@article{TuegBaumann1994, author = {T{\"u}g, Helmut and Baumann, Marcus}, title = {Problems of UV-B radiation measurements in biological research : critical remarks on current techniques and suggestions for improvements}, series = {Geophysical research letters}, volume = {Vol. 21}, journal = {Geophysical research letters}, number = {Iss. 8}, issn = {1944-8007 (E-Journal); 0094-8276 (Print)}, pages = {689 -- 692}, year = {1994}, language = {en} } @article{MedlinLangeBaumann1994, author = {Medlin, L. K. and Lange, M. and Baumann, Marcus}, title = {Genetic differentiation among three colony-forming species of Phaeocystis : further evidence for the phylogeny of the Prymnesiophyta}, series = {Phycologia}, volume = {Vol. 33}, journal = {Phycologia}, number = {Iss. 3}, issn = {0031-8884}, pages = {199 -- 212}, year = {1994}, language = {en} } @incollection{MedlinBarkerBaumannetal.1994, author = {Medlin, L. K. and Barker, G. L. A. and Baumann, Marcus and Hayes, P. K.}, title = {Molecular biology and systematics}, series = {The Haptophyte Algae (Special volume / Systematics Association : 51)}, booktitle = {The Haptophyte Algae (Special volume / Systematics Association : 51)}, publisher = {Clarendon Press}, address = {Oxford}, isbn = {0-19-857772-9}, pages = {393 -- 411}, year = {1994}, language = {en} } @article{TuegBaumann1995, author = {T{\"u}g, Helmut and Baumann, Marcus}, title = {Reply to the comments by R.L. McKenzie and P.V. Johnston on our paper "Problems of UV-B radiation measurements in biological research: Critical Remarks on current techniques and suggestions for improvements"}, series = {Geophysical research letters}, volume = {Vol. 22}, journal = {Geophysical research letters}, number = {Iss. 9}, issn = {1944-8007 (E-Journal); 0094-8276 (Print)}, pages = {1159 -- 1160}, year = {1995}, language = {en} } @inproceedings{BrandiniBaumann1997, author = {Brandini, Frederico P. and Baumann, Marcus}, title = {The potential role of melted 'brown ice' as sources of chelators and ammonia to the surface waters of the Weddell Sea, Antarctica}, series = {Proceedings of the NIPR Symposium on Polar Biology : 10}, booktitle = {Proceedings of the NIPR Symposium on Polar Biology : 10}, address = {Tokyo}, organization = {National Institute of Polar Research}, issn = {0914-563X}, pages = {1 -- 13}, year = {1997}, language = {en} } @misc{BesslerMaurerMerkeletal.2009, author = {Bessler, Cornelius and Maurer, Karl-Heinz and Merkel, Marion and Siegert, Petra and Wieland, Susanne}, title = {Subtilisin from Bacillus Pumilus and detergent and cleaning agents containing said novel subtilisin [US Patentanmeldung / Internationale Patentanmeldung]}, publisher = {USPTO; WIPO}, address = {Washington; Genf}, pages = {1 -- 39}, year = {2009}, language = {en} } @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{JakobMartinezMandaweetal.2013, author = {Jakob, Felix and Martinez, Ronny and Mandawe, John and Hellmuth, Hendrik and Siegert, Petra and Maurer, Karl-Heinz and Schwaneberg, Ulrich}, title = {Surface charge engineering of a Bacillus gibsonii subtilisin protease}, series = {Applied microbiology and biotechnology}, volume = {Vol. 97}, journal = {Applied microbiology and biotechnology}, number = {Iss. 15}, publisher = {Springer}, address = {Berlin}, issn = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)}, pages = {6793 -- 6802}, year = {2013}, 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{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} }