| Natural enzymes attract much attention due to its high catalysis efficiency and strong specificity, but as a biology activator which is subjected to inactivated due to environmental factors. Therefore mimic enzymes have attracted a great deal of researcher interest. Because of their topological structures, large specific surface areas, easy for design,cut and function, MOFs have broad application prospects in light-emitting, separation, gas storage, catalysis, sensors, biological chemistry, and other fields. Design unique structural form and artificial enzyme for catalytic oxidation has been the focus of scholars.This paper makes use of various research methods. Finally with a self-designed Fe-MIL-101materials, studied its peroxidatic activity. our study shows that Fe-MIL-101, possesses an intrinsic enzyme mimicking activity similar to that found in natural horseradish peroxidase. Besides, the effect of concentration,pH and temperature on Fe-MIL-101were also studied. The effect of each parameter on existence of the periodic solution is discussed by analyzing the dynamical properties of the solutions of the equation. The results show that, the optimum reaction temperature and pH were45℃and4.0. The Michaelis constant of Fe-MIL-101reaction at present condition was0.315mM. The Michaelis constant (Km) of Fe-MIL-101with H2O2as the substrate is about616-fold smaller than free HRP,indicating a much higher affinity for H2O2than HRP. Fe-MIL-101also exhibited significantly higher affinity than homogeneous artificial complexes. The Michaelis constant (Km) of Fe-MIL-101with ABTS as the substrate is0.916Mm and3.7mM for H2O2, indicating a bit better affinity for H2O2than HRP.The results show that the catalytic activity of the Fe-MIL-101is higher than that of the natural horseradish peroxidase.The consequences provide potential application for biological and medical areas in the near future. |
