Lipase mediated chiral resolution of 4-arylthio-2-butanol as an intermediate for beta-lactam antibiotics.
This paper deals with chiral enzymatic resolution of 4-arylthio-2-butanols by lipase to prepare potential intermediates of beta-lactam antibiotics. Among several lipases employed, lipase P type enzyme gave the highest ee value to prepare (R)-4-arylthio-2-butyl acetate. The enzymatic resolution of phenyl substituted alcohol (6a) using lipase P showed the highest ee value (99.7%) among those of 4-arylthio-2-butanol derivatives. Lipase P mediated hydrolysis of acylester 7a gave also (R)-alcohol 6a selectively. For determination of enantiomeric purity of these enzymatic resolved analytes, liquid chromatographic analysis was performed using two coupled Chiralcel OD and (R,R)-WhelkO chiral column.
Hwang
Kwang-Jin
KJ
Department of Chemical System Engineering, Hongik University, Jochiwon, Chungnam 339-701, Korea. kjhwang@wow.hongik.ac.kr
Lee
Jinkue
J
Chin
Sungmin
S
Moon
Chi Jang
CJ
Lee
Wonjae
W
Baek
Chae-Sun
CS
Kim
Hyung Jin
HJ
D000440:Butanols / Q000032:analysis / Q000138:chemical synthesis*; D008049:Lipase / Q000032:analysis / Q000138:chemical synthesis*; D013237:Stereoisomerism; D047090:beta-Lactams / Q000032:analysis / Q000138:chemical synthesis*
D000440:Butanols; D047090:beta-Lactams; C043958:2-butanol; D008049:Lipase