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A region suffering from an attack of a nerve agent requires not only a highly sorptive material but also a fast-acting catalyst to decontaminate the lethal chemical present. The product should be capable of high sorptive capacity, selectivity and quick response time to neutralize the long lasting harmful effects of nerve agents. Herein, we have utilized organophosphorus hydrolase (OPH) as a non-toxic bio-catalytic material held in with the supporting matrix of poly-β-cyclodextrin (PCD) as a novel sorptive reinforced self-decontaminating material against organophosphate intoxication. OPH coated PCD (OPH-PCD) will not only be providing support for holding enzyme but also would be adsorbing methyl paraoxon (MPO) used as a simulant, in a host-guest inclusion complex formation. Sorption trend for PCD revealed preference towards the more hydrophobic MPO against para-nitrophenol (pNP). The results show sorption capacity of 1.26 mg/g of 100 μM MPO with PCD which was 1.7 times higher compared to pNP. The reaction rate with immobilized OPH-PCD was found to be 23% less compared to free enzyme. With the help of OPH-PCD, continuous hydrolysis (100%) of MPO into pNP was observed for a period of 24 h through packed bed reactor with good reproducibility and stability of enzyme. The long-term stability also confirmed its stable nature for the investigation period of 4 days where it maintained activity. Combined with its fast and reactive nature, the resulting self-decontaminating regenerating material provides a promising strategy for the neutralization of nerve agents and preserving the environment.

V-type nerve agents, known as VX, are organophosphate (OP) compounds, and show extremely toxic effects on human and animals by causing cholinergic overstimulation of synapses. The bacterial organophosphorus hydrolase (OPH) has attracted much attention for detoxifying V-type agents through hydrolysis of the P-S bond. However, low catalytic efficiency of OPH has limited the practical use of the enzyme. Here we present rational design of OPH with high catalytic efficiency for a V-type nerve agent. Based on the model structure of the enzyme and substrate docking simulation, we predicted the key residues that appear to enhance the access of the substrate to the active site of the enzyme, and constructed numerous OPH mutants. Of them, double mutant, L271/Y309A, was shown to exhibit a 150-fold higher catalytic efficiency for VX than the wild-type.