Haloalkane dehalogenases (HLDs) are enzymes that use a hydrolytic mechanism to catalyze the cleavage of the carbon halogen bond resulting in the formation of an alcohol, proton, and a free halide. The haloalkane dehalogenase family has a broad range of substrate specificities. Due to halogenated compounds being toxic byproducts of many industrial processes, HLDs have significant potential in biosensing and bioremediation processes. A recently characterized HLD from <i>Caulobacter crescentus </i>(DccA) was found to be highly active towards longer (greater than three carbons) brominated and chlorinated haloalkanes. Many of the most important toxic halogenated compounds are smaller, chlorinated compounds such as 1,2,3-trichloropropane, 1,2-dichloroethane and 1-chlorobutane. Here we will present the results of our ongoing directed evolution efforts to improve DccA’s activity towards chlorinated haloalkanes and the identification of activity on smaller haloalkanes.

Directed evolution of the haloalkane dehalogenase from <i>Caulobacter crescentus</i>

251st National Meeting (2016)

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Directed evolution of the haloalkane dehalogenase from Caulobacter crescentus