Detoxification of Sarin, an Acetylcholinesterase Inhibitor, by Recombinant Organophosphorus Acid Anhydrolase

  • Kim, Seok-Chan (Department of Material Science, Korea Institute of Military Science & Technology) ;
  • Lee, Nam-Taek (Department of Chemistry, Korea Military Academy)
  • Received : 2001.05.24
  • Accepted : 2001.07.07
  • Published : 2001.09.30

Abstract

Pesticide waste and chemical stockpiles are posing a potential threat to both Vie environment and human health. There is currently a great effort toward developing effective and economical methods for the detoxification of these toxic organophosphates. In terms of safety and economy, enzymatic biodegradation has been recommended as the most promising tool to detoxify these toxic materials. To develop an enzymatic degradation method to detoxify such toxic organophosphorus compounds, a gene encoding organophosphorus acid anhydrolase (OPAA) from genomic DNA of Alteromonas haloplanktis C was subcloned and expressed. The enzyme consists of a single polypeptide chain with a molecular weight of 48 kDa. It demonstrates strong hydrolyzing activity on sarin, an acetylcholinesterase inhibitor. Moreover, its high activity is sustained for a considerable length of time. It is projected that the recombinant OPAA can be applied as an enzymatic tool that can be used not only for the detoxification of pesticide wastes, but also for the demilitarization of chemical stockpiles.

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