The enantioselective hydrolysis of racemic epichlorohydrin (ECH) leading to enantiopure (R)-ECH using recombinant epoxide hydrolase (EH) was successfully undertaken in organic solvents. The lyophilized recombinant whole-cell Pichia pastoris expressing the EH gene of Rhodotorula glutinis was used as the biocatalyst; n-dodecane containing 2.5 % (v/v) water was employed as the reaction medium to prevent the spontaneous chemical degradation of racemic ECH. Enantiopure (R)-epichlorohydrin (ECH) with 99 % ee was obtained from 20 mM of the racemate with a yield of 28.5 % in n-dodecane within 60 min.