Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols

• Published in: Comptes Rendus Chimie
• Main Authors: Merabet-Khelassi, Mounia, Bouzemi, Nassima, Fiaud, Jean-Claude, Riant, Olivier, Aribi-Zouioueche, Louisa
• Other Authors: UCL - SST/IMCN/MOST - Molecules, Solids and Reactivity
• Format: Article in Journal/Newspaper
• Language: English
• Published: Elsevier 2011
• Subjects: Arylalkylcarbinols; Enzymatic kinetic resolution; Isopropenyl acetate; Lipases; Selectivity; Succinic anhydride; Vinyl acetate; Antarc*; Antarctica
• Online Access: http://hdl.handle.net/2078.1/108408; https://doi.org/10.1016/j.crci.2011.07.005

This study shows the influence of the amount of Candida Antarctica-B lipase on reactivity and selectivity in lipase-catalyzed acylation of arylalkylcarbinols 1-8. For 1-indanol 1 and with isopropenyl acetate, the selectivity E increases from 60 to > 500 when the amount of the lipase decreases from 150 to 3 mg. For the 1,2,3,4-tetrahydronaphthalen-1-ol 4, in the presence of succinic anhydride, the decrease of the amount of Candida Antarctica-B from 150 to 20 mg brings an improvement of the selectivity from E = 50 to E = 140. For the acylation of α-hydroxyferrocene 8 with vinyl acetate, high selectivities are reached with the lipases of Candida Antarctica-B, C = 50% E > 500 and Pseudomonas cepacia, C = 42% E = 425. The reduction of the amount of CAL-B, in toluene, results in an increase of the selectivity of acylation of ferrocenylethanol 8, from E = 20 to E > 500. This effect is not displayed in di-isopropylether. © 2011 Académie des sciences. Published by Elsevier Masson SAS. All rights reserved.