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. |
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| 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] |
| Copyright of Food Research International is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 178149273 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Changes of structure properties and potential allergenicity of ovalbumin under high hydrostatic pressures. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Yang%2C+Jing%22">Yang, Jing</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> jyang@ctbu.edu.cn</i><br /><searchLink fieldCode="AR" term="%22Kuang%2C+Hong%22">Kuang, Hong</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kumar%2C+Nandan%22">Kumar, Nandan</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Song%2C+Jiajia%22">Song, Jiajia</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Li%2C+Yonghui%22">Li, Yonghui</searchLink><relatesTo>1,3</relatesTo> (AUTHOR)<i> yonghui@ksu.edu</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Food+Research+International%22">Food Research International</searchLink>. Aug2024, Vol. 190, pN.PAG-N.PAG. 1p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Sulfhydryl+group%22">Sulfhydryl group</searchLink><br /><searchLink fieldCode="DE" term="%22Free+groups%22">Free groups</searchLink><br /><searchLink fieldCode="DE" term="%22Circular+dichroism%22">Circular dichroism</searchLink><br /><searchLink fieldCode="DE" term="%22Zeta+potential%22">Zeta potential</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+structure%22">Molecular structure</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrostatic+pressure%22">Hydrostatic pressure</searchLink><br /><searchLink fieldCode="DE" term="%22Dichroism%22">Dichroism</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: [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] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Food Research International is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.foodres.2024.114658 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 1 StartPage: N.PAG Subjects: – SubjectFull: Sulfhydryl group Type: general – SubjectFull: Free groups Type: general – SubjectFull: Circular dichroism Type: general – SubjectFull: Zeta potential Type: general – SubjectFull: Molecular structure Type: general – SubjectFull: Hydrostatic pressure Type: general – SubjectFull: Dichroism Type: general Titles: – TitleFull: Changes of structure properties and potential allergenicity of ovalbumin under high hydrostatic pressures. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Yang, Jing – PersonEntity: Name: NameFull: Kuang, Hong – PersonEntity: Name: NameFull: Kumar, Nandan – PersonEntity: Name: NameFull: Song, Jiajia – PersonEntity: Name: NameFull: Li, Yonghui IsPartOfRelationships: – BibEntity: Dates: – D: 15 M: 08 Text: Aug2024 Type: published Y: 2024 Identifiers: – Type: issn-print Value: 09639969 Numbering: – Type: volume Value: 190 Titles: – TitleFull: Food Research International Type: main |
| ResultId | 1 |
