Compartmentalization of Biocatalysts by Immobilizing Bienzyme in Hollow ZIF-8 for Colorimetric Detection of Glucose and Phenol

Based on glucose oxidase (GOx) and horse-radish peroxidase (HRP), compartmentalization of a bienzyme system was successfully carried out by immobilizing them in hollow metal-organic frameworks via a protein-induced soft-templating pathway. The morphology, structure, and properties of the obtained HRP@H-ZIF-8-GOx (GOx and HRP were immobilized in the shell and cavity of hollow ZIF-8, respectively) were investigated by powder X-ray diffraction, scanning transmission electron microscopy (STEM), and so forth. HRP@H-ZIF-8-GOx showed excellent catalytic activity for the cascade reaction with glucose and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt as the substrates. The temperature adaptability, thermal stability, mechanical stability, and long-term storage stability of HRP@H-ZIF-8-GOx are better than that of HRPGOx@H-ZIF-8 (GOx and HRP were coimmobilized in the cavity of hollow ZIF-8). HRP@H-ZIF-8-GOx was used for the detection of glucose and phenol, which showed excellent detection performance. This proposed platform provides a facile strategy for constructing a compartmental multienzyme system and expands the application potential of multienzyme in biosensor construction, biocatalysis, and environmental field.