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卵白蛋白与绿原酸分子互作对蛋白结构及乳液稳定性的影响 被引量:3

Effect of Molecular Interaction between Ovalbumin and Chlorogenic Acid on Protein Structure and Emulsion Stability
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摘要 多酚和蛋白质是构成复杂食品体系的重要物质,利用多酚和蛋白质之间的分子互作,改变蛋白结构并提升乳液稳定性,已成为当前食品加工领域的研究热点。通过荧光光谱法、同步荧光光谱法、圆二色谱法、红外光谱法研究卵白蛋白(OVA)与绿原酸(CA)的相互作用,并利用OVA-CA复合物制备高稳定性乳液。结果表明:CA对OVA的内源荧光猝灭机理为静态猝灭,结合位点数为1,结合位点更接近于OVA分子中色氨酸残基的位置。二者结合的主要作用力是氢键和疏水相互作用。CA的加入会改变OVA的蛋白质二级结构,其中,随着CA浓度的增加,α-螺旋含量逐渐增加,β-折叠含量逐渐减小。通过比较不同浓度CA下OVA-CA乳液的粒径,选择OVA∶CA=1∶0.1(摩尔比)为最适比例,制备粒径为(755.13±140.29)nm的乳液。与OVA乳液相比,OVA-CA乳液在常温下保持7 d,乳液状态稳定,同时pH值和盐离子(0~0.125 mol/L)稳定性显著提高。研究结果将为改善蛋清蛋白功能特性,拓展其在食品加工中的应用领域提供参考。 Polyphenols and proteins are important material sources that constitute a complex food system. Molecular interactions between polyphenols and proteins would change the structure of proteins and improve emulsion stability. It has become a research hotspot in the current food processing field. In this experiment, the interaction between ovalbumin(OVA) and chlorogenic acid(CA) was studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, circular dichroism, and infrared spectroscopy. The OVA-CA complex was used to prepare high stable emulsion. The experimental results showed that OVA and CA were 1∶1 binding. The binding site is closer to the position of the tryptophan residue in the OVA molecule. The quenching mechanism of CA to OVA’s endogenous fluorescence was static quenching,and the main force of the combination was hydrophobic interaction. The addition of CA would change the protein secondary structure of OVA. Among of them, the content of α-helix increased, and the content of β-sheet gradually decreased with the increase of CA concentration. The ratio of CA and OVA was optimized according to the particle size of the emulsion. The results showed that the particle size was the smallest when the ratio of CA and OVA was 1 ∶0.1. The particle size was(755.13±140.29) nm. Compared with OVA emulsion, OVA-CA emulsion remains stable for 7-day at room temperature, while the pH value and salt ion(0-0.125 mol/L) stability of OVA-CA emulsion were significantly improved. This research will provide a theoretical basis for improving the functional properties of egg white protein and expand the application of egg white protein in food processing.
作者 温鹤迪 宁珍珍 李金铭 关玉 贺家华 赵颂宁 刘静波 张婷 Wen Hedi;Ning Zhenzhen;Li Jinming;Guan Yu;He Jiahua;Zhao Songning;Liu Jingbo;Zhang Ting(Jilin Provincial Key Laboratory of Nutrition and Functional Food,Changchun 130062;College of Food Science and Engineering,Jilin University,Changchun 130062)
出处 《中国食品学报》 EI CAS CSCD 北大核心 2022年第10期66-76,共11页 Journal of Chinese Institute Of Food Science and Technology
基金 吉林省科技发展计划技术攻关项目(20210402048GH) 中央高校基本业务费(JLUXKJC2021Q Z11)。
关键词 卵白蛋白 绿原酸 乳液 稳定性 分子互作 ovalbumin chlorogenic acid emulsion stability molecular interaction
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