K E Jaeger

Summary

Country: Germany

Publications

  1. ncbi request reprint Directed evolution of enantioselective enzymes for organic chemistry
    K E Jaeger
    Ruhr Universitat Bochum, Fakultat fur Biologie, Lehrstuhl für Biologie der Mikroorganismen, Bochum, 44780, Germany
    Curr Opin Chem Biol 4:68-73. 2000
  2. ncbi request reprint Microbial lipases form versatile tools for biotechnology
    K E Jaeger
    Lehrstuhl Biologie der Mikroorganismen, Ruhr Universitat, Bochum, Germany
    Trends Biotechnol 16:396-403. 1998
  3. ncbi request reprint Directed evolution and the creation of enantioselective biocatalysts
    K E Jaeger
    Ruhr Universitat Bochum, Lehrstuhl Biologie der Mikroorganismen, Germany
    Appl Microbiol Biotechnol 55:519-30. 2001
  4. ncbi request reprint Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases
    K E Jaeger
    Lehrstuhl Biologie der Mikroorganismen, Ruhr Universitat, Bochum, Germany
    Annu Rev Microbiol 53:315-51. 1999
  5. ncbi request reprint Extracellular lipase from Pseudomonas aeruginosa is an amphiphilic protein
    K E Jaeger
    Lehrstuhl für Biologie der Mikroorganismen, Ruhr Universitat, Bochum, Germany
    Biochim Biophys Acta 1120:315-21. 1992
  6. pmc Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase
    K Liebeton
    Lehrstuhl für Biologie der Mikroorganismen, Ruhr Universitat Bochum, D 44780 Bochum, Germany
    J Bacteriol 183:597-603. 2001
  7. ncbi request reprint Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional structure
    T Eggert
    Lehrstuhl Biologie der Mikroorganismen, , Germany
    FEBS Lett 502:89-92. 2001
  8. ncbi request reprint A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerases
    J L Arpigny
    Lehrstuhl für Biologie der Mikroorganismen, Ruhr Universitat Bochum, Germany
    FEMS Microbiol Lett 167:69-73. 1998
  9. pmc A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa
    S Wilhelm
    Lehrstuhl Biologie der Mikroorganismen, Ruhr Universitat, D 44780 Bochum, Germany
    J Bacteriol 181:6977-86. 1999
  10. pmc DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa
    A Urban
    , , D-44780 Bochum, Germany
    J Bacteriol 183:587-96. 2001

Collaborators

  • M T Reetz
  • J L Arpigny
  • T Eggert
  • K Liebeton
  • A Urban
  • S Wilhelm
  • M Leipelt
  • B W Dijkstra
  • A Zacharias
  • G van Pouderoyen
  • J Tommassen

Detail Information

Publications10

  1. ncbi request reprint Directed evolution of enantioselective enzymes for organic chemistry
    K E Jaeger
    Ruhr Universitat Bochum, Fakultat fur Biologie, Lehrstuhl für Biologie der Mikroorganismen, Bochum, 44780, Germany
    Curr Opin Chem Biol 4:68-73. 2000
    ..The creation of enantioselective enzymes by directed evolution will become an important technology in the near future...
  2. ncbi request reprint Microbial lipases form versatile tools for biotechnology
    K E Jaeger
    Lehrstuhl Biologie der Mikroorganismen, Ruhr Universitat, Bochum, Germany
    Trends Biotechnol 16:396-403. 1998
    ..Immobilization in hydrophobic sol-gel matrices and in vitro evolution are promising novel approaches to increasing the stability or enantioselectivity, respectively, of lipases...
  3. ncbi request reprint Directed evolution and the creation of enantioselective biocatalysts
    K E Jaeger
    Ruhr Universitat Bochum, Lehrstuhl Biologie der Mikroorganismen, Germany
    Appl Microbiol Biotechnol 55:519-30. 2001
    ..Enantioselectivity is a biocatalyst property of major biotechnological importance that is, however, difficult to deal with. We discuss recent examples of creating enantioselective biocatalysts by directed evolution...
  4. ncbi request reprint Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases
    K E Jaeger
    Lehrstuhl Biologie der Mikroorganismen, Ruhr Universitat, Bochum, Germany
    Annu Rev Microbiol 53:315-51. 1999
    ..At the same time, directed evolution in combination with appropriate screening systems will be used extensively as a novel approach to develop lipases with high stability and enantioselectivity...
  5. ncbi request reprint Extracellular lipase from Pseudomonas aeruginosa is an amphiphilic protein
    K E Jaeger
    Lehrstuhl für Biologie der Mikroorganismen, Ruhr Universitat, Bochum, Germany
    Biochim Biophys Acta 1120:315-21. 1992
    ..This result demonstrates that extracellular lipase of P. aeruginosa exhibits an amphiphilic character like intrinsic membrane proteins...
  6. pmc Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase
    K Liebeton
    Lehrstuhl für Biologie der Mikroorganismen, Ruhr Universitat Bochum, D 44780 Bochum, Germany
    J Bacteriol 183:597-603. 2001
    ..This conclusion was supported by the finding that the disulfide bond function could partly be substituted by a salt bridge constructed by changing the two cysteine residues to arginine and aspartate, respectively...
  7. ncbi request reprint Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional structure
    T Eggert
    Lehrstuhl Biologie der Mikroorganismen, , Germany
    FEBS Lett 502:89-92. 2001
    ....
  8. ncbi request reprint A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerases
    J L Arpigny
    Lehrstuhl für Biologie der Mikroorganismen, Ruhr Universitat Bochum, Germany
    FEMS Microbiol Lett 167:69-73. 1998
    ..The protein is highly thermostable and is able to hydrolyse a variety of lipid substrates thus providing a promising tool for potential biotechnological applications...
  9. pmc A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa
    S Wilhelm
    Lehrstuhl Biologie der Mikroorganismen, Ruhr Universitat, D 44780 Bochum, Germany
    J Bacteriol 181:6977-86. 1999
    ..To our knowledge, this esterase is unique in that it exemplifies in P. aeruginosa (i) the first enzyme identified in the outer membrane and (ii) the first example of a type IV secretion mechanism...
  10. pmc DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa
    A Urban
    , , D-44780 Bochum, Germany
    J Bacteriol 183:587-96. 2001
    ..We conclude that the correct formation of the disulfide bond catalyzed in vivo by DsbA is necessary to stabilize periplasmic lipase. Such a stabilization is the prerequisite for efficient secretion using the type II pathway...