Enzymatic resolution of racemic secondary alcohols by lipase B from Candida antarctica

• Published in: Journal of the American Oil Chemists' Society
• Main Authors: Patel, Ramesh N., Banerjee, Amit, Nanduri, Venkata, Goswami, Animesh, Comezoglu, F. T.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2000
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1007/s11746-000-0161-y; https://onlinelibrary.wiley.com/doi/full/10.1007/s11746-000-0161-y

Abstract Chiral intermediates S ‐(+)‐2‐pentanol and S ‐(+)‐2‐heptanol were prepared by a lipase‐catalyzed enzymatic resolution proces. Among various lipases evaluated for the stereoselective acylation of racemic alcohols, lipase B from Candida antarctica catalyzed the acylation of the undesired enantiomer of racemic alcohols leaving the desired S ‐(+)‐alcohols unreacted. A reaction yield of 43–45% and an enantiomeric excess (e.e.) of >99% were obtained for S ‐(+)‐2‐pentanol or S ‐(+)‐2‐heptanol when the reaction was carried out using vinyl acetate or succnic anhydride as acylating agent. In an alternative process, an enantioselective hydrolysis of 2‐pentyl acetate was demonstrated using lipase B giving S ‐(+)‐2‐pentyl acetate and R ‐(−)‐2‐pentanol. A reaction yield of 45% and an e.e. of 98.6% were obtained for S ‐(+)‐2‐pentyl acetate.