Exploring the interaction mechanism of dietary protein ovalbumin and folic acid: A combination research of molecular simulation technology and multispectroscopy

被引:26
|
作者
Cen, Congnan [1 ]
Chen, Jian [1 ]
Wang, Weiqiang [2 ]
Zhang, Jie [3 ]
Yang, Xiangying [3 ]
Fu, Linglin [1 ]
Wang, Yanbo [1 ]
机构
[1] Zhejiang Gongshang Univ, Sch Food Sci & Biotechnol, Food Safety Key Lab Zhejiang Prov, Hangzhou 310018, Peoples R China
[2] Jinhua Jinnian Ham Co Ltd, Jinhua 321041, Zhejiang, Peoples R China
[3] Sci & Technol Res Ctr China Customs, Food Safety Inst, Beijing 100026, Peoples R China
基金
国家重点研发计划; 中国国家自然科学基金;
关键词
Ovalbumin; Folic acid; Fluorescence spectroscopy; Interaction mechanism; Molecular simulation; HUMAN SERUM-ALBUMIN; CURCUMIN; PHOTODEGRADATION; COMPLEXES; EFFICIENT; DYNAMICS; BINDING;
D O I
10.1016/j.foodchem.2022.132536
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
This study aims to reveal the mechanism of the interaction between folic acid (FA) and egg ovalbumin (OVA) through the method of multi-spectroscopic, molecular docking, and molecular dynamics simulation in order to probe OVA as the possibility of a carrier of unstable vitamins. The results of the fluorescence spectra indicated a static quenching in the OVA-FA with a strong affinity of 6.998 x 10(4) M-1. At the same time, the complex formed by FA and OVA has changed the microenvironment. The measurement results of circular dichroism and particle size showed that FA and OVA gradually formed larger particles without changed the secondary structure of the protein. In addition, the results of molecular simulations indicated that the interaction between OVA and FA is mainly stabilized by strong hydrophobic and hydrogen bonds. This research was expanded the application prospect of dietary protein OVA as a transportation and protection system of vitamin substances.
引用
收藏
页数:8
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