Interaction Mechanism of Ovalbumin with Resveratrol and Its Effect on Ovalbumin

被引：1
作者：
Cao Q. [1 ,2 ]
Hu W. [2 ]
Gao J. [2 ]
Chen H. [1 ,3 ]
Tong P. [1 ]
机构：
[1] State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang
[2] School of Food Science and Technology, Nanchang University, Nanchang
[3] Sino-German Joint Research Institute, Nanchang University, Nanchang
来源：
Shipin Kexue/Food Science | 2021年 / 42卷 / 04期
关键词：
Circular dichroism spectroscopy; Fluorescence spectroscopy; Interaction; Ovalbumin; Potential allergenicity; Resveratrol;
D O I：
10.7506/spkx1002-6630-20190918-228
中图分类号：
学科分类号：
摘要：
The interaction mechanism of ovalbumin (OVA) with resveratrol (RES) was examined by analyzing the type of fluorescence quenching, binding site number, thermodynamic parameters and the content of secondary structures using fluorescence and circular dichroism (CD) spectroscopy. Furthermore, the effect of RES on the potential allergenicity of OVA was evaluated by enzyme-linked immunosorbent assay (ELISA) in vitro. Results showed that RES could quench the fluorescence of OVA dynamically. OVA-RES interaction was a spontaneous process (ΔH < 0, ΔS < 0, ΔG < 0) driven by hydrogen bond and van der Waals force. The microenvironment around amino acid residues in OVA and its conformation were changed by RES, thereby increasing the potential allergenicity of OVA. © 2021, China Food Publishing Company. All right reserved.
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页码：31 / 37
页数：6
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