Abstract: Sarcoplasmic proteins (SP) derived from yak meat were oxidized by malondialdehyde (MDA) at different concentrations. The effects of lipid oxidation on physicochemical properties and color stability of SP were investigated by evaluating side-chain amino acid oxidation, protein structure and color of SP and the oxidation status of myoglobin (Mb). The results showed that after MDA oxidation, the a* value, b* value, C* value, and deoxymyoglobin and oxymyoglobin contents of SP significantly decreased (P < 0.05), and the L* value, metmyoglobin content, and ferrylmyoglobin concentration significantly increased (P < 0.05), indicating that MDA oxidation lowered color stability. The contents of carbonyl groups and dimeric tyrosine, the fluorescence intensity of SP-MDA adducts, and the relative contents of β-helix and β-turn significantly increased (P < 0.05), and total sulfhydryl content, surface hydrophobicity, intrinsic fluorescence intensity, and the relative contents of α-helix and random coil significantly declined (P < 0.05). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed blurred expansion of small molecule bands and the formation of macromolecular aggregates, suggesting that MDA promoted the oxidation and aggregation of SP. Pearson correlation analysis revealed significant correlations between MDA oxidation and physicochemical properties and color stability of SP (P < 0.05). This study reveals that MDA alters the structure of SP by directly oxidizing it or mediating Mb oxidation, causing cross-linked aggregation of SP and reducing its color stability.

Key words: malondialdehyde oxidation; sarcoplasmic protein; color stability; yak meat