Advancements in lipase immobilization: Enhancing enzyme efficiency with nanomaterials for industrial applications

One of the most widely utilized enzymes, lipase is crucial to many biotechnological and industrial processes, including those in the biodiesel, food, paper, and oleochemical sectors, as well as in applications related to medicine. However, its use is highly costly and challenging due to its instability and aqueous solubility. Immobilization is a commonly employed way to enhance lipase activity, and it has proven to be a successful approach. In comparison to free lipase, immobilized lipase on nanomaterials (NMs) as demonstrated superior properties, including greater pH and temperature stability, a longer stable duration, and the ability to be recycled. However, under specific circumstances, protein loading is comparatively decreased and lipase immobilization on NMs might also occasionally result in activity loss. The processes of immobilization, the kind of NM's being employed, and the physicochemical characteristics of the NMs (such as particle size, aggregation behaviour, NM dimension, and kind of coupling/modifying agents being used) all affect the overall performance of immobilized lipase on NM's. In recent years, innovative nanostructured forms such nanoflowers, carbon nanotubes, nanofibers, and metal-organic frameworks (MOFs) have been researched for numerous applications along with classic nanomaterials like nano silicon, magnetic nanoparticles, and nanometal particles. To use immobilized lipase on/in nanomaterials for large-scale industrial applications, a few issues still need to be resolved. This study addresses the current advancements and the impact of NMs on lipase immobilization and activity based on the unique characteristics of lipase and NM's.