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R‐stereopreference analysis of lipase Novozym®435 in kinetic resolution of flurbiprofen
Author(s) -
Zhang Hua Yun,
Wang Xin,
Ching Chi Bun
Publication year - 2006
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20347
Subject(s) - chemistry , flurbiprofen , kinetic resolution , enantiomer , lipase , candida antarctica , enantioselective synthesis , methanol , chirality (physics) , kinetic energy , resolution (logic) , stereochemistry , homochirality , reaction mechanism , enzyme , organic chemistry , catalysis , medicine , nambu–jona lasinio model , chiral symmetry breaking , physics , quantum mechanics , artificial intelligence , quark , computer science , pharmacology
Immobilized lipase from Candida antarctica (Novozym®435) was employed in the kinetic resolution of racemic flurbiprofen by enantioselective esterification with methanol. It was found that the lipase has the R‐stereopreference and the reaction matches Bi Bi Ping Pong mechanism with dead‐end inhibition of methanol. Furthermore, the R‐stereopreference was analyzed in details from the aspects of enzymatic kinetic mechanism and reaction activation energy of both enantiomers. The R‐enantiomer shows lower activation energy and higher maximum reaction rate than the S‐enantiomer, which implies the R‐stereopreference of the lipase and makes the kinetic resolution of flurbiprofen via enzymatic reaction feasible. Chirality 2006. © 2006 Wiley‐Liss, Inc.