Nanostructured materials for harnessing the power of horseradish peroxidase for tailored environmental applications

High catalytic efficiency, stereoselectivity, and sustainability outcomes of enzymes entice chemists for considering biocatalytic transformations to supplant conventional synthetic routes. As a green and versatile enzyme, horseradish peroxidase (HRP)-based enzymatic catalysis has been widely employed in a range of biological and chemical transformation processes. Nevertheless, like many other enzymes, HRP is likely to denature or destabilize in harsh realistic conditions due to its intrinsic fragile nature, which results in inevitably shortened lifespan and immensely high bioprocess cost. Enzyme immobilization has proven as a prospective strategy for improving their biocatalytic performance in continuous industrial processes. Nanostructured materials with huge accessible surface area, abundant porous structures, exceptional functionalities, and high chemical and mechanical stability have recently garnered intriguing research interests as novel kinds of supporting matrices for HRP immobilization. Many reported immobilized biocatalytic systems have demonstrated high catalytic performances than that to the free form of enzymes, such as enhanced enzyme efficiency, selectivity, stability, and repeatability due to the protective microenvironments provided by nanostructures. This review delineates an updated overview of HRP immobilization using an array of nanostructured materials. Furthermore, the general physicochemical aspects, improved catalytic attributes, and the robust practical implementations of engineered HRP-based catalytic cues are also discussed with suitable examples. To end, concluding remarks, challenges, and worthy suggestions/perspectives for future enzyme immobilization are also given. (C) 2020 Elsevier B.V. All rights reserved.