Karl Erich Jaeger

Summary

Country: Germany

Publications

  1. pmc Mechanism of acetaldehyde-induced deactivation of microbial lipases
    Benjamin Franken
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Forschungszentrum Julich GmbH, D 52426 Jülich, Germany
    BMC Biochem 12:10. 2011
  2. ncbi request reprint Lipases for biotechnology
    Karl Erich Jaeger
    Institute for Molecular Enzyme Technology, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, D 52425, Julich, Germany
    Curr Opin Biotechnol 13:390-7. 2002
  3. ncbi request reprint Enantioselective biocatalysis optimized by directed evolution
    Karl Erich Jaeger
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universität Duesseldorf, Forschungszentrum Juelich, D 52426 Juelich, Germany
    Curr Opin Biotechnol 15:305-13. 2004
  4. ncbi request reprint Biocatalytic production of enantiopure cyclohexane-trans-1,2-diol using extracellular lipases from Bacillus subtilis
    Jean Detry
    Institut für Biotechnologie 2, Forschungszentrum Julich, D 52425 Julich, Germany
    Appl Microbiol Biotechnol 72:1107-16. 2006
  5. doi request reprint Novel broad host range shuttle vectors for expression in Escherichia coli, Bacillus subtilis and Pseudomonas putida
    Sonja Christina Troeschel
    Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Center Juelich, D 52426 Juelich, Germany
    J Biotechnol 161:71-9. 2012
  6. ncbi request reprint Novel biocatalysts for white biotechnology
    Thomas Drepper
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Center Julich, Julich, Germany
    Biotechnol J 1:777-86. 2006
  7. ncbi request reprint Combination of computational prescreening and experimental library construction can accelerate enzyme optimization by directed evolution
    Susanne Aileen Funke
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, Germany
    Protein Eng Des Sel 18:509-14. 2005
  8. doi request reprint Conservation of dark recovery kinetic parameters and structural features in the pseudomonadaceae "short" light, oxygen, voltage (LOV) protein family: implications for the design of LOV-based optogenetic tools
    Raj Rani
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, Stetternicher Forst, D 52426 Jülich, Germany
    Biochemistry 52:4460-73. 2013
  9. doi request reprint A T7 RNA polymerase-based toolkit for the concerted expression of clustered genes
    Solmaz Arvani
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, D 52426 Jülich, Germany
    J Biotechnol 159:162-71. 2012
  10. doi request reprint Structural basis for the slow dark recovery of a full-length LOV protein from Pseudomonas putida
    Franco Circolone
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, D 52426 Jülich, Germany
    J Mol Biol 417:362-74. 2012

Collaborators

Detail Information

Publications47

  1. pmc Mechanism of acetaldehyde-induced deactivation of microbial lipases
    Benjamin Franken
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Forschungszentrum Julich GmbH, D 52426 Jülich, Germany
    BMC Biochem 12:10. 2011
    ..Previous studies showed that several lipases were sensitive toward acetaldehyde deactivation whereas others were insensitive; however, a general explanation of the acetaldehyde-induced inactivation mechanism is missing...
  2. ncbi request reprint Lipases for biotechnology
    Karl Erich Jaeger
    Institute for Molecular Enzyme Technology, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, D 52425, Julich, Germany
    Curr Opin Biotechnol 13:390-7. 2002
    ..Furthermore, novel biotechnological applications have been successfully established using lipases for the synthesis of biopolymers and biodiesel, the production of enantiopure pharmaceuticals, agrochemicals, and flavour compounds...
  3. ncbi request reprint Enantioselective biocatalysis optimized by directed evolution
    Karl Erich Jaeger
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universität Duesseldorf, Forschungszentrum Juelich, D 52426 Juelich, Germany
    Curr Opin Biotechnol 15:305-13. 2004
    ....
  4. ncbi request reprint Biocatalytic production of enantiopure cyclohexane-trans-1,2-diol using extracellular lipases from Bacillus subtilis
    Jean Detry
    Institut für Biotechnologie 2, Forschungszentrum Julich, D 52425 Julich, Germany
    Appl Microbiol Biotechnol 72:1107-16. 2006
    ....
  5. doi request reprint Novel broad host range shuttle vectors for expression in Escherichia coli, Bacillus subtilis and Pseudomonas putida
    Sonja 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...
  6. ncbi request reprint Novel biocatalysts for white biotechnology
    Thomas Drepper
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Center Julich, Julich, Germany
    Biotechnol J 1:777-86. 2006
    ..Furthermore, we have isolated and characterized biocatalysts relevant for the preparation of enantiopure compounds...
  7. ncbi request reprint Combination of computational prescreening and experimental library construction can accelerate enzyme optimization by directed evolution
    Susanne Aileen Funke
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, Germany
    Protein Eng Des Sel 18:509-14. 2005
    ..Both QM/MM-based calculations and molecular biology experiments identify histidine 76 as a residue that strongly affects the catalytic activity. The experiments demonstrate its important influence on enantioselectivity...
  8. doi request reprint Conservation of dark recovery kinetic parameters and structural features in the pseudomonadaceae "short" light, oxygen, voltage (LOV) protein family: implications for the design of LOV-based optogenetic tools
    Raj Rani
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, Stetternicher Forst, D 52426 Jülich, Germany
    Biochemistry 52:4460-73. 2013
    ..e., LOV-based optogenetic tools). ..
  9. doi request reprint A T7 RNA polymerase-based toolkit for the concerted expression of clustered genes
    Solmaz Arvani
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, D 52426 Jülich, Germany
    J Biotechnol 159:162-71. 2012
    ..Our findings clearly indicate that due to its unique properties T7 RNA polymerase can be applied for overexpression of large and complex bacterial gene regions...
  10. doi request reprint Structural basis for the slow dark recovery of a full-length LOV protein from Pseudomonas putida
    Franco Circolone
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, D 52426 Jülich, Germany
    J Mol Biol 417:362-74. 2012
    ..The overall structural arrangement of PpSB1-LOV, together with a complementary phylogenetic analysis, highlights a common ancestry of bacterial LOV photoreceptors and Per-ARNT-Sim chemosensors...
  11. ncbi request reprint Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation
    Denis Tielker
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Juelich, D 52426 Juelich, Germany
    Microbiology 151:1313-23. 2005
    ..Staining of biofilm cells using fluorescently labelled LecB confirmed the presence of these ligands...
  12. doi request reprint TREX: a universal tool for the transfer and expression of biosynthetic pathways in bacteria
    Anita Loeschcke
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Center Julich, Julich, Germany
    ACS Synth Biol 2:22-33. 2013
    ..Thus, TREX represents a valuable tool for accessing natural products by allowing comparative expression studies with clustered genes...
  13. pmc Cofactor trapping, a new method to produce flavin mononucleotide
    Ulrich Krauss
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, D 52426 Jülich, Germany
    Appl Environ Microbiol 77:1097-100. 2011
    ..This approach uses an overexpressed flavoprotein to trap FMN, which is thus removed from the cascade regulating FMN production in E. coli. This, in turn, allows the isolation of highly pure FMN...
  14. doi request reprint LOVely enzymes - towards engineering light-controllable biocatalysts
    Ulrich Krauss
    Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Centre Juelich, D 52426 Juelich, Germany
    Microb Biotechnol 3:15-23. 2010
    ..Hence, it appears that fusion of LOV photoreceptors to functional enzyme target sites via appropriate linker structures may represent a straightforward strategy to design light controllable biocatalysts...
  15. doi request reprint Lights on and action! Controlling microbial gene expression by light
    Thomas Drepper
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Forschungszentrum Julich, Stetternicher Forst, 52426, Julich, Germany
    Appl Microbiol Biotechnol 90:23-40. 2011
    ....
  16. ncbi request reprint Extracellular lipases from Bacillus subtilis: regulation of gene expression and enzyme activity by amino acid supply and external pH
    Thorsten Eggert
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universität Duesseldorf, Forschungszentrum Juelich, D 52426 Juelich, Germany
    FEMS Microbiol Lett 225:319-24. 2003
    ..The expression of lipA was repressed by high amino acid concentrations, whereas the lipB gene expression remained unaffected...
  17. pmc Fusion of a flavin-based fluorescent protein to hydroxynitrile lyase from Arabidopsis thaliana improves enzyme stability
    Kathrin Emmi Scholz
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universität Düsseldorf and Forschungszentrum Jülich, Julich, Germany
    Appl Environ Microbiol 79:4727-33. 2013
    ..The fusion strategy presented here reveals a surprising means for the stabilization of enzymes and stresses the importance of a thorough in vitro characterization of in vivo-employed fluorescent fusion proteins. ..
  18. pmc Synthesis of chiral cyanohydrins by recombinant Escherichia coli cells in a micro-aqueous reaction system
    Kathrin Emmi Scholz
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universität Düsseldorf and Forschungszentrum Jülich, Julich, Germany
    Appl Environ Microbiol 78:5025-7. 2012
    ..Microscopy studies employing a fusion of AtHNL with a flavin-based fluorescent protein (FbFP) reveal that the cells remain intact in the reaction system...
  19. doi request reprint Rapid sequence scanning mutagenesis using in silico oligo design and the Megaprimer PCR of whole plasmid method (MegaWHOP)
    Ulrich Krauss
    Institute of Molecular Enzyme Technology, Research Centre Julich, Heinrich Heine University, Dusseldorf, Julich, Germany
    Methods Mol Biol 634:127-35. 2010
    ....
  20. doi request reprint Enlightened enzymes: strategies to create novel photoresponsive proteins
    Ulrich Krauss
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Forschungszentrum Julich, Julich, Germany
    Chemistry 17:2552-60. 2011
    ..Recent cell biological examples will be highlighted and possible biotechnological applications will be presented...
  21. ncbi request reprint Multiplex-PCR-based recombination as a novel high-fidelity method for directed evolution
    Thorsten Eggert
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, 52426 Julich, Germany
    Chembiochem 6:1062-7. 2005
    ....
  22. ncbi request reprint Lipase-specific foldases
    Frank Rosenau
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, 52428 Jülich, Germany
    Chembiochem 5:152-61. 2004
    ....
  23. pmc Distribution and phylogeny of light-oxygen-voltage-blue-light-signaling proteins in the three kingdoms of life
    Ulrich Krauss
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, Julich, Germany
    J Bacteriol 191:7234-42. 2009
    ....
  24. pmc Flavin mononucleotide-based fluorescent reporter proteins outperform green fluorescent protein-like proteins as quantitative in vivo real-time reporters
    Thomas Drepper
    Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Center Juelich, Stetternicher Forst, D 52426 Juelich, Germany
    Appl Environ Microbiol 76:5990-4. 2010
    ..Instead, flavin mononucleotide (FMN)-binding fluorescent proteins (FbFPs) are suitable for quantitative real-time in vivo assays under these conditions...
  25. pmc Structural and functional characterisation of TesA - a novel lysophospholipase A from Pseudomonas aeruginosa
    Filip Kovačić
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungszentrum Julich, Julich, Germany
    PLoS ONE 8:e69125. 2013
    ..aeruginosa. The enzyme is localized in the periplasm and may exert important functions in the homeostasis of phospholipids or detoxification of lysophospholipids. ..
  26. doi request reprint The subcellular localization of a C-terminal processing protease in Pseudomonas aeruginosa
    Rien 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...
  27. pmc Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides
    Christian Degering
    Institute of Molecular Enzyme Technology, Heinrich Heine Universitat Dusseldorf, Research Center Julich, Julich, Germany
    Appl Environ Microbiol 76:6370-6. 2010
    ....
  28. doi request reprint Lipase LipC affects motility, biofilm formation and rhamnolipid production in Pseudomonas aeruginosa
    Frank 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...
  29. doi request reprint A novel T7 RNA polymerase dependent expression system for high-level protein production in the phototrophic bacterium Rhodobacter capsulatus
    Nadine Katzke
    Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Forschungszentrum Juelich, Stetternicher Forst, D 52426 Juelich, Germany
    Protein Expr Purif 69:137-46. 2010
    ..capsulatus cultures. This result clearly indicates that the novel R. capsulatus-based expression system is well suited for the high-level expression of soluble proteins...
  30. ncbi request reprint Reporter proteins for in vivo fluorescence without oxygen
    Thomas Drepper
    Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Center Juelich, Stetternicher Forst, D 52426 Juelich, Germany
    Nat Biotechnol 25:443-5. 2007
    ....
  31. doi request reprint Mutual exchange of kinetic properties by extended mutagenesis in two short LOV domain proteins from Pseudomonas putida
    Katrin Jentzsch
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, FZ Julich, Stetternicher Forst D 52426 Jülich, Germany
    Biochemistry 48:10321-33. 2009
    ....
  32. pmc The autotransporter esterase EstA of Pseudomonas aeruginosa is required for rhamnolipid production, cell motility, and biofilm formation
    Susanne 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...
  33. ncbi request reprint A novel transposon for functional expression of DNA libraries
    Christian Leggewie
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universität Duesseldorf, Forschungszentrum Juelich, D 52426 Juelich, Germany
    J Biotechnol 123:281-7. 2006
    ..Furthermore, this transposon allows the bidirectional sequencing of the respective clones starting from unique primer binding sites...
  34. ncbi request reprint Prospecting for biocatalysts and drugs in the genomes of non-cultured microorganisms
    Wolfgang R Streit
    Institut fur Mikrobiologie und Genetik, Universitat Gottingen, Grisebachstrasse 8, D 37077 Gottingen, Germany
    Curr Opin Biotechnol 15:285-90. 2004
    ..So far, metagenome-based approaches have led to the isolation of many novel biocatalysts and a variety of other molecules with a high potential for downstream applications...
  35. ncbi request reprint Learning from directed evolution: theoretical investigations into cooperative mutations in lipase enantioselectivity
    Marco Bocola
    Max Planck Institut fur Kohlenforschung, Kaiser Wilhelm Platz 1, 45470 Mulheim an der Ruhr, Germany
    Chembiochem 5:214-23. 2004
    ..The simulations provide insight into remote and cooperative effects of mutations...
  36. ncbi request reprint Select the best: novel biocatalysts for industrial applications
    Monika Konarzycka-Bessler
    Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Centre Juelich, D 52428 Juelich, Germany
    Trends Biotechnol 24:248-50. 2006
    ....
  37. ncbi request reprint Learning from directed evolution: Further lessons from theoretical investigations into cooperative mutations in lipase enantioselectivity
    Manfred T Reetz
    Max Planck Institut fur Kohlenforschung, Kaiser Wilhelm Platz 1, 45470 Mulheim Ruhr, Germany
    Chembiochem 8:106-12. 2007
    ..This study supports our original postulate regarding the relay mechanism, offers further mechanistic insight into the role of individual mutations, and provides mutants that display even higher enantioselectivity (E of up to 64)...
  38. ncbi request reprint Functional cell-surface display of a lipase-specific chaperone
    Susanne Wilhelm
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Centre Julich, 52426 Julich, Germany
    Chembiochem 8:55-60. 2007
    ..The foldase autodisplay system reported here can be used for a variety of applications including the ultrahigh-throughput screening of large libraries of foldase variants generated by directed evolution...
  39. pmc Identification of novel benzoylformate decarboxylases by growth selection
    Helge Henning
    Institute of Molecular Enzyme Technology, Heinrich Heine University Duesseldorf, Research Centre Juelich, D 52426 Jülich, Germany
    Appl Environ Microbiol 72:7510-7. 2006
    ....
  40. pmc Hexadecane and Tween 80 stimulate lipase production in Burkholderia glumae by different mechanisms
    Bouke K H L Boekema
    Department of Molecular Microbiology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands
    Appl Environ Microbiol 73:3838-44. 2007
    ..In conclusion, hexadecane and Tween 80 enhance lipase production in B. glumae, and they act via different mechanisms...
  41. doi request reprint Mutations towards enantioselectivity adversely affect secretion of Pseudomonas aeruginosa lipase
    Sascha 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...
  42. doi request reprint Single-cell high-throughput screening to identify enantioselective hydrolytic enzymes
    Stefan Becker
    Institute for Biochemistry and Organic Chemistry, Technische Universitat Darmstadt, Petersenstrasse 22, 64287 Darmstadt, Germany
    Angew Chem Int Ed Engl 47:5085-8. 2008
  43. ncbi request reprint A generic system for the Escherichia coli cell-surface display of lipolytic enzymes
    Stefan Becker
    Abteilung für Molekulare Genetik und Präparative Molekularbiologie, Institut fur Mikrobiologie und Genetik, Georg August Universitat Gottingen, Grisebachstrasse 8, D 37077 Gottingen, Germany
    FEBS Lett 579:1177-82. 2005
    ..EstA provides a useful tool for surface display of lipases including variant libraries generated by directed evolution thereby enabling the identification of novel enzymes with interesting biological and biotechnological ramifications...
  44. ncbi request reprint A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens
    Reto Meier
    Department of Chemistry and Biochemistry, University Bern Freiestrasse 3, CH 3012 Bern, Switzerland
    J Biol Chem 282:31477-83. 2007
    ..The analysis of the properties of the beta-roll domains suggests an intramolecular chaperone function...
  45. ncbi request reprint Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV-LOV dimerization and interdomain interactions
    Valentina Buttani
    Dept of Physics, University of Parma, via G P Usberti 7 A, 43100 Parma, Italy
    Photochem Photobiol Sci 6:41-9. 2007
    ..The data uncover a common surface for LOV-LOV and intraprotein interaction, involving the central beta-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins...
  46. ncbi request reprint Lectin-based affinity tag for one-step protein purification
    Denis 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...
  47. ncbi request reprint Ultrahigh-throughput screening to identify E. coli cells expressing functionally active enzymes on their surface
    Stefan Becker
    Department of Biochemistry, Clemens Schöpf Institute, Darmstadt University of Technology, Petersenstrasse 22, Darmstadt, Germany
    Chembiochem 8:943-9. 2007
    ..This strategy of covalently attaching a biotin label to esterase-proficient bacteria might open new avenues to ultrahigh-throughput screening of enzyme libraries for hydrolytic enzymes with enhanced activities or enantioselectivities...