Su Chang, Huang Yuxin, Chen Jiaxin, Li Hongjun, Zhang Dong, Tang Yong
College of Food and Bioengineering, Xihua University, Chengdu 610039, China; Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Chengdu 610039, China; School of Future Food Modern Industry, Xihua University, Chengdu 610039, China.
College of Food and Bioengineering, Xihua University, Chengdu 610039, China; Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Chengdu 610039, China.
Food Chem. 2025 Apr 30;472:142898. doi: 10.1016/j.foodchem.2025.142898. Epub 2025 Jan 13.
The effects of high-intensity ultrasound (HIU) on the dispersibility of myofibrillar proteins (MPs) in low-salt medium were investigated. HIU-assisted STPP or TSPP could sharply improve the solubility and dispersibility of MPs (from 38.12 % to 94.08 % and 37.80 % to 89.91 %, respectively), whereas the use of NaCl or SHMP had negligible effects. MPs in STPP and TSPP medium had higher surface charge and stronger hydrophilic ability than those in NaCl and SHMP medium. The results of CLSM and SDS-PAGE showed MP depolymerization in STPP and TSPP medium. MPs in STPP and TSPP displayed a flexible α-helix conformation. HIU could induce the rearrangement of myosin and actin in STPP and TSPP medium and generated soluble oligomers by disulfide bonds. By contrast, MPs in SHMP and NaCl exhibited a stable β-sheet conformation, hindering the modification effect of HIU. Medium could affect the modification effect of HIU on MPs by changing surface charge and hydrophilicity.
研究了高强度超声（HIU）对低盐介质中肌原纤维蛋白（MPs）分散性的影响。HIU辅助的三聚磷酸钠（STPP）或焦磷酸钠（TSPP）可显著提高MPs的溶解度和分散性（分别从38.12%提高到94.08%和从37.80%提高到89.91%），而氯化钠（NaCl）或六偏磷酸钠（SHMP）的作用可忽略不计。STPP和TSPP介质中的MPs比NaCl和SHMP介质中的MPs具有更高的表面电荷和更强的亲水性。共聚焦激光扫描显微镜（CLSM）和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）结果表明STPP和TSPP介质中的MPs发生了解聚。STPP和TSPP中的MPs呈现出灵活的α-螺旋构象。HIU可诱导STPP和TSPP介质中肌球蛋白和肌动蛋白的重排，并通过二硫键生成可溶性低聚物。相比之下，SHMP和NaCl中的MPs呈现出稳定的β-折叠构象，阻碍了HIU的修饰作用。介质可通过改变表面电荷和亲水性来影响HIU对MPs的修饰作用。
