Effect of nanomaterials on activity of immobilized lipases

In last few decades lipases have gained lots of interest in biotechnological and industrial processes due to its capability to catalyze a wide range of reactions [1]. But its aqueous solubility and instability, have been limited the practical applications‎ of lipases. ‎To take advantage of this potential enzyme, it is suggested to immobilized it on nanomaterials (NMs) through varieties of methodologies such as adsorption, entrapment, covalent coupling or cross-linking [2]. The immobilized lipase has shown superiority to the free lipase in term of reusability, pH and thermal stability, and the capacity of being stored. However, high production cost, non-uniformity and aggregation potential of NMs as well as lack of knowledge on mechanisms of immobilization severely limit the applicability of them [3]. Therefore, reviewing the influence of characteristic features of NMs on their performance including type, size, surface charge and type of modifying agents constitutes a topic of great importance. Considering the unique functions of lipases and NMs as novel and promising supports, this review discusses on conformational changes, kinetic behavior, feasible mechanisms and challenges for commercialization of nanobiocatalysts.