ArticleFoods (Basel, Switzerland)2023
Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol-Protein Interaction Approach.
Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Preparation and Characterization of a Hypoglycemic Complex of Gallic Acid-Antarctic Krill Polypeptide Based on Polylactic Acid-Hydroxyacetic Acid (PLGA) and High-Pressure Microjet Microencapsulation.Foods (Basel, Switzerland) · 2024Article
- Effect of Microwave Vacuum Freeze-Drying Power on Emulsifying and Structure Properties of Egg White Protein.Foods (Basel, Switzerland) · 2023Article
- Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model.Foods (Basel, Switzerland) · 2023Article
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Authors and funding
6 authors.
Funding
Abstract
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
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