食品科学 ›› 2020, Vol. 41 ›› Issue (6): 16-24.doi: 10.7506/spkx1002-6630-20190124-307

• 食品化学 • 上一篇    下一篇

鸡蛋中卵白蛋白和溶菌酶相互作用对其结构和致敏性的影响

汪吴晶,佟平,陈红兵,高金燕   

  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:2020-03-25 发布日期:2020-03-23
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2018YFD0400300);国家自然科学基金地区科学基金项目(31660436)

Effects of Interaction on the Structure and Potential Allergenicity of Ovalbumin and Lysozyme

WANG Wujing, TONG Ping, CHEN Hongbing, GAO Jinyan   

  1. (1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China;2. College of Food Science and Technology, Nanchang University, Nanchang 330047, China;3. Sino-German Joint Research Institute, Nanchang University, Nanchang 330047, China)
  • Online:2020-03-25 Published:2020-03-23

摘要: 了解蛋白质在热处理中相互作用对结构和致敏性的影响,以蛋清中卵白蛋白和溶菌酶为对象,对其在不同温度下的相互作用情况进行研究,通过浊度、溶解度、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳对其物理性质进行分析,利用圆二色光谱、紫外光谱、荧光光谱方法对其空间结构进行表征,并通过竞争酶联免疫吸附测定的方法对蛋白质的潜在致敏性进行探究。结果表明,卵白蛋白-溶菌酶(ovalbumin-lysozyme,OVA-Lys)在60、65 ℃加热10 min后不会显著影响彼此的结构以及潜在致敏性,而在70 ℃,由于OVA三级结构的展开,Lys疏水基团的暴露,两者会通过二硫键相互作用而显著降低彼此的潜在致敏性。

关键词: 卵白蛋白, 溶菌酶, 相互作用, 结构, 致敏性

Abstract: To understand the effect of protein-protein interactions during heat treatment on the structure and allergenicity of ovalbumin (OVA) and lysozyme (Lys), the interaction between OVA and Lys in egg white at different temperatures was studied. The physical properties including turbidity, solubility and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile were analyzed. The spatial structure was characterized by circular dichroism spectroscopy, ultraviolet spectroscopy and fluorescence spectroscopy. Finally, the potential allergenicity of proteins was studied by competitive enzyme linked immunosorbent assay (ELISA). The results showed that OVA-Lys interaction during heating for 10 minutes at 60 and 65 ℃ did not significantly affect the structure and potential allergenicity of each other. However, when treated at 70 ℃, the tertiary structure of OVA was unfolded, and the hydrophobic groups of Lys were exposed outside. Thus, the interaction between OVA and Lys was formed through disulfide bonds and could significantly reduce the potential allergenicity of each other.

Key words: ovalbumin, lysozyme, interaction, structure, allergenicity

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