Effect of Malondialdehyde Oxidation on the Structure and Functional Properties of Myofibrillar Protein in Yak Meat

To explore the effect of different levels of lipid oxidation on the structural and functional properties of myofibrillar protein (MP) in yak meat, the oxidation of side-chain amino acids, structure, rheological characteristics, and emulsion stability of MP incubated in the presence of different concentrations (0, 0.1, 1, 5, 10 and 20 mmol/L) of malondialdehyde (MDA) were measured. The results showed that with an increase in MDA concentration, the contents of carbonyl group, MDA-MP adducts and dimeric tyrosine and the relative content of β-turn in MP overall increased, while total sulfhydryl content, surface hydrophobicity, endogenous fluorescence intensity, and the relative contents of α-helix and β-sheet decreased. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results indicated gradual loss of myosin heavy and light chains, implying that interaction with MDA could induce MP oxidation and cross-linked aggregation and result in structural transition from an ordered to a disordered state. In addition, moderate oxidation (with MAD concentration < 10 mmol/L) increased the storage and loss moduli and improved the gel quality of MP; however, excessive oxidation (with MAD concentration ≥ 10 mmol/L) led to serious aggregation of MP and a decrease in the storage and loss moduli as well as a decrease in the emulsion stability and color deterioration. In conclusion, MDA oxidation can promote the oxidation of MP, and alter the structural and functional properties.