Engineering aldolases as biocatalysts

•Aldolase enzymes are attractive candidates as biocatalysts.•Stability, stereoselectivity and substrate specificity of aldolases have been altered.•Aldolases with desirable activities have been produced using a variety of methods.•Combining computational with other methods produces efficient designer aldolases. Aldolases are seen as an attractive route to the production of biologically important compounds due to their ability to form carbon–carbon bonds. However, for many industrial reactions there are no naturally occurring enzymes, and so many different engineering approaches have been used to address this problem. Engineering methods have been used to alter the stability, substrate specificity and stereospecificity of aldolases to produce excellent enzymes for biocatalytic processes. Recently greater understanding of the aldolase mechanism has allowed many successes with both rational engineering approaches and computational design of aldolases. Rational engineering approaches have produced desired enzymes quickly and efficiently while combination of computational design with laboratory methods has created enzymes with activity approaching that of natural enzymes.