ArticleEuropean biophysics journal : EBJ2011
The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 19 citations in OpenAlex.
- Role of Php domain and related enzymes in the enzymatic degradation of G-series nerve agents.Molecular genetics and genomics : MGG · 2025Review
- Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions.Frontiers in chemistry · 2020Article
- Bicontinuous Interfacially Jammed Emulsion Gels (bijels) as Media for Enabling Enzymatic Reactive Separation of a Highly Water Insoluble Substrate.Scientific reports · 2019Article
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11 authors at 8 institutions in 3 countries.
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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.
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