Wei Qihang, Sun Qinxiu, Hou Qian, Zheng Ouyang, Xiao Naiyong, Liu Shucheng
College of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Provincial Engineering Technology Research Center of Seafood, Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution, Zhanjiang 524088, China.
College of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Provincial Engineering Technology Research Center of Seafood, Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution, Zhanjiang 524088, China; Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, China.
Food Chem. 2025 Apr 15;471:142836. doi: 10.1016/j.foodchem.2025.142836. Epub 2025 Jan 10.
The effects of static magnetic field-assisted freezing (MF) on the structural and functional characteristics of Litopenaeus vannamei myofibrillar protein (MP) at various temperatures (-35 ∼ -20 °C) were examined to assess its influence on MP and its energy-saving potential. The results indicated that -35 °C MF (MF-35) exhibited greater solubility and lower turbidity than -35 °C immersion freezing (IF-35), suggesting that MF-35 inhibited MP aggregation. MF-35 prevented the reduction in fluorescence intensity and α-helix content, protecting the MP tertiary and secondary structures. The emulsifying stability and gel strength of MF-35 surpassed those of the other frozen samples, indicating that MF-35 was the most efficient at mitigating the degradation of MP emulsifying and gel properties generated by freezing. No significant differences in solubility, surface hydrophobicity, emulsifying activity, and gel strength were detected between IF-35 and MF-25 (P > 0.05). In conclusion, MF impeded the denaturation of MP and exhibited energy-saving potential.
研究了静磁场辅助冷冻（MF）在不同温度（-35 ∼ -20°C）下对凡纳滨对虾肌原纤维蛋白（MP）结构和功能特性的影响，以评估其对MP的影响及其节能潜力。结果表明，-35°C的MF（MF-35）比-35°C的浸渍冷冻（IF-35）具有更高的溶解度和更低的浊度，这表明MF-35抑制了MP的聚集。MF-35阻止了荧光强度和α-螺旋含量的降低，保护了MP的三级和二级结构。MF-35的乳化稳定性和凝胶强度超过了其他冷冻样品，表明MF-35在减轻冷冻引起的MP乳化和凝胶性能降解方面最有效。IF-35和MF-25之间在溶解度、表面疏水性、乳化活性和凝胶强度方面未检测到显著差异（P > 0.05）。总之，MF阻碍了MP的变性并具有节能潜力。
