Aplicação da lipase Eversa® Transform 2.0 na síntese de biolubrificantes por meio de simulações computacionais

Abstract

Biolubricants have been gaining more market share given the increased interest in replacing the use of petroleum-based lubricants. They are produced using renewable raw materials such as vegetable oils, and lipases can be used as catalysts for their syntheses, making these processes more environmentally friendly. Among the innovations created with enzymatic engineering tools, lipase Eversa® Transform 2.0 appears as an enzymatic formulation, genetically modified, of lower cost, and has high activity for the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, computational tools, such as docking and molecular dynamics, can be allied in the development of competitive products with low environmental impact. These simulation tools make it possible to understand the reaction mechanism of a process, save on the expense of reagents, and support the choice of materials and conditions that can be used in real processes. Thus, this work proposed the modeling and analysis of synthesis reactions of biolubricants derived from oleic acid, using different types of alcohols and the lipase Eversa® Transform 2.0 as a catalyst for the reactions. From the molecular dockings, it was observed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the lipase and its surroundings were Van der Waals or hydrophobic. In the molecular dynamics simulations, it was found that these interactions provided the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed in the simulation times. Furthermore, the low variation in the position of the lipase/ligand complexes concerning their initial conformations in the production steps, attested that the chosen docking poses were adequate to describe the conformations of the ligands in the region of the active site of the lipase. These results provide a structural view of the interactions between lipase Eversa® and fatty esters used as lubricants and indicate which would possibly be the best alcohols used for the process, but they cannot reliably attest to the behavior of the proposed systems under experimental conditions, since many other variables, such as enzymatic activity, inhibition mechanisms of the catalyst, alteration of the reaction equilibrium, among others, can significantly alter the dynamics of the process.