研究报告

乳清蛋白与黄豆苷元/葛根素相互作用及复合物性质研究

  • 杨敏 ,
  • 王裕成 ,
  • 季伟 ,
  • 李茜
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  • (甘肃农业大学 理学院,甘肃 兰州,730070)
第一作者:博士,教授(通信作者,E-mail:yummy12@163.com)

收稿日期: 2022-06-13

  修回日期: 2022-06-28

  网络出版日期: 2023-08-07

基金资助

国家自然科学基金项目(32060549);甘肃农业大学伏羲杰出人才培育计划(Gaufx-02J02);甘肃省自然科学基金项目(21JR1RA207);兰州市科技计划项目(2021-1-147)

Interaction between daidzein or puerarin and whey protein and the characteristics of their complexes

  • YANG Min ,
  • WANG Yucheng ,
  • JI Wei ,
  • LI Qian
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  • (College of Science, Gansu Agricultural University, Lanzhou 730070, China)

Received date: 2022-06-13

  Revised date: 2022-06-28

  Online published: 2023-08-07

摘要

黄豆苷元和葛根素是天然多酚,具有多种生物活性,但其生物利用度低。该研究以乳清蛋白为载体,以黄豆苷元、葛根素为配体,采用荧光光谱法研究了二者相互作用;制备了乳清蛋白-黄豆苷元/葛根素复合物,采用傅里叶变换红外光谱、X射线衍射、扫描电镜等手段表征了复合物结构;分析了复合物的热稳定性和抗氧化性,并评价了复合物中黄豆苷元和葛根素的胃肠模拟释放性。结果表明,葛根素与乳清蛋白间的主要作用为氢键和范德华力,而黄豆苷元主要以疏水作用与乳清蛋白结合。与乳清蛋白结合后,黄豆苷元和葛根素的部分特征红外峰及X射线衍射峰消失,但喷干后复合物的微观形貌与乳清蛋白相似。与乳清蛋白结合后,黄豆苷元的DPPH自由基清除活性提高。模拟消化试验表明,与乳清蛋白结合减缓了黄豆苷元和葛根素的肠道释放率。研究结果可为黄豆苷元、葛根素以及乳清蛋白在功能食品中的应用提供参考依据。

本文引用格式

杨敏 , 王裕成 , 季伟 , 李茜 . 乳清蛋白与黄豆苷元/葛根素相互作用及复合物性质研究[J]. 食品与发酵工业, 2023 , 49(13) : 200 -208 . DOI: 10.13995/j.cnki.11-1802/ts.032653

Abstract

Daidzein and puerarin are natural polyphenols with multiple bioactivities, but their bioavailability is low. In this study, whey protein was chosen as the matrix and daidzein or puerarin was chosen as a ligand to prepare complexes. The interaction between daidzein/puerarin and whey protein was analyzed by using fluorescence spectroscopy. The structures of the complexes were characterized by Fourier transform infrared spectroscopy (FTIR), X-Ray diffraction (XRD), and scanning electron microscope (SEM). The thermal stability and antioxidant properties of the complexes were evaluated, as well as the release properties of daidzein or puerarin from the complexes during simulated gastrointestinal digestion. Results showed that the main interaction between puerarin and whey protein was hydrogen bonds and Van der Waals forces, but hydrophobic forced in daidzein-whey protein. After combining with whey protein, some of the FTIR and XRD typical peaks for daidzein and puerarin disappeared. However, the morphology of the daidzein/puerarin-whey protein complexes was similar to that of free whey protein. The DPPH radical scavenging activity of daidzein was enhanced by complexing with whey protein. In addition, the combination with whey protein inhibited the release of daidzein and puerarin during simulated intestinal digestion. The results could provide the basic references for the application of daidzein and puerarin in functional foods, as well as whey protein.

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