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