Enzyme-Encapsulated Zeolitic Imidazolate Frameworks Formed Inside the Single Glass Nanopore: Catalytic Performance and Sensing Application.

Metal-organic frameworks (MOFs) can improve the stability and activity of enzymes under the MOF encapsulation. However, it remains a challenge to explore the effects of the MOF environment on enzymatic activity in a confined space. In this work, we immobilized the enzyme inside a glass nanopore to study the catalytic activity and stability of the enzyme in the MOF environment. Horseradish peroxidase (HRP) is encapsulated in zeolitic imidazolate framework-90 (ZIF-90) and zeolitic imidazolate framework-8 (ZIF-8), which are used as the catalytic platforms. The HRP can catalyze 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)diammonium salt (ABTS) molecules to generate ABTS ions, and the change of the transmembrane ion current will be monitored in real time. As the concentration of HO increases, the amount of produced ABTS will increase; thus, the ionic current increases. The effects of the MOF structure on enzyme activity and stability are also investigated. The HRP encapsulated in the MOF and modified inside the nanopore provides a novel and unlabeled design for studying enzymatic catalysis in a confined environment, which should have extensive applications in chemical-/bio-sensing, electrocatalysis, and fundamental electrochemistry.