Abstract

Nearly monodispersed Ag3PO4 nanocrystals with size of 10 nm were prepared through a colloidal chemical route. It was proven that the synthesized Ag3PO4 nanoparticles have intrinsic peroxidase-like catalytic activity. They can quickly catalyze oxidation of the peroxidase substrate 3, 3, 5, 5-tetramethylbenzidine (TMB) in the presence of H2O2, producing a blue color. The catalysis reaction follows Michaelis-Menten kinetics. The calculated kinetic parameters indicate a high catalytic activity and the strong affinity of Ag3PO4 nanocrystals to the substrate (TMB). These results suggest the potential applications of Ag3PO4 nanocrystals in fields such as biotechnology, environmental chemistry, and medicine.

Highlights

  • Owing to its excellent photocatalytic properties and broad range of applications such as in water-splitting, photocatalytic reactions, silver phosphate has got extensive study and has become a well studied material [1]

  • Extensive studies have been made for the photocatalytic applications of various Ag3PO4 micro-/nanoparticles and their composites, the application of Ag3PO4 in biological systems, for example used as biocatalyst, has rarely been studied, while the presence of phosphorus in biological systems is well known

  • Several kinds of micro/nanoparticles with smaller size or special structure were prepared for developing enzyme mimics, including the ferromagnetic nanoparticles with peroxidase-like activity [14,15,16,17,18,19,20,21,22,23], ceria oxide nanoparticles [24,25,26,27], and V2O5 nanowires [28], carbon-based nanomaterials [29,30,31,32,33,34,35,36] and so on [37,38,39,40,41,42]

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Summary

Introduction

Owing to its excellent photocatalytic properties and broad range of applications such as in water-splitting, photocatalytic reactions, silver phosphate has got extensive study and has become a well studied material [1]. The reaction catalyzed by these Ag3PO4 nanoparticles followed a Michaelis-Menten kinetic behavior with an excellent catalytic activity, making it a promising mimic of peroxidase.

Results
Conclusion
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