ABSTRACT
In this study, the protein stability of hen egg-white lysozymes (HEWL) by Fe3O4 and Fe3O4-coated trehalose (Fe3O4@Tre) magnetic nanoparticles (NPs) is investigated. For this purpose, the co-precipitation method was used to synthesize magnetic NPs. The synthesized NPs were characterized by XRD, FT-IR spectroscopy, FE-SEM, and VSM analysis. In addition, the stability of HEWLs exposed to different NP concentrations in the range of 0.001-0.1 mg mL-1 was investigated by circular dichroism (CD) spectroscopy, fluorescence, and UV-Vis analysis. Based on the results, in the NP concentration range of 0.001-0.04 mg mL-1 the protein structure is more stable, and this range was identified as the range of kosmotropic concentration. The helicity was measured at two concentration points of 0.02 and 0.1 mg mL-1. According to the results, the α-helix at 0.02 mg mL-1 of Fe3O4 and Fe3O4@Tre was increased from 35.5% for native protein to 37.7% and 38.7%, respectively. The helicity decreased to 36.1% and 37.4%, respectively, with increasing the concentration of Fe3O4 and Fe3O4@Tre to 0.1 mg mL-1. The formation of hydrated water shells around protein molecules occurred by using Fe3O4@Tre NPs. Hence, it can be concluded that the trehalose as a functional group along with magnetic NPs can improve the stability of proteins in biological environments.
