Abstract: In order to study the effect of lipid oxidation on protein oxidation, the primary lipid metabolite peroxyl radicals produced by 2,2'-azobis (2-amidinopropane) dihydrochloride (AAPH) was used to treat rabbit myofibrillar protein (MP). The results showed that with the increase of AAPH concentration, the carbonyl content, surface hydrophobicity, brightness and yellowness of rabbit meat MP increased significantly (P<0.05). However, the total sulfhydryl group, free ammonia, solubility, endogenous fluorescence intensity and the absolute value of Zeta potential of rabbit meat MP showed a significant decreasing trend (P<0.05). Moreover, the results of Raman spectroscopy showed that the α-helix content of MP decreased and the content of irregular coils increased, which further confirmed that the protein secondary structure had changed. Besides, sodium dodecyl sulfate-polyacrylamide gelelectrophoresis (SDS-PAGE)results showed that the pyrolysis products of AAPH could cause cross-linking and aggregation of MP, forming aggregates with larger molecular weight. As a result, peroxyl radicals can affect the physicochemical properties of MP by promoting the oxidation of rabbit meat myofibril protein, which provides a theoretical basis for controlling the oxidation of protein during the processing of rabbit meat by regulating lipid oxidation.
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