Biosynthesis of benzyl cinnamate using an efficient immobilized lipase entrapped in nano-molecular cages

To improve the performance of lipase in biosynthesis of benzyl cinnamate, a new immobilized lipase by entrapping enzyme into nano-molecular cages was designed. Consequently, the entrapped lipase showed a robust immobilization, which diminished the leakage of lipase notably in use. Moreover, the entrapped lipase exhibited higher activity (57.1 U/mg) than free lipase (50.0 U/mg), demonstrating that the native conformation of lipase was not destroyed during immobilization. Compared with the adsorbed lipase (half-life 40.7 min) and free lipase (half-life 29.8 min), the entrapped lipase (half-life 85.3 min) increased the stability by about 2-3 times. Furthermore, the entrapped lipase was applied in biosynthesis of benzyl cinnamate, where it showed excellent activity and re-usability. After 7 cycles, the yield of benzyl cinnamate catalyzed by the entrapped lipase remained 70.2%, while the yield catalyzed by the adsorbed lipase was only about 10%. These results indicated that the nano-molecular cages could inhibit denaturation of lipase and maintain its activity well.

Automated summary

The design of a new immobilized lipase entrapped in nano-molecular cages improved its performance in biosynthesis, demonstrating higher activity and stability compared to free and adsorbed lipase. The entrapped lipase exhibited excellent activity and reusability in the biosynthesis of benzyl cinnamate, indicating the nano-molecular cages could inhibit denaturation and maintain lipase activity.