Abstract
Whole cells of Rhodococcus sp. NCIMB 11216 catalyze the asymmetric hydrolysis of racemic epoxides giving access to chiral epoxides and diols, which are important chiral building blocks for the synthesis of bioactive compounds. Employing a four-step purification procedure, the epoxide hydrolase responsible for the reaction was isolated and characterized to be a cofactor-independent, soluble monomeric protein of ~35kDa, exhibiting an isoelectric point of 4.7.
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