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.
Highlights
Eversa® Transform 2.0 (ET2) has been mostly used in its free form as recommended by the supplier, proper immobilization may enhance a great deal of properties such as stability, activity, selectivity, or specificity, resistance to inhibitors or chemicals, and applications as biocatalyst in other reactions [8,9]
The addition of larger quantities of enzyme does not increase enzyme activity and, activity per mg of enzyme is reduced [21]. As mentioned above, those aggregates have a direct influence on obtaining derivatives with high enzyme loading, as the aggregate dismembers on a gradual basis, the immobilization speed decreases and progresses very slowly [22,23]
The strategy of hydrophobic interaction by interfacial activation was used for ET2 immobilization in Immobead IB-ADS-3
Summary
Lipases (triacylglycerol hydrolases, EC 3.1.1.3) are a class of enzymes able to perform a broad range of bioconversions owing to their substrate specificity, selectivity, high stability, and in many instances, high regio- and enantioselectivity [1,2,3]. This versatility, combined with the world’s search for alternatives to supply the growing energy demand, has inspired the use of lipases as biocatalysts to produce biodiesel from a variety of fats and oils [4,5,6]. Phospholipid synthesis via enzymatic process usually occurs under milder conditions and, because biocatalysts present high stereoselectivity, it results in products that cannot be obtained through chemical methods [10]
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