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Traditional methods of determining metals require sophisticated instruments and skilled human labor, which are difficult to operate under field conditions. Metal ions and enzymes can be produced through a variety of chemical reactions, leading to the changes in enzyme activity. Therefore, the change of enzyme activity simulated by nanozymes can be used for specific quantification of analytes. Recently, nanozymes have been successfully used to detect types of metal ions.
Creative Enzymes develops an advanced platform to provide simple, fast and accurate detection of metal ions based on decades of experience with nanozymes. Our experts will answer your questions comprehensively and carefully and help you solve the problems in your studies. We guarantee satisfied and reliable results for our customers all over the world.
We provide noble metal nanozymes and other feasible nanozymes. They have been widely used in the detection of mercury ions due to their unique optical properties and excellent catalytic activity of oxidation mimicking enzymes.
Fig. 1 Hg2+ inhibits the peroxidase-like activity of Au nanozymes in the presence of Bi3+.
| Target Ion | Nanozyme | Enzyme-mimic | Substrate | Mechanism |
|---|---|---|---|---|
| Hg2+ | Pt | Peroxidase | TMB | Amalgamation via metallophilic interaction |
| Hg2+ | Core-shell Au@Pt | Peroxidase | TMB | Metallophilic interaction changes surface properties |
| Hg2+ | Au / BiOI | Oxidase | AR | Metallophilic Au-Hg and Hg-I interaction |
| Hg+ and organic mercury | T60–CuxO / Pt | Oxidase | ABTS | Pt-Hg metallophilic interaction, inhibition |
|
Hg2+ and methyl mercury |
Pt / Au | Peroxidase / Catalase | AR | Hg-Au interaction, switching of enzyme-mimic activity |
| Hg2+ | Au | Peroxidase | AR, Bi3+ | Hg–Au amalgamation in presence of Bi3+ |
| Hg2+ | CoS / rGO | Peroxidase | TMB | Hg–S complex formation blocks active sites |
| Hg2+ | CuS HNSs | Peroxidase | TMB | Hg–S bond formation, Hg2+ displaces Cu from surface |
| Hg2+ | CS-MoSe2 | Peroxidase | TMB | Reduction of Hg2+ to Hg0 on the nanozyme's surface triggers peroxidase-like activity |
We provide a variety of enzymes to detect Ag+, so that our clients can use them quickly and easily in a variety of work environments.
| Target Ion | Nanozyme | Enzyme-mimic | Substrate | Mechanism |
|---|---|---|---|---|
| Ag+ | Chitosan-Pt | Oxidase | TMB | Metallophilic interaction & blocking active sites |
| Ag+ | Citrate-modified Pt | Peroxidase | TMB | Citrate assisted reduction of Ag+ to Ag0 on the Pt |
| Ag+ | β-casein-Au | Peroxidase | TMB | Protein-induced reduction of Ag+ to Ag0 on Au NPs' surface |
| Ag+ | Histidine-Pd | Peroxidase | TMB | Ag+ despoils histidine from nanozyme's surface |
| Ag+ | ZIF-8 / GO hybrid | Peroxidase | TMB | Reduction of Ag+ to Ag0 on the surface of ZIF-8 / GO hybrid by the citric acid-sodium citrate system triggers peroxidase-like activity |
| Target Ion | Nanozyme | Enzyme-mimic | Substrate | Mechanism |
|---|---|---|---|---|
| Cu2+ | Histidine-Au | Peroxidase | TMB | i) Turn-off by Cu2+, ii) followed by turn-on by free histidine |
| Cu2+ | Ag / Pt | Peroxidase | TMB | MPA ligand inhibits activity, Cu2+ oxidized MPA, recover catalytic activity |
| Cu2+ | Urchin-like Co9S8 / Cysteine | Peroxidase | TMB | Cysteine suppresses activity of Co9S8, Cu2+ binds with cysteine and turn-on activity |
| Target Ion | Nanozyme | Enzyme-mimic | Substrate | Mechanism |
|---|---|---|---|---|
| Cr6+ | PEI-Ag | Oxidoreductase | TMB | PEI-Ag NC catalyzes the reaction between Cr6+ and TMB |
| Cr6+ | CuS / frGO | Peroxidase | hydroxy terephthalic acid | Cr6+ ions stimulate the peroxidase-mimic activity of CuS / frGO |
| Cr6+ | Au−Ag / L-Cys-rGO | Peroxidase | TMB | Cr6+ ions promotes the decomposition of H2O2 to O2 and H2O |
| Cr6+ | CeO2NRs-MOF | Oxidase | TMB | Cr6+ enhances the oxidase-like activity by facilitating fast electron transfer |
Creative Enzymes offers metal ion detection services based on nanozymes with customized delivery strategies and precise design. Our advanced technical platforms help our clients solve the problems they may encounter in research based on decades of experience. If you are interested in our services or have some questions, please feel free to contact us or make an online inquiry.
