Effects of malondialdehyde as a byproduct of lipid oxidation on protein oxidation in rabbit meat

•The effects of malondialdehyde on myofibrillar proteins oxidation in muscle homogenate of rabbit meat were investigated.•Malondialdehyde could directly cause myoglobin autoxidation and myofibrillar protein carbonylation.•Malondialdehyde could promote the formation of hypervalent myoglobin species and release of non-heme iron, thereby promoting myofibrillar proteins oxidation. The effects of malondialdehyde (MDA) as a byproduct of lipid oxidation on myoglobin and myofibrillar proteins (MP) oxidations in muscle homogenates containing components native to rabbit muscle were investigated. For myoglobin, MDA could lead to increase in metmyoglobin percentage. For MP, MDA could promote protein carbonylation and loss of tryptophan fluorescence. In addition, MDA could affect reactive oxygen species (ROS)-generating system by promoting the formation of hypervalent myoglobin species and release of non-heme iron. The result of MDA-MP adducts fluorescence intensity indicated that ROS-generating systems may be the main reason for protein carbonylation at the later of incubation treatment. SDS-PAGE analysis revealed that the ability of ROS-generating systems to facilitate protein oxidation was enhanced with MDA, which was responsible for the formation of protein cross-linking throughout incubation treatment. Taken together, the ability of MDA on promoting the oxidation of MP in rabbit muscle homogenates may be relied on both adduct reactions and the influence on ROS-generating system.