FOOD SCIENCE ›› 2021, Vol. 42 ›› Issue (4): 31-37.doi: 10.7506/spkx1002-6630-20190918-228

• Food Chemistry • Previous Articles     Next Articles

Interaction Mechanism of Ovalbumin with Resveratrol and Its Effect on Ovalbumin

CAO Qiang, HU Wei, GAO Jinyan, CHEN Hongbing, TONG Ping   

  1. (1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; 2. School of Food Science and Technology, Nanchang University, Nanchang 330047, China; 3. Sino-German Joint Research Institute, Nanchang University, Nanchang 330047, China)
  • Online:2021-02-25 Published:2021-02-25

Abstract: 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.

Key words: resveratrol; ovalbumin; fluorescence spectroscopy; circular dichroism spectroscopy; interaction; potential allergenicity

CLC Number: