@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}
}
@article{SiegertMcLeishBaumannetal.2005,
  author    = {Siegert, Petra and McLeish, Michael J. and Baumann, Martin and Iding, Hans and Kneen, Malea M. and Kenyon, George L. and Pohl, Martina},
  title     = {Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida},
  series = {Protein engineering, design, and selection : peds},
  volume    = {Vol. 18},
  journal   = {Protein engineering, design, and selection : peds},
  number    = {Iss. 7},
  issn      = {1460-213X (E-Journal); 1741-0134 (E-Journal); 0269-2139 (Print); 1741-0126 (Print)},
  pages     = {345 -- 357},
  year      = {2005},
  language  = {en}
}
@article{DuenkelmannKolterJungNitscheetal.2002,
  author    = {D{\"u}nkelmann, Pascal and Kolter-Jung, Doris and Nitsche, Adam and Demir, Ayhan S. and Siegert, Petra and Lingen, Bettina and Baumann, Martin and Pohl, Martina and M{\"u}ller, Michael},
  title     = {Development of a donor-acceptor concept for enzymatic cross-coupling reactions of adehydes : the first asymmetric cross-benzoin condensation},
  series = {Journal of the American Chemical Society},
  volume    = {Vol. 124},
  journal   = {Journal of the American Chemical Society},
  issn      = {1520-5126 (E-Journal); 0002-7863 (Print)},
  pages     = {12084 -- 12085},
  year      = {2002},
  language  = {en}
}
@article{DuennwaldDemirSiegertetal.2001,
  author    = {D{\"u}nnwald, Thomas and Demir, Ayhan S. and Siegert, Petra and Pohl, Martina and M{\"u}ller, Michael},
  title     = {ChemInform Abstract: Enantioselective synthesis of (S)-2-Hydroxypropanone derivatives by Benzoylformate Decarboxylase Catalyzed C—C Bond Formation},
  series = {Cheminform},
  volume    = {Vol. 32},
  journal   = {Cheminform},
  number    = {Iss. 4},
  issn      = {1522-2667 (E-Journal); 0931-7597 (Print)},
  pages     = {Publ. online},
  year      = {2001},
  language  = {en}
}
@article{DuennwaldDemirSiegertetal.2000,
  author    = {D{\"u}nnwald, Thomas and Demir, Ayhan S. and Siegert, Petra and Pohl, Martina and M{\"u}ller, Michael},
  title     = {Enantioselective Synthesis of (S)-2-Hydroxypropanone Derivatives by Benzoylformate Decarboxylase Catalyzed C-C Bond Formation},
  series = {European journal of organic chemistry},
  volume    = {Vol. 2000},
  journal   = {European journal of organic chemistry},
  number    = {Iss. 11},
  issn      = {0365-5490 (E-Journal); 1099-0690 (E-Journal); 0075-4617 (Print); 0170-2041 (Print); 0947-3440 (Print); 1434-193X (Print); 1434-243X (Print)},
  pages     = {2161 -- 2170},
  year      = {2000},
  language  = {en}
}
@article{IdingDuennwaldGreineretal.2000,
  author    = {Iding, Hans and D{\"u}nnwald, Thomas and Greiner, Lasse and Liese, Andreas and M{\"u}ller, Michael and Siegert, Petra and Gr{\"o}tzinger, Joachim and Demir, Ayhan S. and Pohl, Martina},
  title     = {Benzoylformate Decarboxylase from Pseudomonas putida as Stable Catalyst for the Synthesis of Chiral 2-Hydroxy Ketones},
  series = {Chemistry - a European journal},
  volume    = {Vol. 6},
  journal   = {Chemistry - a European journal},
  number    = {Iss. 8},
  issn      = {1521-3765 (E-Journal); 0947-6539 (Print)},
  pages     = {1483 -- 1495},
  year      = {2000},
  language  = {en}
}
@article{IdingSiegertMeschetal.1998,
  author    = {Iding, Hans and Siegert, Petra and Mesch, K. and Pohl, Martina},
  title     = {Application of α-keto acid decarboxylases in biotransformations},
  series = {Biochimica et biophysica acta (BBA) - Protein structure and molecular enzymology},
  volume    = {Vol. 1385},
  journal   = {Biochimica et biophysica acta (BBA) - Protein structure and molecular enzymology},
  number    = {Iss. 2},
  issn      = {1879-2588 (E-Journal); 0167-4838 (Print)},
  pages     = {307 -- 322},
  year      = {1998},
  language  = {en}
}
@article{PohlSiegertMeschetal.1998,
  author    = {Pohl, Martina and Siegert, Petra and Mesch, K. and Bruhn, H. and Gr{\"o}tzinger, Joachim},
  title     = {Active site mutants of pyruvate decarboxylase from Zymomonas mobilis : a site-directed mutagenesis study of L112, I472, I476, E473 and N482},
  series = {European journal of biochemistry},
  volume    = {Vol. 257},
  journal   = {European journal of biochemistry},
  number    = {Iss. 3},
  issn      = {1432-1033 (E-Journal); 1742-4658 (E-Journal); 0014-2956 (Print); 1742-464X (Print)},
  pages     = {538 -- 546},
  year      = {1998},
  language  = {en}
}
@article{RatkeMilowLisinskietal.2014,
  author    = {Ratke, Lorenz and Milow, Barbara and Lisinski, Susanne and Hoepfner, Sandra},
  title     = {On an effect of fine ceramic particles on the structure of aerogels},
  series = {Microgravity science and technology},
  volume    = {26},
  journal   = {Microgravity science and technology},
  publisher = {Springer Nature},
  address   = {Heidelberg},
  issn      = {0938-0108 ; 1875-0494},
  doi       = {10.1007/s12217-014-9380-2},
  pages     = {103 -- 110},
  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}
}