Enhancement lipase activity using ionic liquids: experimental assays and molecular docking analysis

One of the challenges in biocatalysis is the search for efficient ionic liquids (ILs) as reaction media promoting interfacial activation of the enzyme. The IL-enzyme interaction is the most important factor which affect the enzymatic activity due to the IL direct binding on enzyme structure. Therefore, molecular docking was used for analyse Candida rugosa lipase (CRL) molecular interactions with IL-cations ([P666(14)]+ and [C4min]+) as an additional tool for supporting the experimental assays of hydrolytic activity. According to results obtained all ILs increase in CRL activity, between 95% and 340%, in presence of [P666(14)]+ and [C4min]+ anions, respectively. Molecular docking results reveals that only [C4min]+ interact through hydrophobic interactions with one residue Histidine (His449) on CRL catalytic triad (major drive force in higher enzymatic activity of CRL observed in the presence of this IL). This study offers new insights into ILs and CRL mechanism of interaction, which could be useful for the development of novel biocatalytic processes in presence ILs.