More Oomph for OPH

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Science  30 Mar 2012:
Vol. 335, Issue 6076, pp. 1547
DOI: 10.1126/science.335.6076.1547-b

Enzymes are remarkably adept at accelerating complex chemical reactions, but they tend to work best in the milieu where they evolved. It is therefore often challenging to apply them at high temperature or in the midst of interfering factors. El-Boubbou et al. sought to optimize the use of organophosphorus hydrolase (OPH) in the service of degrading the highly toxic organophosphorus compounds present in certain pesticides and nerve agents. They found that immobilization of the enzyme in mesoporous silica prefunctionalized with ammonium ions conferred substantial thermal stability without compromising the flexibility necessary for catalytic activity. Phosphorus-31 nuclear magnetic resonance spectroscopy was applied to monitor rates for hydrolysis of the model compound paraoxon, and revealed enhanced specific activity of the immobilized enzyme relative to the native enzyme in solution. The silica-bound enzyme remained active after being heated (either dry or in suspension) to temperatures as high as 65°C for extended periods—as long as a month at 45°C.

Adv. Healthcare Mater. 1, 183 (2012).

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