This title appears in the Scientific Report : 2011 

The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity
Wellert, S.
Tiersch, B. / Koetz, J. / Richardt, A. / Lapp, A. / Holderer, O. / Gäb, J. / Blum, M.-M. / Schulreich, C. / Stehle, R. / Hellweg, T.
Neutronenstreuung ; ICS-1
Neutronenstreuung ; Neutronenstreuung; JCNS-1
European biophysics journal, 40 (2011) S. 761 - 774
Berlin Springer 2011
761 - 774
Journal Article
Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
European Biophysics Journal : with Biophysics Letters 40
Please use the identifier: in citations.
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.