@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{BarbazanHagenbachPaulssenetal.2010, author = {Barbaz{\´a}n, Paula and Hagenbach, Adelheid and Paulßen, Elisabeth and Abram, Ulrich and Carballo, Rosa and Rodriguez-Hermida, Sabina and V{\´a}zquez-L{\´o}pez, Ezequiel M.}, title = {Tricarbonyl Rhenium(I) and Technetium(I) Complexes with Hydrazones Derived from 4,5-Diazafluoren-9-one and 1,10-Phenanthroline-5,6-dione}, series = {European Journal of Inorganic Chemistry}, journal = {European Journal of Inorganic Chemistry}, number = {29}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1099-0682}, doi = {10.1002/ejic.201000522}, pages = {4622 -- 4630}, year = {2010}, abstract = {Tricarbonylrhenium(I) and -technetium(I) halide (halide = Cl and Br) complexes of ligands derived from 4,5-diazafluoren-9-one (df) and 1,10-phenanthroline-5,6-dione (phen) derivatives of benzoic and 2-hydroxybenzoic acid hydrazides have been prepared. The complexes have been characterized by elemental analysis, MS, IR, 1H NMR and absorption and emission UV/Vis spectroscopic methods. The metal centres (ReI and TcI) are coordinated through the nitrogen imine atoms and establish five-membered chelate rings, whereas the hydrazone groups stand uncoordinated. The 1H NMR spectra suggest the same behaviour in solution on the basis of only marginal variations in the chemical shifts of the hydrazine protons.}, 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} } @article{BaumannLaraHubbertenetal.1997, author = {Baumann, Marcus and Lara, R.J. and Hubberten, D.N. and Thomas, D. N.}, title = {Dissolved organic matter studies in enclosed systems: Application of hydophobic fractionation for the assessment of organic nitrogen dynamics / Lara, R.J. ; Hubberten, U. ; Thomas, D.N. ; Baumann, M.E.M. ; Kattner, G.}, series = {Journal of Marine Systems. 13 (1997), H. 1-4}, journal = {Journal of Marine Systems. 13 (1997), H. 1-4}, isbn = {0924-7963}, pages = {155 -- 161}, year = {1997}, language = {en} } @article{BaumannThomasGleitz1992, author = {Baumann, Marcus and Thomas, D. N. and Gleitz, M.}, title = {Efficiency of carbon assimilation and photoacclimation in a small unicellular Chaetoceros species from the Weddel Sea (Antarctica): Influence of temperature and irridiance / Thomas, D. ; Baumann, M.E.M. ; Gleitz, M.}, series = {Journal of Experimental Marine Biology and Ecology. 157 (1992), H. 2}, journal = {Journal of Experimental Marine Biology and Ecology. 157 (1992), H. 2}, isbn = {0022-0981}, pages = {195 -- 209}, year = {1992}, 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 and Applied Physics}, volume = {48}, journal = {Indian Journal of Pure and Applied Physics}, number = {11}, publisher = {Council Of Scientific And Industrial Research (CSIR), National Institute Of Science Communication and Policy Research (NIScPR)}, address = {New Delhi}, isbn = {0019-5596}, pages = {782 -- 786}, year = {2010}, abstract = {The optical study carried out on insulating polymers namely polyethyleneterephthalate (PET) and polyvinylchloride (PVC) has been described. The polymers are exposed to different radiation doses by exposing them to swift heavy ions of carbon (90 MeV), silicon (120 MeV) and nickel (100 MeV) which influence on their optical properties. The studies show that amongst the investigated polymers, PVC and PET have potential for application as dosimeter beyond a threshold dose which is strongly dependent on the nature of the material and the radiation type. The optical micrographs show a distinct change in colour of the sample with increase in radiation dose.}, language = {en} } @article{BodeBartschBoulikasetal.1998, author = {Bode, J{\"u}rgen and Bartsch, J{\"o}rg W. and Boulikas, Toulikas and Iber, Michaela and Mielke, Christian and Sch{\"u}beler, Dirk and Seibler, Jost and Benham, Craig}, title = {Transcription-promoting genomic sites in mammalia: their elucidation and architectural principles}, series = {Gene therapy \& molecular biology}, volume = {1}, journal = {Gene therapy \& molecular biology}, number = {1}, issn = {1529-9120}, pages = {1 -- 29}, year = {1998}, language = {en} } @article{MangHodeniusSchmitzRodeetal.2009, author = {Mang, Thomas and Hodenius, Michael A. J. and Schmitz-Rode, Thomas and Baumann, Martin and Ivanova, Gergana and Wong, John Erik and Haulena, Friedhelm and Soenen, Stefaan J. H. and de Cuyper, Marcel}, title = {Absorption of 10-hydroxycamptothecin into the coat of magnetoliposomes / Hodenius, M. A. J. ; Schmitz-Rode, T. ; Baumann, M. ; Ivoanova, G. ; Wong, J. E. ; Mang, T. ; Haulena, F. ; Soenen, S. J. H. ; De Cuyper, M.}, series = {Colloids and Surfaces A: Physicochemical and Engineering Aspects. 343 (2009), H. 1-3}, journal = {Colloids and Surfaces A: Physicochemical and Engineering Aspects. 343 (2009), H. 1-3}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {0927-7757}, pages = {20 -- 23}, year = {2009}, language = {en} }