• 生物工程 •

### 植物乳杆菌（Lactobacillus plantarum）对过敏原原肌球蛋白免疫活性的消减作用

1. （1.上海海洋大学食品学院，上海水产品加工及贮藏工程技术研究中心，上海 201306；2.上海海洋大学 农业农村部水产品贮藏保鲜质量安全风险评估实验室，上海 201306）
• 发布日期:2021-09-29
• 基金资助:
“十三五”国家重点研发计划重点专项（2019YFD0902003）；上海市科技兴农重点攻关项目（沪农科攻字(2016)第4-4号）

### Effect of Lactobacillus plantarum on Reducing the Immunological Activity of Tropomyosin

XIAO Ye, YE Jingqin, LI Xiaochen, LI Xiaohui, SHI Wenzheng, LU Ying

1. (1. Shanghai Engineering Research Center of Aquatic Product Processing & Preservation, College of Food Sciences and Techology, Shanghai Ocean University, Shanghai 201306, China; 2. Laboratory of Quality & Safety Risk Assessment for Aquatic Products on Storage and Preservation, Ministry of Agriculture and Rural Affairs, Shanghai Ocean University, Shanghai 201306, China)
• Published:2021-09-29

Abstract: The impact of Lactobacillus plantarum on the immunological activity of tropomyosin (TM) as the major shrimp allergen was investigated. TM enriched and purified from Penaeus vanname was hydrolyzed for durations between 12 and 48 h with the viable cells, broken cell contents, cell debris and intracellular enzyme extracts of L. plantarum, the cells from which protein, fat or lipoteichoic acid was removed, and those subjected to carboxyl esterification or aminomethylation, separately. The immunological activity was analyzed by SDS-PAGE, Western-blot and competitive enzyme linked immunosorbent assay (ELISA). In order to analyze the site of action of L. plantarum on TM for reduced immunological activity, epitope polyclonal antibodies combined with infrared spectroscopy was used to explore the influence of L. plantarum on the secondary structure and allergenic epitopes of TM. The immunological analysis results showed that the highest percentage reduction (76.9%) of its immunological activity was obtained when TM was treated with the viable cells for 48 h, and the lowest percentage reduction was observed with the cell debris and the aminomethylated cells (60.7% and 61.7%, respectively), indicating that L. plantarum reduced the immunological activity of TM. The infrared spectroscopy and ELISA results displayed that L. plantarum could greatly change the secondary structure and allergenic epitopes of TM, while the aminomethylated cells and cell debris caused the least damage to the α-helical structure and allergenic epitopes of TM, resulting in less folded structure and thus exerting the worst effect on reducing the immunological activity of TM. Additionally, it was found that amino groups may be an important site of action for L. plantarum to reduce the immunological activity of TM. The findings of this study will provide a theoretical reference to control the allergenicity of food allergens and for the development of hypoallergenic aquatic products.