1. Changes of structure properties and potential allergenicity of ovalbumin under high hydrostatic pressures.
- Author
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Yang J, Kuang H, Kumar N, Song J, and Li Y
- Subjects
- Molecular Dynamics Simulation, Circular Dichroism, Spectrometry, Fluorescence, Animals, Egg Hypersensitivity immunology, Food Hypersensitivity immunology, Humans, Food Handling methods, Protein Conformation, Ovalbumin immunology, Ovalbumin chemistry, Hydrostatic Pressure, Allergens chemistry, Allergens immunology
- Abstract
Egg proteins, notably ovalbumin (OVA), contribute to a prevalent form of food allergy, particularly in children. This study aims to investigate the impact of high hydrostatic pressure (HHP) treatment at varying levels (300, 400, 500, and 600 MPa) on the molecular structure and allergenicity of OVA. The structure of HHP-treated OVA was assessed through fluorescence spectroscopy, circular dichroism spectroscopy, and molecular dynamics (MD) simulation. HHP treatment (600 MPa) altered OVA structures, such as α-helix content decreased from 28.07 % to 19.47 %, and exogenous fluorescence intensity increased by 8.8 times compared to that of the native OVA. The free sulfhydryl groups and zeta potential value were also increased with HHP treatment (600 MPa). ELISA analysis and MD simulation unveiled a noteworthy reduction in the allergenicity of OVA when subjected to 600 MPa for 10 min. Overall, this study suggests that the conformational changes in HHP-treated OVA contribute to its altered allergenicity., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)
- Published
- 2024
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