Immobilization of surfactant-lipase complexes and their high heat resistance in organic media

Surfactant-lipase complexes were immobilized in an n-vinyl-2-pyrrolidone gel matrix. Features of a native lipase and gel-immobilized surfactant-lipase complexes were measured by esterification reaction between lauric acid and benzyl alcohol in isooctane. Optimal gel-immobilized surfactant-lipase complex activity was 37.2 mol h−1 kg−1-lipase. Gel-immobilized lipase complexes showed a 51-fold increase in activity and exhibited superior heat resistance compared to native lipases. The optimum temperature for the immobilized lipase complex was 60 °C, as compared to 37 °C for native lipase activity. Gel-immobilized lipase complexes could be readily recovered, and their high activity was completely preserved, even after 10 reuses.