Fabrication and interaction mechanism of ovalbumin‐based nanocarriers for metallic ion encapsulation

Abstract

Ovalbumin (OVA), due to its desirable physiochemistry properties and biocompatibility, has been widely adopted as bioactive compound carriers in the field of pharmacy and food. This study explored the interaction patterns between OVA and three flavonoids, namely naringin, hesperidin and anthocyanin, and the possibilities of OVA-flavonoid complexes as nanocarriers that entrap mineral substances. Results showed that ovalbumin interacts with three flavonoids through hydrophobic interaction and hydrogen bonding. The addition of flavonoids altered the secondary structure of OVA, decreasing the b-sheets by 9-16% and increasing the random coils by about 20-60% for the hydroxyl groups of flavonoids coalesced with the C = O groups of amides of proteins by hydrogen bonding and hydrophobic interaction occurred from conjugation effects between aromatic rings of flavonoids and amino residues of OVA. The OVA-hesperidin complex showed comprehensive advantages over encapsulating mineral substances such as Mn, Fe, Cu and Zn.

Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin

“…Ovalbumin is the most abundant egg white protein (EWP), accounting for more than 50% of the total proteins [ 18 ]. Several studies have demonstrated the use of ovalbumin as nanogels and nanocarriers when combined with surfactants, metal ions, and chitosan [ 19 , 20 , 21 ]. Notably, the ovalbumin epitope, SIINFEKL, which has been extensively used for immune stimulation, was reported to self-assemble to form a stable hydrogel [ 22 ].…”