Abstract Burkholderia cepacia LTBE11 lipase was used in the kinetic resolution of four secondary allylic alcohols by transesterification reactions with vinyl acetate: rac-1 [1-phenylprop-2-en-1-ol], rac-2 [1-(4-chlorophenyl)prop-2-en-1-ol], rac-3 [1-(3-methoxyphenyl)prop-2-en-1-ol] and rac-4 [5-methylhex-1-en-3-ol]. Greater enantioselectivities, expressed as the enantiomeric ratio (ERS or ESR, as appropriate), were obtained with the addition of the lipase immobilized on a polypropylene support (Accurel) than with the addition of a powdered free enzyme preparation. The fast-reacting enantiomer was the R-enantiomer for the alcohols with aromatic substituents (rac-1, rac-2 and rac-3) and the S-enantiomer for the alcohol with an aliphatic substituent (rac-4). The ERS values obtained for rac-1, rac-2 and rac-3 were greater than the ESR value obtained for rac-4. With the increasing temperature, ERS decreased for rac-2 and rac-3, while ESR increased for rac-4. Thermodynamic analysis of the difference in activation energies based on the temperature data showed that ΔR−SΔH# and ΔR−SΔS# were negative in all cases. For rac-2 and rac-3, the selectivity for the R-enantiomer was due to a predominance of enthalpic effects (i.e. ∣ΔR−SΔH#∣>∣TΔR−SΔS#∣). For rac-4, the selectivity for the S-enantiomer was due to a predominance of entropic effects (i.e. ∣TΔR−SΔS#∣>∣ΔR−SΔH#∣). The resolution of rac-2 was investigated in different solvents. ERS enhanced with the increasing values of log P and molecular volume of the solvent but decreased with the increasing dielectric constant. The highest ERS value, 110, was obtained in n-heptane. This elevated enantioselectivity suggests that the lipase of B. cepacia LTBE11 has good potential for the application in the resolution of secondary allylic alcohols.