State Key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Products Processing, Ministry of Agriculture, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
State Key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Products Processing, Ministry of Agriculture, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Ultrason Sonochem. 2024 Nov;110:107059. doi: 10.1016/j.ultsonch.2024.107059. Epub 2024 Sep 5.
The aim of the present study was to evaluate the effects of ultrasound-assisted intermittent tumbling (UT) at 300 W, 20 kHz and 40 min on the conformation, intermolecular interactions and aggregation of myofibrillar proteins (MPs) and its induced gelation properties at various tumbling times (4 and 6 h). Raman results showed that all tumbling treatments led the helical structure of MPs to unfold. In comparison to the single intermittent tumbling treatment (ST), UT treatment exerted more pronounced effects on strengthening the intermolecular hydrogen bonds and facilitating the formation of an ordered β-sheet structure. When the tumbling time was the same, UT treatment caused higher surface hydrophobicity, fluorescence intensity and disulfide bond content in the MPs, inducing the occurrence of hydrophobic interaction and disulfide cross-linking between MPs molecules, thus forming the MPs aggregates. Additionally, results from the solubility, particle size, atomic force microscopy and SDS-PAGE further indicated that, relative to the ST treatment, UT treatment was more potent in promoting the polymerization of myosin heavy chain. The MPs aggregates in the UT group were more uniform than those in the ST group. During the gelation process, the pre-formed MPs aggregates in the UT treatment increased the thermal stability of myosin, rendering it more resistant to heat-induced unfolding of the myosin rod region. Furthermore, they improved the protein tail-tail interaction, resulting in the formation of a well-structured gel network with higher gel strength and cooking yield compared to the ST treatment.
本研究旨在评估 300W、20kHz 下超声辅助间歇翻滚（UT）40min 对肌原纤维蛋白（MPs）构象、分子间相互作用和聚集的影响及其在不同翻滚时间（4h 和 6h）下诱导凝胶特性的影响。拉曼结果表明，所有翻滚处理均导致 MPs 的螺旋结构展开。与单次间歇翻滚处理（ST）相比，UT 处理对增强分子间氢键和促进有序β-折叠结构形成具有更显著的效果。当翻滚时间相同时，UT 处理导致 MPs 的表面疏水性、荧光强度和二硫键含量更高，诱导 MPs 分子间疏水相互作用和二硫键交联的发生，从而形成 MPs 聚集物。此外，溶解度、粒径、原子力显微镜和 SDS-PAGE 的结果进一步表明，与 ST 处理相比，UT 处理更能促进肌球蛋白重链的聚合。与 ST 处理相比，UT 处理组的 MPs 聚集物更均匀。在凝胶化过程中，UT 处理中预先形成的 MPs 聚集物提高了肌球蛋白的热稳定性，使其更能抵抗热诱导的肌球蛋白杆区展开。此外，它们改善了蛋白质尾部-尾部相互作用，形成了具有更高凝胶强度和蒸煮产率的结构良好的凝胶网络，与 ST 处理相比。
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