jenny and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Liesegang, Heiko and Voigt, Birgit and Daniel, Rolf and Hecker, Michael},
  title     = {Cell physiology of the biotechnological relevant bacterium Bacillus pumilus - An omics-based approach},
  series = {Journal of Biotechnology},
  journal   = {Journal of Biotechnology},
  number    = {192(A)},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2014.08.028},
  pages     = {204 -- 214},
  year      = {2014},
  abstract  = {Members of the species Bacillus pumilus get more and more in focus of the biotechnological industry as potential new production strains. Based on exoproteome analysis, B. pumilus strain Jo2, possessing a high secretion capability, was chosen for an omics-based investigation. The proteome and metabolome of B. pumilus cells growing either in minimal or complex medium was analyzed. In total, 1542 proteins were identified in growing B. pumilus cells, among them 1182 cytosolic proteins, 297 membrane and lipoproteins and 63 secreted proteins. This accounts for about 43\% of the 3616 proteins encoded in the B. pumilus Jo2 genome sequence. By using GC-MS, IP-LC/MS and H NMR methods numerous metabolites were analyzed and assigned to reconstructed metabolic pathways. In the genome sequence a functional secretion system including the components of the Sec- and Tat-secretion machinery was found. Analysis of the exoproteome revealed secretion of about 70 proteins with predicted secretion signals. In addition, selected production-relevant genome features such as restriction modification systems and NRPS clusters of B. pumilus Jo2 are discussed.},
  language  = {en}
}