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Research Article | Open Access

Binding mechanism of Monascus pigment and ovalbumin: spectral analysis, molecular docking and molecular dynamics simulation

Pei Zhang1,2, Xinyuan Huang1,2, Chen Fu1,2, Yuanwen Gong1,2, Xun Huang1,2, Jin Zhang2, Xiefei Li1,2( ), Hongbo Song1( ), Qun Huang1,2( )
College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China
School of Public Health, Guizhou Province Engineering Research Center of Health Food Innovative Manufacturing, the Key Laboratory of Environmental Pollution Monitoring and Disease Control of Ministry of Education, Guizhou Medical University, Guiyang 550025, China
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Graphical Abstract

Abstract

The interaction amid Monascus pigment (MP) and ovalbumin (OVA) was studied using multispectral and computer simulations. The fluorescence results demonstrated that MP could effectively quench the fluorescence emission of OVA. According to Stern-Volmer and the double logarithmic equation, the quenching reaction of MP to OVA was static quenching, which was brought on by the combination of two molecules to shape a complex. At 298 K, the conjunction constant Ka of MP and OVA was 1.045 2 × 109 L/mol, and the count of conjunction sites n was 1.955 7. The thermodynamic constant of MP-OVA binding was counted according to Van’s Hoff equation, and the reaction belonged to the active process of reducing Gibbs free energy. The ultraviolet–visible (UV-Vis) absorption spectroscopy indicated an interaction between MP and OVA. The interaction force between MP and OVA and the steadiness of the conjunction were examined by using molecular docking and molecular dynamics simulation. The findings suggested that MP formed a complex with OVA via non-covalent binding, the formation and steadiness of the complex were promoted through hydrogen bonding, hydrophobic interaction, and Van der Waals force.

Keywords

Monascus pigmentovalbuminfluorescence spectroscopyultraviolet-visible (UV-Vis) absorption spectroscopymolecular dockingmolecular dynamics

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Food Science of Animal Products
Volume 1 Issue 4,
December 2023
Article number: 9240038
DOI: 10.26599/FSAP.2023.9240038
Cite this article:
Zhang P, Huang X, Fu C, et al. Binding mechanism of Monascus pigment and ovalbumin: spectral analysis, molecular docking and molecular dynamics simulation. Food Science of Animal Products, 2023, 1(4): 9240038. https://doi.org/10.26599/FSAP.2023.9240038

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Received: 28 September 2023
Accepted: 31 October 2023
Published: 02 January 2024
© Beijing Academy of Food Sciences 2023.

Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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