Pseudomonas cepacia Lipase Immobilized onto Chitosan-Coated Activated Carbon: An Efficient Catalyst for Transesterification Enantiomer Resolution of (R, S)-1-Phenyl-3-buten-1-ol

Pseudomonas cepacia lipase (PSL) immobilized onto chitosan-coated activated carbon (CS-AC) with specific surface area of 798 (m(2)/g), average pore diameter of 2.13 nm and pore volume of 0.43 cm(3)/g was synthesized by a simple adsorption method. The immobilized lipase PSL/CS-AC catalyst exhibited enhanced catalytic activity for resolving racemic 1-phenyl-3-buten-1-ol compared to free PSL and PSL immobilized on sole activated carbon or chitosan. The enantiomeric excess value (ees) of (S)-1-phenyl-3-buten-1-ol and the enantiomeric excess value (eep) of (R)-1-phenyl-3-buten-1-ol acetate reached 99 and 94 %, respectively with the reaction substrate conversion of 51 %. PSL/CS-AC immobilized lipase exposed the more surface active sites resulting in the higher catalytic performances. The preparation of the support for immobilizing lipase is low cost and the reaction conditions are moderate and environmentally friendly. The immobilized lipase PSL/CS-AC catalyst possessed of high thermal stability, reusability and storage stability, it could be a potential chiral catalyst for enantiomer resolution reactions.