Immobilization of Organophosphorus Acid Anhydrolase Mutant Y212F on Silica Nanospheres
Abstract
We have engineered mutants of the wild type organophosphorus acid anhydrolase (OPAA) for activity on G-type chemical nerve agents and observed increased activity on the most-toxic enantiomers. Enzyme stability might be enhanced by attachment of the OPAA to a silicon dioxide nanoparticle. Conjugation of our enzyme mutant was performed by personnel at nanoComposix (San Diego, CA), which is a producer of customized nanoparticles. After conjugation, the activity of the enzymeparticle combination on pinacolyl methyl phosphonofluoridate (GD, soman) was measured and compared with free enzyme. Activity measurements were made to compare a free and immobilized OPAA mutant on the G-agent stimulant diisopropyl fluorophosphates (DFP) and soman.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 01, 2016
- Accession Number
- AD1018277
Entities
People
- Mark A. Guelta
- Melissa M. Dixon
- Richard Baldwin
- Steven P. Harvey
Organizations
- Edgewood Chemical Biological Center