Impact of protein succinylation and myofibrillar protein-lipid co-oxidation interactions on heterocyclic amine formation of thermally processed goose meat.

This study investigated the mechanisms by which protein succinylation and protein-lipid co-oxidation affect protein structural changes, oxidative reactions, the progression of the Maillard reaction, volatile flavor formation, and heterocyclic amine (HCA) generation as evaluated by chemical model systems. The results showed that, under chemical model systems, succinylation induced partial protein unfolding and slight aggregation, reduced the α-helix content, and promoted protein structural rearrangement. Protein succinylation significantly inhibited protein-lipid co-oxidation, as evidenced by decreases in sulfhydryl oxidation, carbonyl formation, and thiobarbituric acid-reactive substances, indicating its effectiveness in alleviating overall oxidative damage. The Maillard reaction was most pronounced in the protein-lipid chemical model system, whereas protein succinylation significantly suppressed its progression in tested systems. The consumption of creatine and reducing sugars was jointly regulated by the Maillard reaction and oxidative processes. By coordinately modulating these reaction pathways, protein succinylation reduced the consumption rates of key HCA precursors. Volatile flavor analysis showed that the lipid chemical model system was dominated by lipid oxidation products, such as nonanal and decanal, whereas the protein chemical model system mainly contained protein oxidation-related compounds and nitrogen-containing derivatives. In contrast, the protein-lipid co-oxidation chemical model system contained abundant lipid oxidation products, protein oxidation products and Maillard reaction products such as pyrazines, indicating the strong dependence of volatile compound profiles on system composition. In addition, pronounced synergistic amplification among multiple reaction pathways jointly shaped the flavor characteristics generated during thermal processing. The protein-lipid co-oxidation chemical model system exhibited the highest HCA levels because of the combined effects of the Maillard reaction and oxidative reactions. Succinylation significantly inhibited HCA formation in the protein chemical model system, with an inhibition rate of 49.91 ± 0.68%. However, its inhibitory effect was markedly weakened in the protein-lipid co-oxidation chemical model system, with an inhibition rate of only 3.01 ± 2.32% showing no significant difference. These results demonstrated that protein succinylation reshaped thermal processing reaction pathways related to HCA formation by regulating protein conformation and suppressing oxidative and Maillard reaction networks, providing a theoretical basis for reducing HCA formation in processed meat products.