Song Futeng, Gu Qingping, Liu Lu, Xu Tianjiao, Li Lulu, Yang Qingli, Lv Liangtao
School of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China.
School of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China.
Food Chem. 2025 Oct 1;488:144910. doi: 10.1016/j.foodchem.2025.144910. Epub 2025 May 24.
This study aims to investigate the allergenicity and gel properties of shrimp myofibrillar protein (MP) cross-linked by different concentrations of transglutaminase (TG) for shrimp gel products. The structural changes of the samples were analyzed using methods such as SDS-PAGE, CD, and UV, revealing that TG cross-linking significantly altered the protein structure. Changes in allergenicity were verified through Western blot and ELISA. The results indicated that TG cross-linked MP reduced its IgE-binding capacity, with the most significant reduction in allergenicity observed at a TG concentration of 90 U/g. The microscopic structure of the gels was validated using 3D printing and scanning electron microscopy, showing significant differences in the aggregation of MP molecules under different concentrations of TG. At 90 U/g, the samples exhibited a tightly knit three-dimensional gel network structure with good printing suitability and precision. This study provides theoretical guidance for producing safer shrimp gel products in the food industry.
本研究旨在探讨不同浓度转谷氨酰胺酶(TG)交联虾肌原纤维蛋白(MP)用于虾凝胶产品时的致敏性和凝胶特性。采用SDS-PAGE、圆二色光谱(CD)和紫外光谱(UV)等方法分析样品的结构变化,结果表明TG交联显著改变了蛋白质结构。通过蛋白质免疫印迹法(Western blot)和酶联免疫吸附测定(ELISA)验证致敏性的变化。结果表明,TG交联的MP降低了其IgE结合能力,在TG浓度为90 U/g时观察到致敏性降低最为显著。使用3D打印和扫描电子显微镜验证凝胶的微观结构,结果显示在不同浓度的TG下MP分子的聚集存在显著差异。在90 U/g时,样品呈现出紧密的三维凝胶网络结构,具有良好的打印适用性和精度。本研究为食品工业生产更安全的虾凝胶产品提供了理论指导。