Internal cavity amplification of shell-like ferritin regulated with the change of the secondary and tertiary structure induced by PEF technology.

This study investigates how pulsed electric field (PEF) treatment affects the morphology and molecular structure of ferritin, a protein obtained from horse spleen. The research indicates that PEF alters ferritin’s structure, which may have applications in using ferritin as a carrier for bioactive molecules in food.

Research Methodology

• The researchers used a variety of scientific methods, such as circular dichroic (CD), fluorescence spectroscopy, Raman spectroscopy, cold-field emission scanning electron microscopy (CF-SEM) and transmission electron microscopy (TEM) to study how PEF treatment alters the apparent morphology and molecular structure of shell-like ferritin from horse spleen.
• The changes in ferritin were also evaluated using molecule dynamics (MD) simulation for verification.

Effects of PEF Treatment on Ferritin

• Treatment of ferritin with PEF resulted in partial unfolding of its structure, as evidenced by a decrease in the α-helix content of the protein indicating a change in its secondary and tertiary structure.
• The minimum α-helix content was observed at 10 kV/cm field strength.
• Interestingly, after a rest period of two hours at room temperature, the α-helix content increased again, suggesting that the PEF-treated ferritin tends to revert to its original structure owing to its reversible assembly characteristics.
• Microstructure analysis revealed aggregation of ferritin particles post PEF treatment, marking a change in the physical properties of the protein.

Implications of PEF Effects on Ferritin

• The changes triggered by PEF, especially the exposure of hydrophobic amino acids and the conversion of disulfide bond configuration, could be taken advantage of to manipulate the stability of ferritin’s internal cavity.
• This knowledge could be applied in using PEF treatments to modify protein structures for various applications.
• The study provides a better understanding of the effect of PEF on ferritin and lays a theoretical basis for using ferritin as a carrier of bioactive molecules in food production, potentially leading to the development of new techniques and products in the food industry.