【作者】 齐鑫； 许朵霞； 朱金锦； 王少甲； 彭静维； 高伟； 曹雁平；

【Author】 Qi Xin;Xu Duoxia;Zhu Jinjin;Wang Shaojia;Peng Jingwei;Gao Wei;Cao Yanping;School of Food and Health,Beijing Technology & Business University(BTBU);Chenguang Biotech Group Co.,Ltd;

【机构】 北京工商大学食品与健康学院； 晨光生物科技基团股份有限公司；

【摘要】 叶黄素酯是一种天然色素,常作为着色剂用于食品加工中。但是,叶黄素酯分子中含有大量的共轭双键,这使得叶黄素酯在应用过程中容易损失。本研究探讨了卵清蛋白与叶黄素二棕榈酸酯的相互作用及卵清蛋白对万寿菊叶黄素酯提取物颜色稳定性的影响。叶黄素二棕榈酸酯通过静态猝灭方式猝灭了卵清蛋白的荧光。结合和热力学参数证明,叶黄素二棕榈酸酯通过范德华力和氢键与卵清蛋白自发结合,二者的化学计量比为1:1。通过三维荧光光谱、傅里叶变换红外光谱和圆二色谱实验,发现添加了叶黄素二棕榈酸酯后,卵清蛋白的构象展开,二级结构改变。透射电镜和粒径结果显示,卵白蛋白-叶黄素二棕榈酸酯体系中存在球形的纳米级聚集体,表明叶黄素二棕榈酸酯不仅可以在分子水平与卵清蛋白结合,而且还促进卵清蛋白的聚集。此外,添加卵清蛋白对万寿菊叶黄素酯提取物的稳定性有积极影响。更多还原

【Abstract】 Lutein esters are a kind of natural pigment,often used as a coloring agent in food processing.However,lutein esters molecules contain a large number of conjugated double bonds,which makes the lutein esters easy to lose during the application process.In this study,the interaction of ovalbumin with lutein dipalmitate and the effect of ovalbumin on marigold lutein esters extracts were investigated.Lutein dipalmitate quenched the fluorescence of ovalbumin by static quenching.Binding and thermodynamic parameters proved that lutein dipalmitate bound to ovalbumin spontaneously by van der Waals force and hydrogen bond,and the complex stoichiometry was 1:1.Through three-dimensional fluorescence spectroscopy,Fourier transform infrared spectroscopy and circular dichroism experiments,the conformation of ovalbumin was unfolded,and alteration in the ovalbumin secondary structure induced by lutein dipalmitate was observed.The results of transmission electron microscopy and particle size revealed that there were spherical and nano-sized aggregates in the ovalbumin-lutein dipalmitate system,indicating the lutein dipalmitate not only could bind to ovalbumin at molecular level,but also promote the aggregation of ovalbumin.Additionally,the addition of ovalbumin had a positive effect on the stability of marigold lutein esters extracts.更多还原