Original Paper

European Biophysics Journal

, Volume 40, Issue 6, pp 761-774

The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity

  • Stefan WellertAffiliated withTU Berlin, Institut für Chemie, Stranski-Laboratorium für Physikalische und Theoretische Chemie Email author 
  • , Brigtte TierschAffiliated withInstitut für Chemie, Universität Potsdam
  • , Joachim KoetzAffiliated withInstitut für Chemie, Universität Potsdam
  • , André RichardtAffiliated withWehrwissenschaftliches Institut für Schutztechnologien–ABC-Schutz
  • , Alain LappAffiliated withLaboratoire Léon Brillouin, C.E.A.-C.E.N. Saclay
  • , Olaf HoldererAffiliated withJülich Center for Neutron Scattering, FRM II Garching
  • , Jürgen GäbAffiliated withBlum-Scientific ServicesInstitute of Pharmaceutical Chemistry, Phillipps University Marburg
  • , Marc-Michael BlumAffiliated withTU Berlin, Institut für Chemie, Stranski-Laboratorium für Physikalische und Theoretische ChemieBlum-Scientific ServicesBioscience Division, Los Alamos National Laboratory
  • , Christoph SchulreichAffiliated withPhysikalische und Biophysikalische Chemie
    • , Ralf StehleAffiliated withSoft Matter und Funktionale Materialien, Helmholtz-Zentrum Berlin für Materialien und Energie
    • , Thomas HellwegAffiliated withPhysikalische und Biophysikalische Chemie Email author 

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The enzyme diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris is of great interest because of its ability to catalyze the hydrolysis of highly toxic organophosphates. In this work, the enzyme structure in solution (native state) was studied by use of different scattering methods. The results are compared with those from hydrodynamic model calculations based on the DFPase crystal structure. Bicontinuous microemulsions made of sugar surfactants are discussed as host systems for the DFPase. The microemulsion remains stable in the presence of the enzyme, which is shown by means of scattering experiments. Moreover, activity assays reveal that the DFPase still has high activity in this complex reaction medium. To complement the scattering experiments cryo-SEM was also employed to study the microemulsion structure.


Dynamic light scattering Neutron spin echo Microemulsion Enzyme catalysis SANS Protein structure