Microbiological transformations. Part 48: Enantioselective biohydrolysis of 2-, 3- and 4-pyridyloxirane at high substrate concentration using the Agrobacterium radiobacter AD1 epoxide hydrolase and its Tyr215Phe mutant

The epoxide hydrolase (EH) from Agrobacterium radiobacter AD1 wild type (ArWT) and its Tyr215Phe mutant were compared for the biocatalyzed hydrolytic kinetic resolution (BHKR) of 2-, 3- and 4-pyridyloxirane. The regioselectivity of the oxirane ring opening as well as the substrate concentration limit and the inhibitory effect of the diol were determined. A gram scale preparation of enantiopure 2-pyridyloxirane (ee>98%) at a concentration as high as 127 mM (15.5 g/L) could be achieved with each of these two enzymes.