食品科学 ›› 2026, Vol. 47 ›› Issue (17): 60-67.doi: 10.7506/spkx1002-6630-20260209-071

• 食品化学 • 上一篇    下一篇

酰化修饰降低鲢鱼小清蛋白致敏性的机制

王舒涵,张敏,刘洁,刘俊,邵艳红,王旭梅   

  1. (1.江西师范大学药学院,江西?南昌 330022;2.江西师范大学生命科学学院,江西?南昌 330022)
  • 出版日期:2026-09-15 发布日期:2026-09-03
  • 基金资助:
    江西省自然科学基金青年项目(20242BAB20320);江西省职业早期青年科技人才培养项目(20244BCE52014); 江西省教育厅青年项目(GJJ2400205);广东省岭南特色食品科学与技术重点实验室开放基金课题(2025省003-1)

Mechanism by Which Acylation Modification Reduces the Allergenicity of Silver Carp Parvalbumin

WANG Shuhan, ZHANG Min, LIU Jie, LIU Jun, SHAO Yanhong, WANG Xumei   

  1. (1. College of Pharmacy, Jiangxi Normal University, Nanchang 330022, China;2. College of Life Sciences, Jiangxi Normal University, Nanchang 330022, China)
  • Online:2026-09-15 Published:2026-09-03

摘要: 以鲢鱼小清蛋白(parvalbumin,PV)为研究对象,采用辛烯基琥珀酸酐(octenyl succinic anhydride,OSA)对其进行酰化修饰。通过光谱学、质谱学和间接酶联免疫吸附测定等技术,分析修饰前后PV的结构及致敏性变化情况。结果表明,OSA与PV之间通过共价结合,导致PV分子质量增加。光谱学分析发现,酰化修饰后PV紫外-可见光谱吸光度和内源荧光强度下降,且游离巯基含量显著降低。质谱分析显示,Lys39、Lys84、Lys88、Lys97及Ser37是OSA的主要酰化位点。致敏性分析结果表明,酰化修饰PV的免疫球蛋白(immunoglobulin,Ig)G/IgE结合能力显著下降。综上,酰化修饰通过破坏PV的致敏表位从而降低其致敏性,因此,基于OSA的酰化修饰是一种有效降低过敏原致敏性的技术。

关键词: 小清蛋白;辛烯基琥珀酸酐;酰化修饰;结构;致敏性

Abstract: Silver carp parvalbumin (PV) was acylated with octenyl succinic anhydride (OSA). The structural and allergenicity changes of PV before and after modification were determined using spectroscopy, mass spectrometry (MS), and an indirect enzyme-linked immunosorbent assay (ELISA). The results indicated that covalent binding occurred between OSA and PV, which led to an increase in the molecular mass of PV. Spectroscopic analysis revealed that after acylation modification, the ultraviolet (UV) absorbance and intrinsic fluorescence intensity of PV decreased, and the free sulfhydryl content significantly fell. MS showed that Lys39, Lys84, Lys88, Lys97, and Ser37 were the primary acylation sites for OSA. Allergenicity analysis results demonstrated that the immunoglobulin (Ig)G/IgE binding capacity of acylated PV was significantly reduced compared with that of native PV. In conclusion, acylation modification reduced the allergenicity of PV by disrupting its allergenic epitopes. Therefore, OSA-based acylation modification is an effective technique for reducing the allergenicity of allergens.

Key words: parvalbumin; octenyl succinic anhydride; acylation modification; structure; allergenicity

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