立陶宛
小虾
化学
精氨酸
生物化学
半胱氨酸
赖氨酸
糖基化
食品科学
过敏原
美拉德反应
氨基酸
表位
免疫球蛋白E
抗体
生物
抗原
过敏
免疫学
酶
渔业
受体
作者
Meng Liu,Fei Huan,Tian-Jiao Han,Sihan Liu,Mengsi Li,Yang Yang,Yunhui Wu,Gui-Xia Chen,Min‐Jie Cao,Guang‐Ming Liu
标识
DOI:10.1021/acs.jafc.1c00718
摘要
Allergic reactions occur after the whole food is ingested, rather than the purified allergen. The present study explores the low-allergenic food processing for Litopenaeus vannamei by analysis of macrostructure, digestibility, and immunoreactivity. Furthermore, the presence of modified amino acids on the reported IgE epitopes was analyzed by mass spectrometry. Results showed that the combination processing of Maillard reaction (shrimp meat with galactose) with high temperature-pressure at 115 °C obviously changed the macrostructure and increased the digestibility for the shrimp meat. Meanwhile, the processing significantly reduced the IgG/IgE-binding activity of the shrimp meat. The hypo-IgE-binding activity in processed shrimp may be due to the modification of lysine, arginine, and cysteine residues in antigen epitopes. This is a comprehensive assessment of the specific amino acid residues modified by glycation of multiple allergens in processed L. vannamei, which provides a new research method to explore the hypo-IgE-binding activity in food.
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