Kinetic and thermodynamic study of enzymatic hydroesterification mechanism to fatty acid methyl esters synthesis

Abstract

Eversa® Transform 2.0 lipase used as biocatalyst to biodiesel (fatty acid methyl esters – FAME) synthesis has been the target of interesting studies due to its thermostability and cost-effectiveness. In these researches, data about reaction conditions that result in satisfactory yields were investigated. Nevertheless, kinetic and thermodynamic parameters considering this enzyme are scarce. This paper presents an estimation of kinetic and thermodynamic parameters for the Eversa® Transform 2.0-mediated hydroesterification to FAME synthesis. Kinetic studies were performed for different methanol, water and lipase loads in distinct temperatures. Parameters adjusted by the thermodynamic model indicate that the hydrolysis is decisive in the overall hydroesterification reaction rate and the esterification reaction is endothermic (ΔHe = 38.98 kJ/mol). Formation of enzymatic complexes is favored by increasing the temperature, especially the enzyme-methanol inhibition complex. Statistical analysis showed that the model was not overparameterized, and the small confidence interval indicated good reliability of the estimated parameters.