Enhancing enzymatic performance with nanoparticle immobilization: improved analytical and control capability for synthetic biochemistry

[Display omitted] Enzymes are incredibly potent catalysts with the potential for rapid turnover rates and exquisite specificity, leading to their desired use in multiple biotechnological processes. Yet using these natural catalysts outside of their evolved role can necessitate significant engineering. Immobilization onto microscale (or larger) scaffolds can impart industrially-desired properties but often sacrifices enzymatic activity for long-term stability; in contrast, nanoparticle (NP) conjugation of enzymes can preserve or even enhance their activity. Here, we focus on recent examples of enzyme immobilization onto NPs as a method to improve their industrial applicability. We highlight the analytical methods that are used to both characterize such enhancement along with provide insight into the phenomena that give rise to it. Finally, a short perspective addresses how to adapt lessons learned at the bench about this phenomena to larger-scale biotechnological applications.