Investigates antioxidant activity enhancement in peptide-hemin conjugates through ultrasonic treatment, suggesting improved food resource utilization.
Porcine blood meal-derived hydrolysate peptides and hemin are natural antioxidants, and the formation of peptide–hemin conjugates can synergistically improve antioxidant performance. Ultrasonic (US) treatment facilitates the binding of different molecules. Therefore, in this study, the effects of ultrasonic power treatments on the antioxidant activity and binding behavior of peptide–hemin conjugates were investigated. The spatial structure of the peptide–hemin conjugates was characterized using endogenous fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, and circular dichroism (CD) spectroscopy, respectively. The results demonstrated that the peptide–hemin binding rate reached the highest value of 91.63% at 400 W US power, with structural changes in conjugates from α-helix to random coil structures. Additionally, US treatment increased the surface hydrophobicity and reduced the enthalpy change in conjugates. The antioxidant capacity was greatly improved and peaked at 400 W US, where DPPH and ABTS radical scavenging rates exceeded 55% and 65%, respectively. This study provided a scientific basis for the high-value utilization of US treatment on porcine blood meal resources.
No takes yet. Share an insight, caveat, or question.
Du et al. (2026) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: