Affiliation: University of Ulm
- Interaction between extracellular lipase LipA and the polysaccharide alginate of Pseudomonas aeruginosaPetra Tielen
Department of Aquatic Microbiology, University of Duisburg Essen, Faculty of Chemistry, Biofilm Centre, Essen, Germany
BMC Microbiol 13:159. 2013..The focus of the current study was the interaction between extracellular lipase LipA and alginate, which may be physiologically relevant in biofilms of mucoid P. aeruginosa...
- Lipase LipC affects motility, biofilm formation and rhamnolipid production in Pseudomonas aeruginosaFrank Rosenau
Institute for Molecular Enzyme Technology, Research Centre Juelich, Heinrich Heine University Duesseldorf, Juelich, Germany
FEMS Microbiol Lett 309:25-34. 2010..Also, the P. aeruginosa lipC mutant showed a significantly altered biofilm architecture. Proteome analysis revealed the accumulation of the response regulator protein PhoP in the lipC mutant...
- The autotransporter esterase EstA of Pseudomonas aeruginosa is required for rhamnolipid production, cell motility, and biofilm formationSusanne Wilhelm
Institute for Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Centre Juelich, Stetternicher Forst, D 52426 Juelich, Germany
J Bacteriol 189:6695-703. 2007..None of the mutant phenotypes could be complemented by expression of EstA*, demonstrating that the phenotypes affected by the estA mutation depend on the enzymatically active protein...
- Specific association of lectin LecB with the surface of Pseudomonas aeruginosa: role of outer membrane protein OprFHorst Funken
Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Juelich, Germany
PLoS ONE 7:e46857. 2012..In an OprF-deficient P. aeruginosa mutant, LecB is no longer detectable in the membrane but instead in the culture supernatant indicating a specific interaction between LecB and OprF...
- Novel broad host range shuttle vectors for expression in Escherichia coli, Bacillus subtilis and Pseudomonas putidaSonja Christina Troeschel
Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Center Juelich, D 52426 Juelich, Germany
J Biotechnol 161:71-9. 2012..subtilis and cutinase from the eukaryotic fungus Fusarium solani pisi in three different host strains. Additionally, we report here the construction of a T7 RNA polymerase-based expression strain of P. putida...
- Mutations towards enantioselectivity adversely affect secretion of Pseudomonas aeruginosa lipaseSascha Hausmann
Research Centre Juelich, Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Juelich, Germany
FEMS Microbiol Lett 282:65-72. 2008..We report here the identification of two amino acid substitutions located on the protein surface, which significantly impair lipase secretion...
- Autotransporters with GDSL passenger domains: molecular physiology and biotechnological applicationsSusanne Wilhelm
Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Center Julich, Juelich, Germany
Chembiochem 12:1476-85. 2011..Furthermore, it is capable of displaying different classes of enzymes in a range of Gram-negative bacteria including Escherichia coli, and FACS-based high-throughput screening for enantioselective esterases could be achieved using EstA...
- The lipase LipA (PA2862) but not LipC (PA4813) from Pseudomonas aeruginosa influences regulation of pyoverdine production and expression of the sigma factor PvdSHorst Funken
Institute of Pharmaceutical Biotechnology, Ulm University, Albert Einstein Allee 11, D 89069 Ulm, Germany
J Bacteriol 193:5858-60. 2011..PvdS expression itself is also influenced by iron-independent stimuli. We show that pyoverdine production and pvdS expression depend on one of the two lipases of P. aeruginosa...
- The subcellular localization of a C-terminal processing protease in Pseudomonas aeruginosaRien Hoge
Research Centre Juelich, Institute for Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Juelich, Germany
FEMS Microbiol Lett 316:23-30. 2011..Our results provide experimental evidence for the generally accepted hypothesis that CTPs are located in the periplasmic space of Gram-negative bacteria...
- Lectin-based affinity tag for one-step protein purificationDenis Tielker
Heinrich Heine University Duesseldorf, Juelich, Germany
Biotechniques 41:327-32. 2006..In conclusion, our results indicate that the lectin LecB of P. aeruginosa can be used as a tag for the high-yield one-step purification of recombinant proteins...
- Growth independent rhamnolipid production from glucose using the non-pathogenic Pseudomonas putida KT2440Andreas Wittgens
Institute for Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Forschungszentrum Julich, D 52426 Jülich, Germany
Microb Cell Fact 10:80. 2011..aeruginosa. In addition, separation of rhamnolipids from fatty acids is difficult and hence costly...