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  • Stabilization of organophosphorus hydrolase by entrapment in silk fibroin: formation of a robust enzymatic material suitable for surface coatings.

Stabilization of organophosphorus hydrolase by entrapment in silk fibroin: formation of a robust enzymatic material suitable for surface coatings.

Biomacromolecules (2012-06-02)
Patrick B Dennis, Anne Y Walker, Matthew B Dickerson, David L Kaplan, Rajesh R Naik
ABSTRACT

Organophosphates are some of the most acutely toxic compounds synthesized on an industrial scale, and organophosphorus hydrolase (OPH) has the ability to hydrolyze and inactivate a number of these chemicals. However, OPH activity is vulnerable to harsh environmental conditions that would accompany its practical utility in the field; a limitation that can also be extended to conditions required for incorporation of OPH into useful materials. Here we present evidence that entrapment of OPH in silk fibroin leads to stabilization of OPH activity under a variety of conditions that would otherwise reduce free enzyme activity, such as elevated temperature, UV light exposure and the presence of detergent. Silk fibroin entrapment of OPH also allowed for its dispersal into a polyurethane-based coating that retained organophosphate hydrolysis activity after formulation, application and drying. Together, the data presented here demonstrate the utility of silk fibroin entrapment for the protection of OPH activity under a variety of environmental conditions.

MATERIALS
Product Number
Brand
Product Description

Supelco
Parathion-methyl solution, 100 μg/mL in cyclohexane, PESTANAL®, analytical standard
Supelco
Parathion-methyl, PESTANAL®, analytical standard