Use of lipases in the resolution of racemic ibuprofen.
Resolution of (R,S)-ibuprofen enantiomers by esterification in different organic solvents was studied using Candida cylindracea lipase. This enzyme preparation had high enantiospecificity for S(+)-ibuprofen in the esterification reaction of a racemic ibuprofen with primary alcohols. The esterification yields of secondary alcohols were much lower than those of primary alcohols. Esterification with tertiary alcohols was not observed. The synthesis of esters was profoundly affected by the amount of water in the reaction mixture. C. cylindracea lipase was active only in very hydrophobic solvents. The esterification activity of the lipase was reduced significantly by addition of water. The R- and S-enantiomers of ibuprofen were determined without derivatization by HPLC using a chiral column.
Mustranta
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VTT, Biotechnical Laboratory, Espoo, Finland.
D000438:Alcohols / Q000737:chemistry; D001426:Bacterial Proteins / Q000378:metabolism*; D004951:Esterification; D005656:Fungal Proteins / Q000378:metabolism*; D007052:Ibuprofen / Q000737:chemistry / Q000302:isolation & purification*; D008049:Lipase / Q000378:metabolism*; D009994:Osmolar Concentration; D012997:Solvents; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature; D014867:Water
D000438:Alcohols; D001426:Bacterial Proteins; D005656:Fungal Proteins; D012997:Solvents; D014867:Water; D008049:Lipase; D007052:Ibuprofen