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@ARTICLE{Wellert:15317,
      author       = {Wellert, S. and Tiersch, B. and Koetz, J. and Richardt, A.
                      and Lapp, A. and Holderer, O. and Gäb, J. and Blum, M.-M.
                      and Schulreich, C. and Stehle, R. and Hellweg, T.},
      title        = {{T}he {DFP}ase from {L}oligo vulgaris in sugar
                      surfactant-based bicontinuous microemulsions: structure,
                      dynamics, and enzyme activity},
      journal      = {European biophysics journal},
      volume       = {40},
      issn         = {0175-7571},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PreJuSER-15317},
      pages        = {761 - 774},
      year         = {2011},
      note         = {J.G. and M.M.B. were supported by the German Ministry of
                      Defense under contract E/UR3G/6G115/6A801. T. H., R. S., C.
                      S. also were financed by the German Ministry of Defense
                      (Contracts E/E590/9Z004/5F159 and E/E590/8Z002/4F170). The
                      SANS experiments were supported by the European Union
                      through the NMI3 program. We are grateful to the Laboratoire
                      Leon Brillouin and the Julich Center for Neutron Scattering
                      at the FRM II for providing beamtime.},
      abstract     = {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.},
      keywords     = {Animals / Carbohydrates: chemistry / Carbohydrates:
                      pharmacology / Emulsions / Loligo: enzymology / Loligo:
                      metabolism / Microscopy, Electron, Scanning / Neutron
                      Diffraction / Phosphoric Triester Hydrolases: analysis /
                      Phosphoric Triester Hydrolases: chemistry / Phosphoric
                      Triester Hydrolases: metabolism / Scattering, Small Angle /
                      Solutions: chemistry / Surface-Active Agents: chemistry /
                      Surface-Active Agents: pharmacology / Carbohydrates (NLM
                      Chemicals) / Emulsions (NLM Chemicals) / Solutions (NLM
                      Chemicals) / Surface-Active Agents (NLM Chemicals) /
                      Phosphoric Triester Hydrolases (NLM Chemicals) /
                      diisopropyl-fluorophosphatase (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
                      Science JCNS (München) ; JCNS-FRM-II / JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / Großgeräte für die Forschung
                      mit Photonen, Neutronen und Ionen (PNI)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
      experiment   = {EXP:(DE-MLZ)J-NSE-20140101},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21416312},
      UT           = {WOS:000290331400006},
      doi          = {10.1007/s00249-011-0689-0},
      url          = {https://juser.fz-juelich.de/record/15317},
}