Protein oxidation is a critical process in the deterioration and spoilage of fish and related commodities during processing and storage. In this study, the hydroxyl radical generation system (HRGS) was used to simulate the effect of oxidation on the functional, conformational and gelling properties of topmouth culter (Culter alburnus) myofibrillar proteins (MP). Additionally, the effects of oxidation on the gel-forming abilities of MP were also systematically analyzed from the perspective of intermolecular interaction forces. Oxidation was shown to decrease the total sulfhydryl content, increase the surface hydrophobicity, and induce conformational changes in MP. Rheological analysis showed that oxidation reduced the gel strength. Water holding capacity (WHC) and low-field nuclear magnetic resonance (LF-NMR) analyses showed that low oxidation could enhance water binding of protein matrix, while high-degree oxidation could substantially reduce the gelling properties of MP. The selective solubility of MP gel proved that oxidation could reduce the content of ionic and hydrogen bonds and increase hydrophobic interactions. All the results indicate that oxidation could alter the intermolecular interactions between protein-protein and protein-water molecules, due to irregular unfolding and inhibition of the cross-linking of amino acid side chains, leading to reduction in the quality and function of fish and related products.
Keywords: Culter alburnus; Intermolecular interaction force; Myofibrillar protein; Protein oxidation.
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