Key Laboratory of Meat Processing and Quality Control, Ministry of Education; National Center of Meat Quality and Safety Control; Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control; College of Food Science and Technology; Nanjing Agricultural University, Nanjing 210095, PR China.
Key Laboratory of Meat Processing and Quality Control, Ministry of Education; National Center of Meat Quality and Safety Control; Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control; College of Food Science and Technology; Nanjing Agricultural University, Nanjing 210095, PR China.
Food Res Int. 2023 Jan;163:112154. doi: 10.1016/j.foodres.2022.112154. Epub 2022 Nov 19.
Great interests have been attracted toward muscle protein in a water-soluble state with improved functionality for further designing meat protein fortified low-salt functional foods. In the present study, electrostatic interaction of chitosan (CH) with myofibrillar proteins (MP) in water aqueous solution was investigated, and the linked structure changes and emulsion stabilization of MP were studied. Results showed that the electrostatic interaction inhibited MP aggregation, and smaller particle size complexes were formed at pH 6.0, leading to the loss of β-sheet contents and recovery of α-helix contents with decreasing MP/CH mixing ratio (5:1 and 1:1). The tertiary structure confirmed the conformation changes of MP in which more hydrophobic groups and active sulfhydryl groups were exposed (P < 0.05), and the fluorescence was also quenched. With decreasing mixing ratio, the droplet size of emulsion decreased (P < 0.05), while the absorbed protein content increased (P < 0.05). After 7 d of storage, complex at a ratio of 1:1 displayed desirable emulsion stability, which could be due to the improved emulsifying capacity, enhanced electrostatic repulsion and steric effects. These findings provide a better understanding of conformation changes of MP in water aqueous solution induced by electrostatic interactions at mild acidic pH and help to fabricate stable protein/polysaccharide emulsification systems for further developing meat protein-based functional food to deliver health.
人们对水溶性肌肉蛋白产生了浓厚的兴趣，因为其具有改善功能，可进一步设计强化低盐功能性肉类蛋白质食品。在本研究中，研究了在水相溶液中壳聚糖（CH）与肌原纤维蛋白（MP）之间的静电相互作用，并研究了 MP 的链接结构变化和乳液稳定性。结果表明，静电相互作用抑制了 MP 的聚集，并且在 pH 值为 6.0 时形成了较小的颗粒尺寸复合物，导致β-折叠含量的损失和α-螺旋含量的恢复，随着 MP/CH 混合比（5:1 和 1:1）的降低。三级结构证实了 MP 的构象变化，其中更多的疏水性基团和活性巯基暴露（P<0.05），并且荧光也被猝灭。随着混合比的降低，乳液的液滴尺寸减小（P<0.05），而吸收的蛋白质含量增加（P<0.05）。在 7 天的储存期后，比例为 1:1 的复合物显示出良好的乳液稳定性，这可能是由于乳化能力提高、静电排斥和空间位阻效应增强所致。这些发现提供了对在温和酸性 pH 值下静电相互作用诱导的 MP 在水相溶液中构象变化的更好理解，并有助于制造稳定的蛋白质/多糖乳化系统，以进一步开发基于肉类蛋白质的功能性食品来促进健康。
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