Yuryev, RuslanRuslanYuryevIvanova, MartaMartaIvanovaDaskalova, ValentinaValentinaDaskalovaMüller, RudolfRudolfMüller2022-05-042022-05-042011-11-15Biocatalysis and Biotransformation 29 (6): 320-327 (2011)http://hdl.handle.net/11420/12460By screening around 30 commercially available lipases and esterases, two enzymes, C. rugosa lipase and P. fluorescens esterase, were found to posess catalytic activity and enantioselectivity (E∼10) for the hydrolysis of 2-chloro-3,3,3-trifluoropropanoic acid (CTFPA) methyl and ethyl ester. Both enzymes were tentatively assigned to be (S)-selective based on the assumption that they have the same stereopreference as in the hydrolysis of methyl 2-chloropropanoate, which is a non-fluorinated analogue of CTFPA. The enzymes were applied in the kinetic resolution of CTFPA ethyl ester and 95% ee of the remaining ester could be achieved at 60% conversion. The crosslinked enzyme aggregate (CLEA) of C. rugosa lipase was found to catalyze enantioselective transesterification (E∼0) of CTFPA methyl ester with ethanol. By conducting the transesterification in a 10-mL packed-bed reactor containing CLEA, it was possible to convert racemic CTFPA methyl ester into the mixture of (S)-methyl and (R)-ethyl esters with 82% and 90% ee, respectively, at 4.0 g/L -1/h-1 space-time yield, which decreased to 1.0 g/L -1/h-1 after four repetitive batches. © 2011 Informa UK, Ltd.en1029-244620116320327Taylor & FrancisC. rugosa lipaseCLEAflourinated compoundskinetic resolutionP. fluorescens esterasetransestereficationBiowissenschaften, BiologieTechnikIngenieurwissenschaftenJournal Article10.3109/10242422.2011.634906Other