Efficient biosynthesis of enantiopure tolvaptan by utilizing alcohol dehydrogenase-catalyzed enantioselective reduction†
Abstract
Using whole cells of Escherichia coli co-expressing alcohol dehydrogenase (PsADH) and formate dehydrogenase (CpFDH) in a biphasic aqueous–soybean oil system is shown to be an efficient method for the biosynthesis of enantiopure tolvaptan. In this system, (S)-tolvaptan with an optical purity of 99.5% and a bioconversion efficiency of 86.1% was achieved.