Abstract
In the past few decades, the enzyme immobilization technology has been exploited a lot and thus became a matter of rational design. Immobilization is an alternative approach to bio-catalysis with the added benefits, adaptability to automation and high-throughput applications. Immobilization-based approaches represent simple but effective routes for engineering enzyme catalysts with higher activities than wild-type or pristine counterparts. From the chemistry viewpoint, the concept of stabilization via manipulation of functional entities, the enzyme surfaces have been an important driving force for immobilizing purposes. In addition, the unique physiochemical and structural functionalities of pristine or engineered cues, or insoluble support matrices (carrier) such as mean particle diameter, swelling behavior, mechanical strength, and compression behavior are of supreme interest and importance for the performance of the immobilized systems. Immobilization of peroxidases into/onto insoluble support matrices is advantageous for practical applications due to convenience in handling, ease separation of enzymes from a reaction mixture and the reusability. A plethora of literature is available explaining individual immobilization system. However, current literature lacks the chemistry viewpoint of immobilization. This review work presents state-of-the-art "Smart" chemistry of immobilization and novel potentialities of several materials-based cues with different geometries including microspheres, hydrogels and polymeric membranes, nanoparticles, nanofibers, composite and hybrid or blended support materials. The involvement of various functional groups including amino, thiol, carboxylic, hydroxyl, and epoxy groups via "click" chemistry, amine chemistry, thiol chemistry, carboxyl chemistry, and epoxy chemistry over the protein surfaces is discussed.