Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols
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 fro...
Published in: | Comptes Rendus Chimie |
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Main Authors: | , , , , |
Other Authors: | |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Elsevier
2011
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Subjects: | |
Online Access: | http://hdl.handle.net/2078.1/108408 https://doi.org/10.1016/j.crci.2011.07.005 |
Summary: | 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. |
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