Esterases as stereoselective biocatalysts

Non-lypolitic esterases are carboxylester hydrolases with preference for the hydrolysis of water-soluble esters bearing short-chain acyl residues. The potential of esterases as enantioselective biocatalysts has enlarged in the last few years due to the progresses achieved in different areas, such as screening methodologies, overproduction of recombinant esterases, structural information useful for understanding the rational behind enantioselectivity, and efficient methods in protein engineering. Contributions of these complementary know-hows to the development of new robust enantioselective esterases are critically discussed in this review.