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

  • 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.

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Metadaten
Author:Stefan Wellert, Brigitte Tiersch, Joachim KoetzORCiDGND, Andre Richardt, Alain Lapp, Olaf Holderer, Juergen Gaeb, Marc-Michael Blum, Christoph Schulreich, Ralf Stehle, Thomas Hellweg
DOI:https://doi.org/10.1007/s00249-011-0689-0
ISSN:0175-7571 (print)
Parent Title (English):European biophysics journal : with biophysics letters ; an international journal of biophysics
Publisher:Springer
Place of publication:New York
Document Type:Article
Language:English
Year of first Publication:2011
Year of Completion:2011
Release Date:2017/03/26
Tag:Dynamic light scattering; Enzyme catalysis; Microemulsion; Neutron spin echo; Protein structure; SANS
Volume:40
Issue:6
Pagenumber:14
First Page:761
Last Page:774
Funder:German Ministry of Defense [E/UR3G/6G115/6A801, E/E590/9Z004/5F159, E/E590/8Z002/4F170]; European Union
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer Review:Referiert