Home > Publications database > The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity |
Journal Article | PreJuSER-15317 |
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2011
Springer
Berlin
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Please use a persistent id in citations: doi:10.1007/s00249-011-0689-0
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.
Keyword(s): Animals (MeSH) ; Carbohydrates: chemistry (MeSH) ; Carbohydrates: pharmacology (MeSH) ; Emulsions (MeSH) ; Loligo: enzymology (MeSH) ; Loligo: metabolism (MeSH) ; Microscopy, Electron, Scanning (MeSH) ; Neutron Diffraction (MeSH) ; Phosphoric Triester Hydrolases: analysis (MeSH) ; Phosphoric Triester Hydrolases: chemistry (MeSH) ; Phosphoric Triester Hydrolases: metabolism (MeSH) ; Scattering, Small Angle (MeSH) ; Solutions: chemistry (MeSH) ; Surface-Active Agents: chemistry (MeSH) ; Surface-Active Agents: pharmacology (MeSH) ; Health and Life (1st) ; Health and Life (1st) ; Biology (2nd) ; Carbohydrates ; Emulsions ; Solutions ; Surface-Active Agents ; Phosphoric Triester Hydrolases ; diisopropyl-fluorophosphatase ; J ; Dynamic light scattering (auto) ; Neutron spin echo (auto) ; Microemulsion (auto) ; Enzyme catalysis (auto) ; SANS (auto) ; Protein structure (auto)
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