Synergistic effects of alternating magnetic field and sodium tripolyphosphate on functional properties of myofibrillar proteins in low-salt systems
文献类型： 外文期刊
作者： Li, Qiang 1 ; Xia, Lizhi 1 ; Lu, Jianfeng 1 ; Song, Yuan 1 ; Yang, Mengru 1 ; Zhou, Beibei 3 ; Lin, Lin 1 ; Miao, Wenhua 4 ; Zheng, Bin 5 ; Zheng, Zhi 1 ;
作者机构： 1.Hefei Univ Technol, Engn Res Ctr Bioproc, Sch Food & Biol Engn, MOE, Hefei, Peoples R China
2.Hefei Univ Technol, Sch Food & Biol Engn, Anhui Prov Key Lab Agr Prod Modern Proc, Hefei, Peoples R China
3.Anhui Acad Agr Sci, Fisheries Res Inst, Hefei, Peoples R China
4.Zhejiang Ocean Univ, Food & Pharm Coll, Zhoushan, Peoples R China
5.Zhejiang Univ Technol, Coll Food Sci & Engn, Hangzhou, Peoples R China
关键词： Myofibrillar protein; Alternating magnetic field; Sodium tripolyphosphate; Gel properties; Low salt
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）
ISSN： 0141-8130
年卷期： 2025 年 316 卷
页码：
收录情况： SCI
摘要： This study investigated the synergistic regulatory mechanisms of alternating magnetic field (AMF) and sodium tripolyphosphate (STPP) on the functional properties of myofibrillar protein (MP) in a low-salt environment. It was found that AMF promotes an increase in MP solubility. When the magnetic field strength was >6 mT, the formation of hydrophobic interactions within the MP molecules reached a dynamic equilibrium with the action of the AMF, resulting in a slowing down of the increase in MP solubility and emulsification activity. The intervention of STPP strengthened the extension of MP structure under the action of AMF and suppressed the intermolecular aggregation, and the solubility under the same magnetic field strength was further enhanced. However, the presence of STPP retained more alpha-helix for the MP gels, forcing a significant increase in beta-sheet in the AMF-modified MP gels mainly contributed by irregular curling. This resulted in a more ordered and stabilized MP gel structure, and the gel strength, textural properties and water-holding capacity were further enhanced. The study revealed the dual regulatory mechanism of AMF-STPP synergistic strategy on the functional properties of proteins, which provided a theoretical basis for the improvement of low-salt surimi products and the design of protein-based materials.
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