A novel peroxidase/oxidase mimetic Fe-porphyrin covalent organic framework enhanced the luminol chemiluminescence reaction and its application in glucose sensing.

Abstract

A Fe-porphyrin covalent organic framework (Fe-PorCOF) was prepared through a postmodification strategy and characterized using different techniques. Fe-PorCOF exhibits an inherent peroxidase/oxidase mimetic catalytic activity and sharply accelerates chemiluminescence (CL) reactions between luminol and hydrogen peroxide (H2 O2 ) or dissolved oxygen (O2 ) under alkaline conditions. The catalytic role was attributed to a significant increase in production of reactive oxygen species. Using the imminent peroxidase mimetic catalytic activity of Fe-PorCOF, a new CL method was developed for determination of H2 O2 over a linear range from 0.01 to 10.0 μmol·L-1 and with a limit of detection of 5.3 nmol·L-1 . The combination of the peroxidase mimetic catalytic activity of Fe-PorCOF with the catalytic activity of glucose oxidase on glucose oxidation presents a sensitive CL method for glucose assay. The linear range and the detection limit for glucose were 0.05-8.0 μmol·L-1 and 4.0 nmol·L-1 , respectively. The practicability of this method was assessed by determination of glucose in human sera. As a peroxidase/oxidase mimetic, Fe-PorCOF is easy to prepare and exhibits good catalytic efficiency in the luminol reaction. We believe that this strategy will promote the development of a CL field with functional COFs as a catalyst.