Palomo_2012_Methods.Mol.Biol_861_329

One important parameter for the application of lipase catalysts in chemical industries is the specific activity displayed towards natural or unnatural substrates. Different strategies to enhance the lipase activity have been described. The immobilization of lipases on hydrophobic supports by interfacial adsorption at low ionic strength permitted the hyperactivation of these enzymes by fixing the open conformation of the lipase on the hydrophobic support. Improvements of activity from 1.2- up to 20-fold with respect to the initial one have been observed for lipases from different sources.A second strategy was based on the presence of additives, in particular surfactants, with hydrophobic character to enhance the activity of lipases immobilized on macroporous supports up to 8 fold and even more than 100-fold in some cases for soluble lipases.Finally, a third strategy to improve the activity in lipases was based on a site-directed chemical modification of the protein on a unique reactive cysteine of the enzyme by disulfide exchange using different tailor-made activated polymers.