Abstract

Enzymes are very versatile catalysts in organic chemistry, although in many occasions they present very low selectivity towards non-natural or artificial compounds. A simple strategy has recently been discovered which allows a greater enhancement of the enzyme selectivity. This strategy -based on the conformational changes of these enzymes during catalysis- consists in the preparation of a biocatalysts library using different immobilization protocols that may permit to immobilize the enzymes via different orientations, with different rigidity or generating different environments. This review examines the way in which different enzymes such as lipases, acylases, β-galactosidases, epoxyhydrolases, phosphorylases, hydroxynitrile lyases, sulfatases, glycosyltranferases, or tyrosynases have shown a huge variation with this solid phase strategy. This methodology has permitted to obtain highly enantioselective biocatalysts in asymmetric reactions, synthesis of β-lactams antibiotics or transglycosylation reactions.

Keywords: Conformational changes, enzymes, immobilization, kinetic resolution, enantioselectivity, regioselectivity