Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule

Interest in the synthesis and application of thymol esters has increased in recent years due to the numerous applications associated with its biological activities. The enzymatic synthesis of thymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipases and immobilized lipase biocatalysts in solvent-free systems. Candida antarctica lipase B in its soluble form was the most active biocatalyst for this reaction. Different thymol and lipase feeding strategies were evaluated to maximize thymol octanoate production. The results suggest that there could be lipase inhibition by the ester product of the reaction. In this way, the optimal reaction condition was given using a thymol/acid molar ratio of 1:4 mol/mol. Under these conditions the conversion of thymol was close to 94% and the lipase maintained more than 90% of its initial activity after the reaction, showing the potential of the enzyme to be used in successive reaction cycles.

Automated summary

Interest in the synthesis and application of thymol esters has increased recently due to its various biological activities. This study explored the enzymatic synthesis of thymol octanoate using soluble lipases and immobilized lipase biocatalysts. Candida antarctica lipase B in its soluble form was found to be the most active biocatalyst. Different feeding strategies were evaluated, and the optimal reaction condition was determined to be a thymol/acid molar ratio of 1:4 mol/mol. This study demonstrated the potential of using the enzyme in successive reaction cycles.