Colorimetric determination of hydrogen peroxide based on the robust peroxidase-like activities of flower-like YVO4 microstructures
2021
Hou, Peng | Ju, Peng | Hao, Lei | Chen, Congcong | Jiang, Fenghua | Ding, Haibing | Sun, Chengjun
In this study, yttrium vanadate (YVO₄) flower-like microstructures assembled by quadrangular prisms (YVFPs) were prepared through a facile hydrothermal method, which were developed as a novel nanoenzyme to determine hydrogen peroxide (H₂O₂) for the first time. In the presence of H₂O₂, YVFPs exhibited a highly efficient peroxidase-like activity in catalyzing the oxidation the typical peroxidase substrate 3,3′,5,5′-tetramethylbenzidine (TMB). Colorless TMB would be turned into oxidized TMB with a visible blue color and UV–visible absorption peak at 652 nm. The catalytic reaction mechanism was proposed according to the kinetics experiments and active species capture tests, indicating that·O₂⁻ radicals played a key role in the peroxidase mimetic reaction. Besides, YVFPs showed a superior affinity to TMB compared with the natural enzyme horse radish peroxidase with a lower Kₘ value. Taking advantage of the strong peroxidase-like activity of YVFPs, a simple, rapid, sensitive, and visual platform was successfully established for colorimetric detection of H₂O₂. The YVFPs-based colorimetric system possessed good selectivity, stability and reusability with a wider linear range from 0.5 μM to 50 μM and a lower detection limit as low as 0.126 μM towards H₂O₂ determination. Moreover, the feasibility of this convenient method was further validated by assaying residual H₂O₂ in milk and contact lens solutions. This work not only provides a novel artificial biomimetic catalyst with efficient catalytic abilities, but also opens up a new potential application field of YVO₄ materials in clinical diagnosis, food safety and biomedicine.
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