研究报告

欧姆加热处理对南美白对虾原肌球蛋白结构及致敏性的影响

  • 方淇 ,
  • 杨耀冲 ,
  • 金银哲 ,
  • 蒋蝉聪
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  • 1(上海海洋大学 食品学院,上海,201306)
    2(上海海洋大学 食品热加工工程中心,上海,201306)
第一作者:硕士研究生(金银哲副教授和蒋蝉聪博士为共同通信作者,E-mail:yzjin@shou.edu.cn;454088567@qq.com)

收稿日期: 2025-10-20

  修回日期: 2025-12-16

  网络出版日期: 2026-09-10

基金资助

国家重点研发计划项目(2020YFD0900905)

Effect of ohmic heating treatment on the structure and allergenicity of tropomyosin from Litopenaeus vannamei

  • FANG Qi ,
  • YANG Yaochong ,
  • JIN Yinzhe ,
  • JIANG Chancong
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  • 1(College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China)
    2(Engineering Research Center of Food Thermal-Processing Technology, Shanghai Ocean University, Shanghai 201306, China)

Received date: 2025-10-20

  Revised date: 2025-12-16

  Online published: 2026-09-10

摘要

该研究旨在系统解析不同欧姆加热(ohmic heating,OH)处理时间(0~130 min)对原肌球蛋白(tropomyosin,TM)构象变化与致敏性消减规律的影响,以揭示OH处理降低其致敏性的结构基础。该研究首先纯化了TM,并将所得纯化TM,于100 ℃、120 V条件下进行OH处理。通过间接酶联免疫吸附实验(enzyme-linked immunosorbent assay,ELISA)评估其免疫球蛋白(immunoglobulin,Ig)G/IgE结合能力。同时,运用SDS-PAGE、圆二色光谱、荧光光谱、紫外光谱、粒径分析、差示扫描量热法(differential scanning calorimetry,DSC)等技术表征了TM的结构变化。结果表明,OH处理70 min后,TM的IgG/IgE结合能力显著下降(P<0.05),分别降至未处理组的73.24%和70.21%。结构分析表明,致敏性降低与TM构象变化密切相关,OH处理破坏了TM的二级和三级结构,并导致蛋白粒径增大和热稳定性改变,这预示着致敏表位被遮蔽或破坏。氨基酸分析进一步表明,包括谷氨酸在内的多种关键致敏氨基酸含量降低,为IgG/IgE结合能力下降提供证据。该研究阐明了OH处理通过诱导TM构象变化以降低其致敏性的作用机制,为基于OH技术的水产品过敏原消减策略提供了重要的理论依据。

本文引用格式

方淇 , 杨耀冲 , 金银哲 , 蒋蝉聪 . 欧姆加热处理对南美白对虾原肌球蛋白结构及致敏性的影响[J]. 食品与发酵工业, 2026 , 52(16) : 107 -114 . DOI: 10.13995/j.cnki.11-1802/ts.044837

Abstract

This study systematically analyzed the effects of ohmic heating (OH) treatment duration (0-130 min) on the conformation and allergenicity of tropomyosin (TM) to reveal the underlying structural mechanisms.Purified TM underwent OH treatment at 100 ℃ and 120 V.An indirect enzyme-linked immunosorbent assay (ELISA) assessed its IgG/IgE binding capacity.Structural changes were characterized using SDS-PAGE, circular dichroism spectroscopy, fluorescence spectroscopy, UV spectroscopy, particle size analysis, and differential scanning calorimetry (DSC).Results showed that after 70 min of OH treatment, the IgG/IgE binding capacity of TM significantly decreased (P<0.05) to 73.24% and 70.21% of the untreated group, respectively.The reduction in allergenicity correlated with conformational changes, OH treatment disrupted the secondary and tertiary structures of TM, increased protein particle size, and altered thermal stability, suggesting the masking or destruction of allergenic epitopes.Amino acid analysis further indicated a decrease in key allergenic amino acids, including glutamic acid, explaining the reduced IgG/IgE binding.This work elucidated how OH treatment reduces TM allergenicity by inducing conformational changes, providing a theoretical basis for OH-based strategies to mitigate allergens in aquatic products.

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