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Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems
The incorporation of hydrophobic ingredients, such as resveratrol (a fat-soluble phytochemical), in nanoemulsions can increase the water solubility and stability of these hydrophobic ingredients. The nanodelivery of resveratrol can result in a marked improvement in the bioavailability of this health...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7601424/ https://www.ncbi.nlm.nih.gov/pubmed/33023075 http://dx.doi.org/10.3390/foods9101394 |
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author | Mora-Gutierrez, Adela Attaie, Rahmat Núñez de González, Maryuri T. Jung, Yoonsung Marquez, Sixto A. |
author_facet | Mora-Gutierrez, Adela Attaie, Rahmat Núñez de González, Maryuri T. Jung, Yoonsung Marquez, Sixto A. |
author_sort | Mora-Gutierrez, Adela |
collection | PubMed |
description | The incorporation of hydrophobic ingredients, such as resveratrol (a fat-soluble phytochemical), in nanoemulsions can increase the water solubility and stability of these hydrophobic ingredients. The nanodelivery of resveratrol can result in a marked improvement in the bioavailability of this health-promoting ingredient. The current study hypothesized that resveratrol can bind to caprine casein, which may result in the preservation of the biological properties of resveratrol. The fluorescence spectra provided proof of this complex formation by demonstrating that resveratrol binds to caprine casein in the vicinity of tryptophan amino acid residues. The caprine casein/resveratrol complex is stabilized by hydrophobic interactions and hydrogen bonds. Hence, to study the rate of resveratrol degradation during processing/storage, resveratrol losses were determined by reversed-phase high performance liquid chromatography (RP-HPLC) in nanoemulsions stabilized by bovine and caprine caseins individually and in combination with polysorbate-20. At 48 h oxidation, 88.33% and 89.08% was left of resveratrol in the nanoemulsions stabilized by caprine casein (α(s1)-I)/polysorbate-20 complex and caprine (α(s1)-II)/polysorbate-20 complex, while there was less resveratrol left in the nanoemulsions stabilized by bovine casein/polysorbate-20 complex, suggesting that oxygen degradation was involved. The findings of this study are crucial for the food industry since they imply the potential use of caprine casein/polysorbate-20 complex to preserve the biological properties of resveratrol. |
format | Online Article Text |
id | pubmed-7601424 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76014242020-11-01 Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems Mora-Gutierrez, Adela Attaie, Rahmat Núñez de González, Maryuri T. Jung, Yoonsung Marquez, Sixto A. Foods Article The incorporation of hydrophobic ingredients, such as resveratrol (a fat-soluble phytochemical), in nanoemulsions can increase the water solubility and stability of these hydrophobic ingredients. The nanodelivery of resveratrol can result in a marked improvement in the bioavailability of this health-promoting ingredient. The current study hypothesized that resveratrol can bind to caprine casein, which may result in the preservation of the biological properties of resveratrol. The fluorescence spectra provided proof of this complex formation by demonstrating that resveratrol binds to caprine casein in the vicinity of tryptophan amino acid residues. The caprine casein/resveratrol complex is stabilized by hydrophobic interactions and hydrogen bonds. Hence, to study the rate of resveratrol degradation during processing/storage, resveratrol losses were determined by reversed-phase high performance liquid chromatography (RP-HPLC) in nanoemulsions stabilized by bovine and caprine caseins individually and in combination with polysorbate-20. At 48 h oxidation, 88.33% and 89.08% was left of resveratrol in the nanoemulsions stabilized by caprine casein (α(s1)-I)/polysorbate-20 complex and caprine (α(s1)-II)/polysorbate-20 complex, while there was less resveratrol left in the nanoemulsions stabilized by bovine casein/polysorbate-20 complex, suggesting that oxygen degradation was involved. The findings of this study are crucial for the food industry since they imply the potential use of caprine casein/polysorbate-20 complex to preserve the biological properties of resveratrol. MDPI 2020-10-02 /pmc/articles/PMC7601424/ /pubmed/33023075 http://dx.doi.org/10.3390/foods9101394 Text en © 2020 by the authors. 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/). |
spellingShingle | Article Mora-Gutierrez, Adela Attaie, Rahmat Núñez de González, Maryuri T. Jung, Yoonsung Marquez, Sixto A. Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems |
title | Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems |
title_full | Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems |
title_fullStr | Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems |
title_full_unstemmed | Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems |
title_short | Interface Compositions as Determinants of Resveratrol Stability in Nanoemulsion Delivery Systems |
title_sort | interface compositions as determinants of resveratrol stability in nanoemulsion delivery systems |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7601424/ https://www.ncbi.nlm.nih.gov/pubmed/33023075 http://dx.doi.org/10.3390/foods9101394 |
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