z-logo
Premium
Experimental optimization of enzymic kinetic resolution of racemic flurbiprofen
Author(s) -
Zhang Hua Yun,
Wang Xin,
Ching Chi Bun,
Wu Jin Chuan
Publication year - 2005
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20040163
Subject(s) - flurbiprofen , chemistry , kinetic resolution , enantiomer , hydrolysis , methanol , alcohol , candida antarctica , enantioselective synthesis , solvent , cyclohexane , lipase , resolution (logic) , organic chemistry , chromatography , triacylglycerol lipase , catalysis , enzyme , artificial intelligence , computer science , pharmacology , medicine
Immobilized lipase from Candida antarctica (Novozym® 435) was employed for the kinetic resolution of racemic flurbiprofen by the method of enantioselective esterification with alcohols. However, the presence of accumulated water from the esterification influenced the enantiomeric ratio and reaction rate, due to increased rate of hydrolysis of the esterified enantiomer. In the present study, the procedure for optimizing the experimental resolution of the racemate was tested, with a focus on solvent and alcohol types, inhibition of alcohol substrates and the nature of the reversible reaction. The optimal concentration of feed flurbiprofen (180 mM or 44 mg/ml) was determined on basis of the maximum water content favourable for esterification, in single resolution, with the use of methanol in the solvent of cyclohexane.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here