大虾
原肌球蛋白
对虾
化学
渔业
食品科学
生物
生物化学
小虾
肌动蛋白
作者
Xiangfei Hu,Hui Wang,Yueming Hu,Pingwei Wen,Xiongchen Wu,Zongcai Tu
标识
DOI:10.1016/j.foodchem.2024.141376
摘要
The effect of electric field intensities (EFIs, 5-20 kV/cm) and treatment times (0.5-2 h) on allergenicity and spatial conformation of prawn tropomyosin was evaluated. The results demonstrated that the IgG and IgE binding capacity of tropomyosin maximally increased by 24.34 % and 29.16 % respectively, followed by a subsequent decrease after 20 kV/cm treatment for 1 h. Interestingly, 5-10 kV/cm treatments significantly decreased the α-helix content (P < 0.05) and fluorescence intensity, while 20 kV/cm treatment promoted extensive spiralization, resulting in a tightly packed structure. The increased flexibility further exposed the hydrolysis sites and strengthened the gastrointestinal digestibility of tropomyosin. Additionally, molecular dynamic simulation indicated that extended EFIs increased structural flexibility and depolymerized the tropomyosin dimers through destroying intermolecular hydrogen bonds (formed within arginine and glutamate), which allowed tropomyosin to be easily recognized by IgG/IgE. Whereas, decrease of solvent-accessibility surface area (SASA), hydrophobic surface area induced conformation folded and caused epitopes masked.
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