A review on the important aspects of lipase immobilization on nanomaterials

Lipase is one of the most widely used enzymes and plays an important role in biotechnological and industrial processes including food, paper, and oleochemical industries, as well as in pharmaceutical applications. However, its aqueous solubility and instability make its application relatively difficult and expensive. The immobilization technique is often used to improve lipase performance, and the strategy has turned out to be a promising method. Immobilized lipase on nanomaterials (NMs) has shown superiority to the free lipase, such as improved thermal and pH stability, longer stable time, and the capacity of being reused. However, immobilization of lipase on NMs also sometimes causes activity loss and protein loading is relatively lowered under some conditions. The overall performance of immobilized lipase on NMs is influenced by mechanisms of immobilization, type of NMs being used, and physicochemical features of the used NMs (such as particle size, aggregation behavior, NM dimension, and type of coupling/modifying agents being used). Based on the specific features of lipase and NMs, this review discusses the recent developments, some mechanisms, and influence of NMs on lipase immobilization and their activity. Multiple application potential of the immobilized lipases has also been considered.