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Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type

In this study, the effect of emulsifier type, i.e. whey protein versus Tween 80, on the digestion behaviour of emulsion gels containing capsaicinoids (CAPs) was examined. The results indicate that the CAP-loaded Tween 80 emulsion gel was emptied out significantly faster during gastric digestion than...

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Autores principales: Luo, Nan, Ye, Aiqian, Wolber, Frances M., Singh, Harjinder
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9993031/
https://www.ncbi.nlm.nih.gov/pubmed/36910917
http://dx.doi.org/10.1016/j.crfs.2023.100473
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author Luo, Nan
Ye, Aiqian
Wolber, Frances M.
Singh, Harjinder
author_facet Luo, Nan
Ye, Aiqian
Wolber, Frances M.
Singh, Harjinder
author_sort Luo, Nan
collection PubMed
description In this study, the effect of emulsifier type, i.e. whey protein versus Tween 80, on the digestion behaviour of emulsion gels containing capsaicinoids (CAPs) was examined. The results indicate that the CAP-loaded Tween 80 emulsion gel was emptied out significantly faster during gastric digestion than the CAP-loaded whey protein emulsion gel. The Tween-80-coated oil droplets appeared to be in a flocculated state in the emulsion gel, had no interactions with the protein matrix and were easily released from the protein matrix during gastric digestion. The whey-protein-coated oil droplets showed strong interactions with the protein matrix, and the presence of thick protein layer around the oil droplets protected their liberation during gastric digestion. During intestinal digestion, the CAP-loaded Tween 80 emulsion gel had a lower extent of lipolysis than the CAP-loaded whey protein emulsion gel, probably because the interfacial layer formed by Tween 80 was resistance to displacement by bile salts, and/or because Tween 80 formed interfacial complexes with bile salts/lipolytic enzymes. Because of the softer structure of the CAP-loaded Tween 80 emulsion gel, the gel particles were broken down much faster and the oil droplets were liberated from the protein matrix more readily than for the CAP-loaded whey protein emulsion gel during intestinal digestion; this promoted the release of CAP molecules from the gel. In addition, the Tween 80 molecules displaced from the interface would participate in the formation of mixed micelles and would help to solubilize the released CAP molecules, leading to improved bioaccessibility of CAP. Information obtained from this study could be useful in designing functional foods for the delivery of lipophilic bioactive compounds.
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spelling pubmed-99930312023-03-09 Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type Luo, Nan Ye, Aiqian Wolber, Frances M. Singh, Harjinder Curr Res Food Sci Research Article In this study, the effect of emulsifier type, i.e. whey protein versus Tween 80, on the digestion behaviour of emulsion gels containing capsaicinoids (CAPs) was examined. The results indicate that the CAP-loaded Tween 80 emulsion gel was emptied out significantly faster during gastric digestion than the CAP-loaded whey protein emulsion gel. The Tween-80-coated oil droplets appeared to be in a flocculated state in the emulsion gel, had no interactions with the protein matrix and were easily released from the protein matrix during gastric digestion. The whey-protein-coated oil droplets showed strong interactions with the protein matrix, and the presence of thick protein layer around the oil droplets protected their liberation during gastric digestion. During intestinal digestion, the CAP-loaded Tween 80 emulsion gel had a lower extent of lipolysis than the CAP-loaded whey protein emulsion gel, probably because the interfacial layer formed by Tween 80 was resistance to displacement by bile salts, and/or because Tween 80 formed interfacial complexes with bile salts/lipolytic enzymes. Because of the softer structure of the CAP-loaded Tween 80 emulsion gel, the gel particles were broken down much faster and the oil droplets were liberated from the protein matrix more readily than for the CAP-loaded whey protein emulsion gel during intestinal digestion; this promoted the release of CAP molecules from the gel. In addition, the Tween 80 molecules displaced from the interface would participate in the formation of mixed micelles and would help to solubilize the released CAP molecules, leading to improved bioaccessibility of CAP. Information obtained from this study could be useful in designing functional foods for the delivery of lipophilic bioactive compounds. Elsevier 2023-03-02 /pmc/articles/PMC9993031/ /pubmed/36910917 http://dx.doi.org/10.1016/j.crfs.2023.100473 Text en © 2023 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Luo, Nan
Ye, Aiqian
Wolber, Frances M.
Singh, Harjinder
Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type
title Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type
title_full Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type
title_fullStr Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type
title_full_unstemmed Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type
title_short Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type
title_sort digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: effect of emulsifier type
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9993031/
https://www.ncbi.nlm.nih.gov/pubmed/36910917
http://dx.doi.org/10.1016/j.crfs.2023.100473
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