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Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach
The preparation of the interaction between polyphenols and protein is of great significance for increasing added value and promoting the application of egg yolk immunoglobulin (IgY). This study systematically investigated the effect of catechin on yolk immunoglobulin structural characteristics and f...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9914673/ https://www.ncbi.nlm.nih.gov/pubmed/36765991 http://dx.doi.org/10.3390/foods12030462 |
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author | Liu, Lili Zhang, Xiaodan Zhang, Mapinyi Zhang, Mengjun Cheng, Weiwei Xu, Baocheng |
author_facet | Liu, Lili Zhang, Xiaodan Zhang, Mapinyi Zhang, Mengjun Cheng, Weiwei Xu, Baocheng |
author_sort | Liu, Lili |
collection | PubMed |
description | The preparation of the interaction between polyphenols and protein is of great significance for increasing added value and promoting the application of egg yolk immunoglobulin (IgY). This study systematically investigated the effect of catechin on yolk immunoglobulin structural characteristics and functional properties. The binding conditions, force types, molecular conformation, and residual microenvironment of the interaction between catechin and IgY were analyzed by molecular docking technology, UV-vis absorption and fluorescence spectroscopy studies. The results showed that the main binding forces in the complex were hydrogen bonding and van der Waals forces. After the interaction, fluorescence quenching occurred and the maximum emission wavelength was redshifted. The results showed that the microenvironment around IgY increased polarity, increased hydrophilicity and decreased hydrophobicity, and the structure of the peptide chain changed. The bacteriostatic thermal stability of the compound against Escherichia coli and Staphylococcus aureus was lower than that of catechin IgY. The bacteriostatic acid and base stability were higher than that of catechin and IgY. The antioxidant activity was catechin, complex, and IgY, in descending order. The antioxidant activity of catechin and complex was significantly higher than that of IgY. At the same concentration, the apparent viscosity of the three samples was complex, IgY and catechin, in descending order. G’ was greater than G” indicating that elastic properties dominate in G”. The G’ and G” values of the complex were higher than those of the other groups. Rheological results indicated that the complex may have high physical stability. This study provides theoretical support for broadening the application field of IgY and suggest its properties change in the machining process. It also provides new ideas for the development of functional foods from poultry eggs. |
format | Online Article Text |
id | pubmed-9914673 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-99146732023-02-11 Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach Liu, Lili Zhang, Xiaodan Zhang, Mapinyi Zhang, Mengjun Cheng, Weiwei Xu, Baocheng Foods Article The preparation of the interaction between polyphenols and protein is of great significance for increasing added value and promoting the application of egg yolk immunoglobulin (IgY). This study systematically investigated the effect of catechin on yolk immunoglobulin structural characteristics and functional properties. The binding conditions, force types, molecular conformation, and residual microenvironment of the interaction between catechin and IgY were analyzed by molecular docking technology, UV-vis absorption and fluorescence spectroscopy studies. The results showed that the main binding forces in the complex were hydrogen bonding and van der Waals forces. After the interaction, fluorescence quenching occurred and the maximum emission wavelength was redshifted. The results showed that the microenvironment around IgY increased polarity, increased hydrophilicity and decreased hydrophobicity, and the structure of the peptide chain changed. The bacteriostatic thermal stability of the compound against Escherichia coli and Staphylococcus aureus was lower than that of catechin IgY. The bacteriostatic acid and base stability were higher than that of catechin and IgY. The antioxidant activity was catechin, complex, and IgY, in descending order. The antioxidant activity of catechin and complex was significantly higher than that of IgY. At the same concentration, the apparent viscosity of the three samples was complex, IgY and catechin, in descending order. G’ was greater than G” indicating that elastic properties dominate in G”. The G’ and G” values of the complex were higher than those of the other groups. Rheological results indicated that the complex may have high physical stability. This study provides theoretical support for broadening the application field of IgY and suggest its properties change in the machining process. It also provides new ideas for the development of functional foods from poultry eggs. MDPI 2023-01-19 /pmc/articles/PMC9914673/ /pubmed/36765991 http://dx.doi.org/10.3390/foods12030462 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Liu, Lili Zhang, Xiaodan Zhang, Mapinyi Zhang, Mengjun Cheng, Weiwei Xu, Baocheng Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach |
title | Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach |
title_full | Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach |
title_fullStr | Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach |
title_full_unstemmed | Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach |
title_short | Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach |
title_sort | effect of catechin on yolk immunoglobulin structure and properties: a polyphenol–protein interaction approach |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9914673/ https://www.ncbi.nlm.nih.gov/pubmed/36765991 http://dx.doi.org/10.3390/foods12030462 |
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