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A novel peroxidase/oxidase mimetic Fe‐porphyrin covalent organic framework enhanced the luminol chemiluminescence reaction and its application in glucose sensing
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 a...
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Published in: | Luminescence (Chichester, England) England), 2020-12, Vol.35 (8), p.1366-1372 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 (H2O2) 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 H2O2 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. |
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ISSN: | 1522-7235 1522-7243 |
DOI: | 10.1002/bio.3899 |