Oxidized myoglobin: Revealing new perspectives and insights on factors affecting the water retention of myofibrillar proteins.

The impact of oxidized myoglobin (Mb) on myofibrillar protein (MP) oxidation and water retention was investigated. Results showed that the oxidation of Mb increased with increasing concentration of oxidized linoleic acid (OLA). In the presence of 100 mmol/L OLA, hemin iron decreased by 62.07 % compared to the control group. Further investigation showed that mild oxidation of Mb (≤10 mmol/L OLA) increased the water retention and the absolute value of the zeta potential of MP, whereas excessive oxidation (>10 mmol/L OLA) decreased these properties. With the increase of Mb oxidation, the carbonyl content in MP increased, and α-helices changed to random helix. And the tertiary structure changed. Pearson correlation analysis suggested that oxidized Mb affected the water retention of MP, which was closely related to hemin iron and non-hemin iron. In conclusion, OLA induced Mb oxidation, further promoted MP oxidation and affected its water retention.

Effect of MDA-mediated oxidation on the protein structure and digestive properties of golden pomfret.

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.