Magnetic Catalyst Gelatin-Hematain/Fe3O4 As An Advanced Substitute For Horseradish Peroxidase (HRP) Enzyme In The Polymerization Of Phenol Compounds For Biomedical Application

Abstract

Horseradish peroxidase (HRP) is widely used as a catalyst in biomedical applications, but its natural enzyme properties present challenges. To address these challenges, researchers have studied an artificial alternative: magnetic nanoparticles coated with gelatin-hematin (MNPs-Ge-He), which mimic HRP function with improved characteristics. Hematin is a traditional substitute for HRP due to its similar heme group, but its poor solubility in neutral media hinders its use in medical applications. To overcome this, hematin was bound with gelatin as a conjugate. The HRP-mimicking catalyst (MNPs-Ge-He) was synthesized by coating magnetic iron oxide nanoparticles (MNPs) with (3-trimethoxysilyl) propyl-ethylenediamine (TSPED) and functionalizing them with gelatin-hematin (Ge-He). Fourier transform infrared spectroscopy (FTIR) confirmed that the MNPs-Ge-He synthesis was effective, and X-ray diffraction (XRD) assessment showed that TSPED, gelatin, and hematin did not affect the crystal structure of the MNPs. Synthetic catalyst magnetisms demonstrated a magnetic function in catalyst recovery in VSM patterns. DLS and TEM analyses confirmed the successful fabrication of MNPs-Ge-He. The enzymatic oxidation of the catalyst was determined using rutin and ABTS assays. MNPs-Ge-He was applied in resveratrol polymerization as a mimicking HRP catalyst. The polymerization process was carried out for different lengths of time (one, two, three, and six hours), and the most effective reaction time was determined using DPPH antioxidant assay. Overall, the study showed that MNPs-Ge-He is an effective alternative to HRP with improved properties, paving the way for its use in various biomedical applications.