The goal of this study was to investigate the effects of protein oxidation on myofibrillar protein (MP) gel structure and rheological properties using a lipoxygenase-linoleic acid system. The results showed that the addition of the linoleic acid significantly increased the protein carbonyl and dityrosine content (P < 0.05), whereas the contents of sulfhydryl and the free amino groups were increased first and then decreased. Circular dichroism spectra and surface hydrophobicity studies evidenced that the disruption of α-helix conformation and the exposure of hydrophobic sites were induced by oxidized linoleic acid (OLA). Results. Of SDS-PAGE indicated that non-disulfide covalent linkages were implicated in the formation of cross-linking in myofibrillar proteins induced by OLA. The rheological tests revealed that the storage modulus (G′) of OLA moderate oxidative modification (≤ 2.5mmol/L) significantly increased, whereas the storage modulus (G′) of OLA excessive oxidative modification (>2.5mmol/L) significantly decreased. Moreover, microstructure analysis indicated the presence...

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