The recombinant halohydrin dehalogenase from Agrobacterium radiobacter ADI was used to obtain enantiomerically pure halohydrins and epoxides by kinetic resolution. By adding an excess of the recombinant epoxide hydrolase from the same organism the reversible conversion was drawn to completion. Halohydrins such as (S)-2,3-dichloro-1-propanol (E>100) and (S)-2-chloro-1-phenylethanol (E=73) were obtained with an enantiomeric excess of higher than 99%. This is a novel biocatalytic route for obtaining enantiomerically pure aromatic halohydrins and epoxides. (C) 1999 Elsevier Science Ltd, All rights reserved.</p