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Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products
The impact of typical primary or secondary lipid oxidation (LPO) products, selected as linoleic acid 13-hydroperoxide (13-HPODE) and malondialdehyde (MDA), on the structural modification of unadsorbed or adsorbed proteins in whey protein isolate (WPI)-stabilized oil-in-water (O/W) emulsions during s...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7999650/ https://www.ncbi.nlm.nih.gov/pubmed/33799885 http://dx.doi.org/10.3390/foods10030593 |
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author | Chen, Jiaxin Zhao, Jinhai Kong, Baohua Chen, Qian Liu, Qian Liu, Chengguo |
author_facet | Chen, Jiaxin Zhao, Jinhai Kong, Baohua Chen, Qian Liu, Qian Liu, Chengguo |
author_sort | Chen, Jiaxin |
collection | PubMed |
description | The impact of typical primary or secondary lipid oxidation (LPO) products, selected as linoleic acid 13-hydroperoxide (13-HPODE) and malondialdehyde (MDA), on the structural modification of unadsorbed or adsorbed proteins in whey protein isolate (WPI)-stabilized oil-in-water (O/W) emulsions during storage up to 48 h at 37 °C in the dark was investigated. The results showed that either 13-HPODE and MDA could lead to structural modifications of unadsorbed or adsorbed proteins with a concentration-dependent manner and time relationship, respectively. Moreover, higher levels of MDA rendered a higher degree of oxidative modifications of WPI than 13-HPODE, indicated by the higher protein carbonyl contents and N’-formyl-L-kynurenine (NFK) and lower fluorescence intensity. Additionally, adsorbed proteins were more easily oxidized by LPO products than unadsorbed proteins. Overall, our results indicated that the formation of secondary LPO products and the protein position were crucial factors to increase the degree of oxidative modifications of WPI in O/W emulsion systems. |
format | Online Article Text |
id | pubmed-7999650 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79996502021-03-28 Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products Chen, Jiaxin Zhao, Jinhai Kong, Baohua Chen, Qian Liu, Qian Liu, Chengguo Foods Article The impact of typical primary or secondary lipid oxidation (LPO) products, selected as linoleic acid 13-hydroperoxide (13-HPODE) and malondialdehyde (MDA), on the structural modification of unadsorbed or adsorbed proteins in whey protein isolate (WPI)-stabilized oil-in-water (O/W) emulsions during storage up to 48 h at 37 °C in the dark was investigated. The results showed that either 13-HPODE and MDA could lead to structural modifications of unadsorbed or adsorbed proteins with a concentration-dependent manner and time relationship, respectively. Moreover, higher levels of MDA rendered a higher degree of oxidative modifications of WPI than 13-HPODE, indicated by the higher protein carbonyl contents and N’-formyl-L-kynurenine (NFK) and lower fluorescence intensity. Additionally, adsorbed proteins were more easily oxidized by LPO products than unadsorbed proteins. Overall, our results indicated that the formation of secondary LPO products and the protein position were crucial factors to increase the degree of oxidative modifications of WPI in O/W emulsion systems. MDPI 2021-03-11 /pmc/articles/PMC7999650/ /pubmed/33799885 http://dx.doi.org/10.3390/foods10030593 Text en © 2021 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 (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Article Chen, Jiaxin Zhao, Jinhai Kong, Baohua Chen, Qian Liu, Qian Liu, Chengguo Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products |
title | Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products |
title_full | Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products |
title_fullStr | Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products |
title_full_unstemmed | Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products |
title_short | Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products |
title_sort | comparative study of oxidative structural modifications of unadsorbed and adsorbed proteins in whey protein isolate-stabilized oil-in-water emulsions under the stress of primary and secondary lipid oxidation products |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7999650/ https://www.ncbi.nlm.nih.gov/pubmed/33799885 http://dx.doi.org/10.3390/foods10030593 |
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