磁场
降水
化学
粒径
压实
结构稳定性
化学物理
表征(材料科学)
化学工程
材料科学
理论(学习稳定性)
收缩(语法)
纳米技术
密度泛函理论
领域(数学)
生物系统
粒子(生态学)
蛋白质二级结构
生物物理学
磁性结构
核磁共振
磁性纳米粒子
重组
还原(数学)
凝聚态物理
磁滞
作者
Xin Chang,Yonggang Yue,Zhijian Lu,Yue Tong,Jingjing Li,Z. Q. Hu,Lanjun Yang,Pei-Ling Liu
标识
DOI:10.1016/j.foodres.2025.117856
摘要
This study investigates the structural and functional changes of β-lactoglobulin (β-LG) under incremental magnetic fields (IMF: 5, 10, 15, 20 T). Multi-scale characterization reveals four stages of conformational transition: contraction (5 T), folded compaction (10 T), aggregation/refolding (15 T), and unfolding/etching (20 T). The magnetic field was found to induce ordering of the secondary structure and promote oxidation reactions among CC, C-O-C, and O-C=O groups, thereby enhancing the crystallinity, emulsifying properties, and freeze-thaw stability of β-LG. Notably, at 10 T, the particle size reached a minimum of 67.46 ± 2.33 μm, representing a 32.23 % reduction (p < 0.05). The secondary structure showed increased order, with α-helix and β-sheet contents of 7.45 % and 58.74 %, respectively. Functional properties were optimized at 10 T: emulsifying activity increased to 10.26 m2/g (a 34.82 % improvement) and emulsifying stability to 81.70 % (a 72.04 % improvement), while freeze-thaw water precipitation was reduced by 15.4 %. These results fully demonstrate that IMF can precisely restructure β-LG through oxidative folding-unfolding transitions, establishing 10 T as the critical magnetic field strength for enhancing functionality in dairy and bioactive delivery applications.
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