Lipase-catalyzed kinetic resolution on solid-phase via a "capture and release" strategy.
The lipase-catalyzed kinetic resolution of (R/S)-3-phenylbutyric acid 2 using solid-supported cyclohexane-1,3-dione (CHD) 6 is described. In each case the predominant enantiomer observed, after cleavage from the resin, was (R)-(-)-3-phenylbutyric acid (R)-2 (ee > 99%) rather than the expected (S)-enantiomer of 2. This observation is in contrast to the fact that Chromobacterium viscosum lipase shows high enantiospecificity for the (S)-enantiomer in the corresponding solution-phase hydrolysis reactions. The (R)-acyl group was subsequently released from the resin by NaOH hydrolysis, and the yield of the reaction could be improved by triple acylation of the resin.
Humphrey
Cara E
CE
School of Chemistry, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh, Scotland, UK.
Turner
Nicholas J
NJ
Easson
Morag A M
MA
Flitsch
Sabine L
SL
Ulijn
Rein V
RV
D000215:Acylation; D002264:Carboxylic Acids / Q000737:chemistry / Q000302:isolation & purification*; D002384:Catalysis; D004952:Esters / Q000737:chemistry / Q000302:isolation & purification*; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D013237:Stereoisomerism; D013379:Substrate Specificity
D002264:Carboxylic Acids; D004952:Esters; C109511:bis(polyoxyethylene bis(amine)); D011092:Polyethylene Glycols; D008049:Lipase; C454481:lipase, Chromobacterium viscosum