Quality enhancement of Pacific white shrimp (Litopenaeus vannamei) during frozen storage via static magnetic field-assisted freezing: insights into myofibrillar protein structure and functionality

  • Food Chem. 2026 Aug 1:519:149711. doi: 10.1016/j.foodchem.2026.149711.
Qinxiu Sun  1 Yao Chen  2 Qihang Wei  1 Ouyang Zheng  2 Jun Mei  3 Shucheng Liu  4
Affiliations
  • 1. 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.
  • 2. 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.
  • 3. College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China.
  • 4. 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. Electronic address: [email protected].
Abstract

The effect of air freezing (AF-35), immersion freezing (IF-35), and static magnetic field-assisted freezing at -35 °C and - 25 °C (MF-35, MF-25) on the structure and functional properties of myofibrillar protein (MP) in Litopenaeus vannamei during frozen storage was investigated in this study. MF-35 exhibited higher reactive/total sulfhydryl groups and solubility (P < 0.05). This indicates superior inhibition of protein oxidation and aggregation, and it also preserved the highest α-helical content and fluorescence strength (P < 0.05), which demonstrates it effectively minimized disorder in secondary structure and unfolding of the tertiary structure. MF-35's emulsifying stability, rheological properties, and gel strength surpassed Other treatments, demonstrating its effectiveness in mitigating MP emulsifying and gel properties degradation. IF-35 and MF-25 did not differ significantly in MP solubility, fluorescence intensity, or gel strength (P > 0.05). Overall, MF treatment delays MP degradation during frozen storage and also reduces energy use.

Keywords
Frozen storage; Functional property; Litopenaeus vannamei; Myofibrillar structure; Static magnetic field-assisted freezing.
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