Immobilization of Organophosphorus Acid Anhydrolase Mutant Y212F on Silica Nanospheres
Technical Report,01 Aug 2014,31 Dec 2014
Edgewood Chemical Biological Center Aberdeen Proving Ground United States
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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.