In this study, golden pomfret myofibrillar protein (MP) was used as the research object, and the oxidation system of malondialdehyde (MDA) as an inducer and the static digestion model in vitro was established for the analysis of the changes in protein structure and molecular morphology during oxidation and digestion. Subsequently, the effects of MDA-mediated oxidation on the structure and digestive properties of golden pomfret myofibrillar fibrillar protein were determined. The results showed that the hydrolysis degree and digestion rate of MP were inhibited with the increase in MDA concentration (0, 0.5, 1, 2, 5, 10 mmol/L), and the carbonyl group, surface hydrophobicity, irregular curling, and MDA content increased significantly (P < 0.05), whereas the total sulfhydryl groups, α-helices, free amino groups, hydrolysis degree, and MDA incorporation decreased significantly (P < 0.05), The molecular particle size was significantly reduced (P < 0.05), and the molecular morphology and molecular structure were analyzed (P >0.05). Finally, the molecular size and cross-linking degree gradually increased. In conclusion, MDA can alter the structure and morphology of proteins, resulting in a decrease in hydrolysis and digestion rate. This study can provide theoretical support and reference for the regulation of protein digestion.
Keywords: Golden pomfret; In vitro digestion; Malondialdehyde oxidation; Myofibrillar protein; Protein structure.
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