Research Information System
ChemistrySelect, vol.10, no.34, 2025 (SCI-Expanded)
In this study, a biomimetic horseradish peroxidase (HRP@ZIFM) containing nanohemoglobin with natural enzyme-like activity in the presence of zeolitic imidazolate framework functional monomer (ZIFM), has been synthesized. In the first step, ZIFM has been synthesized using Zn2+, 2-methylimidazole, and methacryloylhistidine. Then, the enzymatic activity of HRP@ZIFM has beeninvestigated by adding appropriate amino acid functional monomers to mimic the natural HRP active site. Horseradish peroxidase (HRP) is a heme enzyme whose active site contains heme and different amino acids. HRP oxidizes both organic and inorganic species using H2O2. The optimal pH for the enzyme peroxidase is usually between 6 and 6.5. When peroxidase is exposed to a substrate with different pH levels, the pH of the peroxidase becomes more basic. A decrease in the reaction rate is then noticed as the pH of the enzyme becomes more basic, making peroxidase more unstable. Therefore, with the synthesized ZIFM complex structure, especially using a novel approach to create multiple active centers that mimic nano-hemoglobin-based micromaterials integrated into stable peroxidase-like ZIF-nanozymes, it not only offers superior pH stability and reusability but also shows significantly higher activity, particularly with TMB substrate, compared to other synthetic or biomimetic HRPs in the literature. This provides a notable advantage for industrial and biotechnological applications.