食品科学 ›› 2017, Vol. 38 ›› Issue (23): 51-58.doi: 10.7506/spkx1002-6630-201723009

• 基础研究 • 上一篇    下一篇

热加工对鸡蛋中4种主要过敏原结构的影响

刘 珂1,2,熊丽姬1,2,高金燕2,陈红兵1,3,佟 平1,*   

  1. 1.南昌大学 食品科学与技术国家重点实验室,江西 南昌 330047;2.南昌大学食品学院,江西 南昌 330047;3.南昌大学中德联合研究院,江西 南昌 330047
  • 出版日期:2017-12-15 发布日期:2017-12-07
  • 基金资助:
    国家高技术研究发展计划(863计划)项目(2013AA102205);国家自然科学基金青年科学基金项目(31301524); 江西省科技厅重点研发计划项目(20161BBG70062);江西省自然科学基金重点项目(20133ACB20009); 食品科学与技术国家重点实验室项目(SKLF-ZZA-201612;SKLF-QN-201514)

Effect of Thermal Processing on Structure of Four Major Egg White Allergens

LIU Ke1,2, XIONG Liji1,2, GAO Jinyan2, CHEN Hongbing1,3, TONG Ping1,*   

  1. 1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; 2. School of Food Science and Technology, Nanchang University, Nanchang 330047, China; 3. Sino-German Joint Research Institute, Nanchang University, Nanchang 330047, China
  • Online:2017-12-15 Published:2017-12-07

摘要: 为探究热加工对鸡蛋主要过敏原结构的影响,对鸡蛋清中的4 种过敏原进行不同条件的热加工,并利用圆 二色光谱、紫外-可见光光谱、外源荧光光谱对加热前后过敏原的空间结构进行表征。结果表明,卵转铁蛋白对热 不稳定,随加热时间的延长和温度的升高,分子结构逐渐展开,芳香族残基和疏水基团暴露于分子表面;轻微加热 使卵白蛋白分子的二级结构更加有序,吸光度减小,表面疏水性增大,随着加热程度的增大,其二级结构变得无 序,分子发生聚集;加热后卵类黏蛋白的二级结构较为稳定,轻微加热其分子展开,吸光度和荧光强度增大,继续 加热使蛋白分子部分聚集;热处理使溶菌酶分子的有序性下降,芳香族残基和疏水基团逐渐暴露,但随着加热程度 的增加,蛋白分子发生部分聚集。本实验结果为后续研究加热对鸡蛋过敏原致敏性的影响提供理论依据。

关键词: 热加工, 鸡蛋过敏原, 光谱分析, 结构

Abstract: In order to explore the impact of thermal processing on the structure of egg white allergens, four major allergens in hen’s egg white were heated under different conditions of temperature and time. Circular dichroism, ultraviolet and fluorescence spectroscopy were used to detect the spatial structure of allergens. Results showed that ovotransferrin was unstable to heat, and its molecular structure was unfolded, with the aromatic residues and hydrophobic groups exposed on the molecular surface after heating. The secondary structure of ovalbumin became more ordered, ultraviolet absorbance value decreased, and surface hydrophobicity increased when it was heated slightly; however, with increasing temperature and heating time, ovalbumin became unordered and aggregated. The secondary structure of ovomucoid was relatively stable, and its molecules were unfolded after mild heating, leading to increased absorption and fluorescence intensities, and then aggregated partly after further heating. The secondary structure of lysozyme became disordered with the aromatic residues and hydrophobic groups gradually exposed after heating, but with increasing degree of heating, part of lysozyme became aggregated. The present study may provide a theoretical basis for studying the effect of heating on the allergenicity of egg allergens.

Key words: thermal processing, egg white allergens, spectral analysis, structure

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