Candida antarctica Lipase B: A Tool for the Preparation of Optically Active Alcohols

Abstract

Lipases (E.C. 3.1.1.3) have proved to be efficient catalysts for the preparation of enantiomerically enriched compounds. Among them, Candida antarctica lipase B (CALB) has been found to be a particularly useful biocatalyst for the asymmetric transformation of sec-alcohols and related compounds. Indeed, about 200 compounds have already been successfully resolved using this enzyme. This number includes some chiral acids, but other lipases have proved to be superior to CALB for the resolution of most chiral acids. This chapter will, therefore, focus on the resolution of chiral alcohols. CALB is supplied as a recombinant protein patented by Novo-Nordisk. Despite its origin in the Antarctics, CALB is stable at 60-80°C for extended periods of time, once it is immobilized (1). Furthermore, CALB retains most of its activity and robustness in nonaqueous media. An example is that Glaxo selected CALB out of two lipases suitable for a multikilo resolution, because of its stability over multiple-use cycles in nonaqueous media (2).