J. Iran. Chem. Soc., Vol. 7, No. 4 December 2010, pp.883~889.

Current location: JICS Archive > Vol. 7 > No. 4 > Articles : 13

Enzymatic Resolution of Racemic Sulcatol by Lipase from Candida Antarctica in a Large Scale  

H.V. Ferreiraa, L.C. Rochaa, R.P. Severinoa,b, R.B. Vianaa, A.B.F. da Silvaa and A.L.M. Portoa,*

aInstituto de QuĂ­mica de SĂ£o Carlos, Universidade de SĂ£o Paulo, Av. Trabalhador SĂ£o-carlense, 400, CEP 13560-970, SĂ£o Carlos, SP, Brazil
bDepartamento de QuĂ­mica, Universidade Federal de Goiás, Campus Avançado de CatalĂ£o, Av. Dr. Lamartine Pinto de Avelar, 1120, 75704-020, CatalĂ£o, GO, Brazil

Large scale enzymatic resolution of racemic sulcatol 2 has been useful for stereoselective biocatalysis. This reaction was fast and selective, using vinyl acetate as donor of acyl group and lipase from Candida antarctica (CALB) as catalyst. The large scale reaction (5.0 g, 39 mmol) afforded high optical purities for S-(+)-sulcatol 2 and R-(+)-sulcatyl acetate 3, i.e., ee > 99 per cent and good yields (45 per cent) within a short time (40 min). Thermodynamic parameters for the chemoesterification of sulcatol 2 by vinyl acetate were evaluated. The enthalpy and Gibbs free energy values of this reaction were negative, indicating that this process is exothermic and spontaneous which is in agreement with the reaction obtained enzymatically.

Keywords: Enzymatic resolution, Lipase, Candida antarctica, Sulcatol, Biocatalysis

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