Effect of lipid peroxidation on the allergenicity and functional properties of soybean β-conglycinin (7S) and glycinin (11S)

Protein oxidation‐induced changes in the physicochemical properties and quality of plant food

“…Emulsification is an important functional property of protein, which refers to the ability of oil and water to form emulsion, including emulsification and emulsification stability. Studies have shown that the emulsification of soybean protein treated by AAPH and acrolein was higher than that of unoxidised protein, which may be due to the hydrophobic domains of 7S and 11S were exposed and changed by lipid oxidation, thus improving the emulsifying activity of protein (Han et al ., 2023; Ye et al ., 2023). In contrast, the emulsifying activity index (EAI) of oxidised rice protein increased gradually and then decreased steadily, when concentration of 13‐hydroperoxyoctadecadienoic acid was 0.1 mmol/L (Wu et al ., 2020b).…”

“…The structures of 7S and 11S were fully expanded and became loose after oxidation, and the foaming ability (FC) and foam stability (FS) of 7S and 11S after oxidation were also significantly improved, indicating that oxidation can accelerate protein diffusion at the water–vapour interface (Ye et al ., 2023). Also, with the increase of oxidation degree, the FC and FS of walnut protein increased first and then decreased, which may be due to the interaction between hydrophobic residues caused by the expansion of peptide chain, resulting in lower surface tension and faster protein diffusion to the air–water interface, thereby promoting the formation of bubbles.…”

“…Especially in emulsions, protein is easily prone to oxidation due to the presence of pro‐oxidant in the oil, water or interfacial phase (Meissner et al ., 2020). Lipid oxidation has the capability to change the conformational structure of β‐conglycinin (7S) and glycinin (11S) by exposing hydrophobic domains, thereby improving the emulsifying activity of SPI (Ye et al ., 2023).…”