Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis.
Lipases are important catalysts in chiral synthesis due to their wide substrate recognition combined with a high stereoselectivity. We demonstrate here that the state, free or immobilized, of Candida antarctica lipase B (CaLB) affects enantioselectivity and also alters the temperature dependancy of the enzyme. This indicates that CaLB undergoes various conformations induced by its interaction with the different immobilization supports studied. Molecular imprinting experiments, using immobilized enzyme co-dried with mimic substrate molecules, enhanced the enantiomeric ratio two-fold or three-fold, depending on the immobilization support. The structure of the acyl donor has a pronounced effect on CaLB catalyzed resolution, due to the proximity of the acyl and alcohol moieties during catalysis. When the acylation of pentan-2-ol was examined, we found that the 3C methyl propanoate donor afforded the highest resolution. Trans-(Z)-cyclooct-5-en-1,2-diol was used as a model racemic substrate to study the ability of lipase to catalyze the resolution of difunctionalized compounds. There was a clear enhancement in the enantiomer selectivity of the biotransformation of the diol when vinyl butanoate is used as the acyl donor. The conversion and enantiomeric excess of (1R,2R)-monoacetates were enhanced, using immobilized CaLB, when the chain length of the donors increased from C2 to C4.
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: mgraber@univ-lr.fr.
Marianne
M
Graber
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: hrouilla@univ-lr.fr.
Hervé
H
Rouillard
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: regis.delatouche@univ-lr.fr.
Régis
R
Delatouche
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: najla.fniter@gmail.com.
Najla
N
Fniter
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: belsem.belkhiria@gmail.com.
Belsem
B
Belkhiria
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: antoine.bonnet@univ-lr.fr.
Antoine
A
Bonnet
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: ldomon@univ-lr.fr.
Lisianne
L
Domon
Université de La Rochelle, UMR CNRS 7266 LIENSs, Avenue M. Crépeau, 17042 La Rochelle, France. Electronic address: vthiery@univ-lr.fr.
Valérie
V
Thiéry
D019149:Bioreactors; D034242:Cyclooctanes / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism*; D009584:Nitrogen; D000439:Pentanols / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013696:Temperature
D034242:Cyclooctanes; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D000439:Pentanols; D008049:Lipase; C431349:lipase B, Candida antarctica; D009584:Nitrogen
Biocatalysis; Bioreactors; Immobilized enzymes; Kinetic resolution; Lipase; Substrate engineering