Abstract
l-asparaginase is an essential enzyme in medicine and a well-known chemotherapeutic agent. This enzyme's importance is not limited to its use as an anti-cancer agent; it also has a wide variety of medicinal applications. Antimicrobial properties, prevention of infectious disorders, autoimmune diseases, and canine and feline cancer are among the applications. Apart from the healthcare industry, its importance has been identified in the food industry as a food manufacturing agent to lower acrylamide levels. When isolated from their natural habitats, they are especially susceptible to different denaturing conditions due to their protein composition. The use of an immobilization technique is one of the most common approaches suggested to address these limitations. Immobilization is a technique that involves fixing enzymes to or inside stable supports, resulting in a heterogeneous immobilized enzyme framework. Strong support structures usually stabilize the enzymes' configuration, and their functions are maintained as a result. In recent years, there has been a lot of curiosity and focus on the ability of immobilized enzymes. The nanomaterials with ideal properties can be used to immobilize enzymes to regulate key factors that determine the efficacy of bio-catalysis. With applications in biotechnology, immunosensing, biomedicine, and nanotechnology sectors have opened a realm of opportunities for enzyme immobilization.