Mengzhe Li , Xin Wang , Tong Shi , Xiaoli Zhang , Wengang Jin , Li Yuan , Ruichang Gao
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引用次数: 0
Abstract
Myofibrillar protein (MP), a key functional protein in muscle foods, strongly affects emulsion stability. However, the impact of oxidation on its interfacial behavior remained unclear. This study aimed to clarify how oxidative modification affects the conformational behavior of snakehead (Channa argus) MP, its dynamic adsorption at the oil-water interface, and the related emulsifying properties. MP was oxidized with different H2O2 concentrations (0, 2, 4, 8, 16 mM). Moderate oxidation (≤ 4 mM) increased structural flexibility and exposed hydrophobic groups, thereby enhancing interfacial pressure, diffusion (Kdiff), penetration (KP), and rearrangement rates (KR). The 4 mM group produced the most stable emulsion with favorable rheology due to a compact interfacial film. In contrast, excessive oxidation (≥ 8 mM) promoted aggregation, buried hydrophobic sites, and reduced interfacial activity, leading to poor stability. These findings demonstrated that controlled oxidation could optimize MP functionality, providing a theoretical basis for developing protein-stability emulsion systems.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.