Abstract
Herein, the nanozymatic behavior of protein-protected gold and SiO2@gold nanoparticles were evaluated and their results compared with each other. The results showed that both protein-protected gold and SiO2@gold nanoparticles reveal intrinsic peroxidase-like activity. Hence, to precise comparison of nanozymatic behavior of these nanozymes, the kinetic studies were performed using the Michaelis–Menten steady-state kinetics model and the velocity and affinity factors were calculated for both nanozyme and then utilized as a reliable way for comparison of nanozymatic behavior of these nanozymes. The results showed that the Vmax of protein-protected gold nanoparticles was 12.0-fold higher than that of SiO2@gold nanoparticles, revealing that the catalytic efficiency of protein-protected gold nanoparticles is 12.0-fold higher than SiO2@AuNPs nanocomposite. Besides, the Km value of SiO2@gold nanoparticles was 2-order higher than that of protein-protected gold nanoparticles, indicating that the substrate affinity toward protein-protected gold nanoparticles is 2.0-order higher than the SiO2@gold nanoparticles. Based on the results of this work it can be concluded that protein-protected gold nanoparticles are more efficient nanozymes than SiO2@gold nanoparticles.