Abstract: The invention comprises isolated, mutant, non-wild-type organophosphorus acid anhydrolase (OPAA) enzymes having two site mutations, methods of production, and methods of use to effectively degrade cylcosarin (GF) (cyclohexyl methylphosphonofluoridate) with greater catalytic efficiency than the wild-type OPAA.

Abstract: The invention is directed toward mutant, non-wild-type organophosphorus acid anhydrolases (OPPAs) having three or more site mutations, methods of production, kits and methods of use to effectively degrade toxic V-agent type chemical compounds such as VX, VR, CVX, and VM.

Abstract: The invention is directed toward mutant, non-wild-type organophosphorus acid anhydrolase enzymes having three site mutations, methods of production, and methods of use to effectively degrade toxic organophosphorus compounds, most preferably GP (2, 2?-dimethylcyclopentyl methylphosphonofluoridate).

Abstract: The invention is directed toward mutant, non-wild-type organophosphorus acid anhydrolase enzymes having three site mutations, methods of production, and methods of use to effectively degrade toxic organophosphorus compounds, most preferably GP (2,2?-dimethylcyclopentyl methylphosphonofluoridate).

Abstract: Genetically engineered organophosphorus acid anhydrolases (OPAA) with improved catalytic efficiency and relaxed stereospecificity are provided. The variants typically include a mutation at the residue corresponding to H343 of wildtype Alteromonas sp. OPAA. The mutation allows the OPAA enzyme to effectively process both VR enantiomers. The OPAA optionally include one or more mutations selected the residues corresponding to Y212, V342, and I215 of wildtype Alteromonas sp. OPAA which improve the enzyme's catalytic efficiency for VX and VR. A particularly preferred OPAA includes mutations at the residues corresponding Y212F, V342L, I215Y, and H343D relative to wildtype Alteromonas sp. OPAA. Compositions including an effective amount of OPAA to increase hydrolysis of an organophosphate, and methods of use thereof for treating subjects exposed to an organophosphate, or a surface or liquid contaminated with an organophosphate are also provided.

Abstract: Disclosed herein are non-wild-type organophosphorus acid anhydrolases having two site mutations, methods of production, and methods of use to effectively degrade toxic chemicals such as ((RS)-Propan-2-yl methylphosphonofluoridate) (Sarin) and other organophosphorus compounds.

Abstract: Disclosed herein are non-wild-type organophosphorus acid anhydrolases having three site mutations, methods of production, and methods of use to effectively degrade toxic chemicals such as((RS)-Propan-2-yl methylphosphonofluoridate)(Sarin) and other organophosphorus compounds.

Abstract: The invention comprises isolated, mutant, non-wild-type organophosphorus acid anhydrolase (OPAA) enzymes having three site mutations, methods of production, and methods of use to effectively degrade organophosphorus compound EA1356 (2-methylcyclohexyl methylphosphonofluoridate) with greater catalytic efficiency than the wild-type OPAA enzyme.

Abstract: This invention is directed toward a non-wild-type organophosphorus acid anhydrolase enzyme having two site mutations, method of production, and method of use to more effectively degrade toxic organophosphorus compounds and, in particular, toxic chemical GD (3,3-Dimethylbutan-2-ylmethylphosphonofluoridate), than the wild type organophosphorus acid anhydrolase.

Abstract: The invention is directed toward non-wild-type organophosphorus acid anhydrolases having three site mutations, method of production, and method of use to effectively degrade toxic chemical compounds such as (Ethyl({2-[bis(propan-2-yl)amino]ethyl}sulfanyl)(methyl)phosphinate (“VX”).

Abstract: The invention is directed toward non-wild-type organophosphorus acid anhydrolases having three site mutations, method of production, and method of use to effectively degrade toxic chemicals such as N,N-diethyl-2-(methyl-(2-methylpropoxy)phosphoryl)sulfanylethanamine) (“VR”).

Abstract: Genetically engineered organophosphorus acid anhydrolases (OPAA) with improved catalytic efficiency and relaxed stereospecificity are provided. The variants typically include a mutation at the residue corresponding to H343 of wildtype Alteromonas sp. OPAA. The mutation allows the OPAA enzyme to effectively process both VR enantiomers. The OPAA optionally include one or more mutations selected the residues corresponding to Y212, V342, and I215 of wildtype Alteromonas sp. OPAA which improve the enzyme's catalytic efficiency for VX and VR. A particularly preferred OPAA includes mutations at the residues corresponding Y212F, V342L, I215Y, and H343D relative to wildtype Alteromonas sp. OPAA. Compositions including an effective amount of OPAA to increase hydrolysis of an organophosphate, and methods of use thereof for treating subjects exposed to an organophosphate, or a surface or liquid contaminated with an organophosphate are also provided.

Abstract: Provided are non-wild-type organophosphorus acid anhydrolases that are capable of degrading (ethyl {2-[bis(propan-2-yl)amino]ethyl}sulfanyl) (methyl)phosphinate and other V-agents. Particular embodiments include an organophosphorus acid anhydrolase including an amino acid substitution at position 212.

Abstract: The present invention is generally related to systems and methods to permit the growth of anaerobic, ethanol-producing bacteria using pretreated biomass such as cellulose in a manner to facilitate the efficient conversion of cellulose to ethanol.

Abstract: An assay for screening potential hydrolysis enhancing agents capable of facilitating the hydrolysis of a substantially water insoluble halogenated compound such as mustard gas (HD) in an aqueous reaction mixture is disclosed. The assay includes at least one chamber adapted for receiving and retaining the substantially water insoluble mustard gas compound and a potential hydrolysis agent in an aqueous reaction mixture, and a pH indicating agent adapted to produce a visible color change corresponding to the amount of the substantially water insoluble mustard gas compound hydrolyzed in the aqueous reaction mixture wherein the rate of hydrolysis can be established by measuring the change in the detectable signal over time.

Abstract: The present invention relates to a near-universal non-corrosive, non-toxic, environmentally safe and user friendly decontaminant capable of detoxifying organophosphorus (OP)-based G-type, V-type neurotoxic chemical warfare, sulfur-mustard, and related OP based hazardous industrial materials in a dry powder form. The decontaminant contains OPH enzyme, OPAA enzyme, DFPase enzyme, dehalogenase enzyme, quaternary ammonium salt, a pH control reagent, a fire-fighting agent, and a foaming agent. The decontaminant is mixed with available water for use.

Abstract: The present invention relates to a near-universal non-corrosive, non-toxic, environmentally safe and user friendly decontaminant capable of detoxifying organophosphorus (OP)-based G-type, V-type neurotoxic chemical warfare, sulfur-mustard, and related OP based hazardous industrial materials in a dry powder form. The decontaminant contains OPH enzyme, OPAA enzyme, DFPase enzyme, dehalogenase enzyme, quaternary ammonium salt, a pH control reagent, a fire-fighting agent, and a foaming agent. The decontaminant is mixed with available water for use.

Abstract: A process for the detoxification or demilitarization of the chemical warf agent HT, a mixture of 2,2'-dichlorodiethyl sulfide and bis-(2-(2-chloroethylthio)ethyl) ether, is disclosed. The process includes 1) treating HT with a hydrolyzing agent to form a mixture of thiodiglycol (TDG) and bis-(2-(2-hydroxyethylthio)ethyl) ether(s?) (T-OH); 2) neutralizing the TDG and T-OH mixture to a pH sufficient for biodegradation of the mixture; and biodegrading the neutralized TDG and T-OH mixture. In preferred embodiments, the hydrolyzing agent is water and the neutralizing is carried out with NAOH. Biodegradation is preferably carried out with a sequential batch reactor.