Berlin 2012 – wissenschaftliches Programm

Bereiche | Tage | Auswahl | Suche | Aktualisierungen | Downloads | Hilfe

CPP: Fachverband Chemische Physik und Polymerphysik

CPP 30: New Perspectives of Scattering at Soft Matter

CPP 30.4: Vortrag

Mittwoch, 28. März 2012, 16:00–16:15, C 264

Dynamics in an enzyme containing bicontinuous microemulsion: A quasielastic scattering study — Ralph Neubauer¹, Stefan Wellert², Andreas Richardt³, Marc-Michael Blum⁴, and •Thomas Hellweg¹ — ¹Phys. und Biophys. Chemie (PC III), Universität Bielefeld, Universitätsstr. 25, 33615 Bielefeld, Germany — ²Stranski Lab. f. Physikalische und Theoretische Chemie, TU Berlin, Straße des 17. Juni 124, 10623 Berlin, Germany — ³WIS Munster, ABC-Schutz, Humboldtstraße 100, 29633 Munster, Germany — ⁴Blum-Scientific Services, Ledererstraße 23, 80331 Munich, Germany

The enzyme diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris is of relevance due to its ability to catalyze the hydrolysis of highly toxic organophosphates. In the present work, the enzyme structure in solution (native state) is studied by different scattering methods. The results are compared to hydrodynamic model calculations. Bicontinuous microemulsions (bME) made of sugar surfactants are discussed as reaction media for the DFPase. The bME remains stable in the presence of the enzyme, which is revealed by scattering experiments. It is shown that the DFPase still has a high activity in the bME [1]. The collective and the local motion of the surfactant interface in the bME is studied by means of neutron spin-echo. Moreover, it is tried to study the enzyme motion decoupled from the microemulsion by contrast variation.
[1]S. Wellert, B. Tiersch, J. Koetz, A. Richardt, A. Lapp, J. Gäb, O. Holderer, M.-M. Blum, C. Schulreich, R. Stehle und T. Hellweg; European Biophys. J., 40:761–774, 2011.