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Changes of structure properties and potential allergenicity of ovalbumin under high hydrostatic pressures.

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Title: Changes of structure properties and potential allergenicity of ovalbumin under high hydrostatic pressures.
Authors: Yang, Jing1,2 (AUTHOR) jyang@ctbu.edu.cn, Kuang, Hong1 (AUTHOR), Kumar, Nandan3 (AUTHOR), Song, Jiajia4 (AUTHOR), Li, Yonghui1,3 (AUTHOR) yonghui@ksu.edu
Source: Food Research International. Aug2024, Vol. 190, pN.PAG-N.PAG. 1p.
Subjects: Sulfhydryl group, Free groups, Circular dichroism, Zeta potential, Molecular structure, Hydrostatic pressure, Dichroism
Abstract: [Display omitted] • HHP caused OVA fragmentation and unfolding. • HHP induced the secondary and tertiary structural changes of OVA. • The allergenicity of OVA decreased by 24.13 % at 600 MPa. • HHP induced potential epitope alterations of OVA. 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. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
Description
Abstract:[Display omitted] • HHP caused OVA fragmentation and unfolding. • HHP induced the secondary and tertiary structural changes of OVA. • The allergenicity of OVA decreased by 24.13 % at 600 MPa. • HHP induced potential epitope alterations of OVA. 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. [ABSTRACT FROM AUTHOR]
ISSN:09639969
DOI:10.1016/j.foodres.2024.114658