分析与检测

基于重组虾铁蛋白装载山奈酚的三种不同方法的比较分析

  • 李蝶 ,
  • 张斌 ,
  • 申淼淼 ,
  • 袁欣 ,
  • 侯原菲 ,
  • 李树红 ,
  • 李冉 ,
  • 张志清 ,
  • 李美良
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  • (四川农业大学 食品学院,四川 雅安,625000)
第一作者:硕士研究生(李美良副教授为通信作者,E-mail:liml@sicau.edu.cn)

收稿日期: 2022-12-17

  修回日期: 2023-02-07

  网络出版日期: 2024-01-17

基金资助

大学生创新训练计划(202210626007);大学生科研兴趣项目(2023021);雅安市区校合作项目(2222239002);四川省科技厅项目(2020YFN0108)

Comparative analysis of three different loading methods of kaempferol based on recombinant marsupenaeus japonicus ferritin

  • LI Die ,
  • ZHANG Bin ,
  • SHEN Miaomiao ,
  • YUAN Xin ,
  • HOU Yuanfei ,
  • LI Shuhong ,
  • LI Ran ,
  • ZHANG Zhiqing ,
  • LI Meiliang
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  • (College of Food Science, Sichuan Agricultural University, Ya′an 625000, China)

Received date: 2022-12-17

  Revised date: 2023-02-07

  Online published: 2024-01-17

摘要

该研究以分离纯化后的虾重组铁蛋白和山奈酚为原料,采用超声辅助法、尿素诱导法以及pH调控法3种不同装载方法制备重组虾铁蛋白-山奈酚复合物。对比3种复合物的蛋白分子质量、装载率、粒径、电势以及二级结构。电泳结果显示3种不同装载方法对铁蛋白分子质量都不产生影响;3种复合物的装载率分别达到了20%、18.5%、16.7%;电镜图以及粒径分布图显示超声辅助法可抑制铁蛋白聚集;傅里叶红外光谱结果表明pH调控法制备的复合物对铁蛋白的二级结构有一定的影响。超声处理制备铁蛋白与活性物质的复合物具有较高装载率、蛋白质分散性良好、不破坏铁蛋白二级结构的优点,该成果对铁蛋白装载活性小分子物质具有重要意义。

本文引用格式

李蝶 , 张斌 , 申淼淼 , 袁欣 , 侯原菲 , 李树红 , 李冉 , 张志清 , 李美良 . 基于重组虾铁蛋白装载山奈酚的三种不同方法的比较分析[J]. 食品与发酵工业, 2023 , 49(24) : 251 -258 . DOI: 10.13995/j.cnki.11-1802/ts.034651

Abstract

Ferritin is a kind of good nano-carrier, which can be used to load kaempferol with poor water solubility, but the self-assembly of ferritin in the extreme environment will cause the destruction of the secondary structure. The recombinant marsupenaeus japonicus ferritin and kaempferol were used as raw materials. The complex of ferritin and kaempferol was prepared by ultrasonic-assisted loading method, urea induction method, and pH regulation method. The molecular weight, loading rate, particle size, electric potential, and secondary structure of the three complexes were compared. The electrophoretic results showed that the molecular weight of ferritin was not affected by the three loading methods. The loading rates of the three compounds reached 20%, 18.5%, and 16.7% respectively. Transmission electron microscopy and particle size distribution showed that ferritin aggregation could be inhibited by the ultrasonic-assisted method. The results of Fourier infrared spectroscopy showed that the complex prepared by pH regulation had a certain effect on the secondary structure of ferritin. The complex of ferritin and active substance prepared by ultrasonic treatment had the advantages of a high loading rate, good protein dispersion, and no damage to the secondary structure of ferritin. The results are of great significance for the ferritin loading of active small molecules.

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