Lipid oxidation and protein oxidation occur side by side in meat. Here, the effect of malondialdehyde (MDA), the major product of lipid oxidation, on the digestibility of beef myofibrillar proteins (MP) was studied. MP samples were incubated with 0, 0.1, 0.3, 0.5, and 0.7 mM MDA at 4 °C for 12 h and then subjected to in vitro gastrointestinal digestion. The result showed that MDA remarkably reduced the digestibility of MP (p < 0.05). MDA treatments significantly increased carbonyl and Schiff base contents in MP (p < 0.05). The microstructure observed by atomic force microscopy showed that MDA treatments resulted in the aggregation of MP. Non-reducing and reducing electrophoresis suggested the aggregation was mainly caused by covalent bonds including disulfide bond and carbonyl−amine bond. Proteomics analysis proved that the myosin tail was the main target of MDA attack, meanwhile, lysine residues were the major modification sites. Taken together, the above results imply that MDA induces protein oxidation, aggregation, and blockage of hydrolysis sites, consequently leading to the decrease in both gastric and gastrointestinal digestibility of MP.
Keywords: in vitro digestion; lipid oxidation; malondialdehyde; oxidation sites; protein oxidation.