Effect of ultrasound-assisted phosphates treatment on solubilization and stable dispersion of rabbit Myofibrillar proteins at low ionic strength

Chang Su; Yuxin Huang; Jiaxin Chen; Hongjun Li; Dong Zhang; Yong Tang

doi:10.1016/j.foodchem.2025.142898

Effect of ultrasound-assisted phosphates treatment on solubilization and stable dispersion of rabbit Myofibrillar proteins at low ionic strength

Food Chem. 2025 Jan 13:472:142898. doi: 10.1016/j.foodchem.2025.142898. Online ahead of print.

Authors

Chang Su¹, Yuxin Huang¹, Jiaxin Chen², Hongjun Li³, Dong Zhang¹, Yong Tang⁴

Affiliations

¹ 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.
² 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.
³ College of Food Science, Southwest University, Chongqing 400715, China.
⁴ 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. Electronic address: yongtang@mail.xhu.edu.cn.

PMID: 39862610
DOI: 10.1016/j.foodchem.2025.142898

Abstract

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.

Keywords: Dispersibility; High intensity ultrasound; Myofibrillar proteins; Phosphate medium; Solubility; Synergistic effect.