Strategies for the Immobilization of Eversa® Transform 2.0 Lipase and Application for Phospholipid Synthesis

Abstract

Eversa® Transform 2.0 lipase (ET2) is a recent lipase formulation derived from the Thermomyces lanuginosus lipase cultivated on Aspergillus oryzae and specially designed for biodiesel production. Since it has not been available for a long time, research on the efficiency of this enzyme in other applications remains unexplored. Moreover, even though it has been launched as a free enzyme, its immobilization may extend the scope of ET2 applications. This work explored ET2 immobilization on octadecyl methacrylate beads (IB-ADS-3) and proved the efficiency of the derivatives for esterification of glycerophosphocholine (GPC) with oleic acid in anhydrous systems. ET2 immobilized via interfacial activation on commercial hydrophobic support Immobead IB-ADS-3 showed maximum enzyme loading of 160 mg/g (enzyme/support) and great stability for GPC esterification under 30% butanone and solvent-free systems. For reusability, yields above 63% were achieved after six reaction cycles for GPC esterification. Considering the very high enzyme loading and the number of reuses achieved, these results suggest a potential application of this immobilized biocatalyst for esterification reactions in anhydrous media. This study is expected to encourage the exploration of other approaches for this enzyme, thereby opening up several new possibilities.

Lipase‐catalyzed preparation of deacidified Buah Merah (Pandanus conoideus) oil

“…It has been reported that ET 2.0 has the greatest catalytic activity at temperatures of 25 • C−40 • C. However, several reports employing immobilized ET 2.0 as the biocatalyst for different types of reactions have found that the immobilized lipase display higher optimal temperatures (45 • C−65 • C) than their free counterparts (Facin et al, 2021;Lee et al, 2019;Oh et al, 2022). These results suggest that the immobilization of ET 2.0 on support materials might enhance the thermostability of the lipase.…”