Release profile of amino acids encapsulated in solid lipid particles during in vitro oro-gastrointestinal digestion.


Journal

Food research international (Ottawa, Ont.)
ISSN: 1873-7145
Titre abrégé: Food Res Int
Pays: Canada
ID NLM: 9210143

Informations de publication

Date de publication:
Aug 2024
Historique:
received: 02 02 2024
revised: 04 06 2024
accepted: 04 06 2024
medline: 1 7 2024
pubmed: 1 7 2024
entrez: 30 6 2024
Statut: ppublish

Résumé

Some amino acids are known to mediate immune responses through gut microbiota metabolism in both humans and monogastric animals. However, through the diet, most free amino acids are absorbed in the small intestine and only a small quantity reaches the microbiota-rich colon. To enhance microbial metabolism of amino acids and their potential health benefits, encapsulation strategies are developed for their protection and delivery to the colon. So far, the main encapsulation systems for amino acids are based on solid lipid particles, but their fate within the digestive tract has never been fully clarified. In this study, we investigated the release of various amino acids (branched-chain amino acid mixture, or lysine, or tryptophan) loaded in solid lipid particles during in vitro oro-gastrointestinal digestion mimicking the piglet. The loaded solid lipid particles were fully characterized for their composition, thermal behavior, molecular structure, crystalline state, surface morphology, and particle size distribution. Moreover, we investigated the effect of particle size by sieving solid lipid particles into two non-overlapping size fractions. We found that amino acid release was high during the gastric phase of digestion, mainly controlled by physical parameters, namely particle size and crystalline state including surface morphology. Large particle size and/or smooth ordered particle indeed led to slower and lower release. Although lipid hydrolysis was significant during the intestinal phase of digestion, the impact of the crystalline state and surface morphology was also observed in the absence of enzymes, pointing to a dominant water/solute diffusion mechanism through these porous solid lipid particles.

Identifiants

pubmed: 38945573
pii: S0963-9969(24)00675-6
doi: 10.1016/j.foodres.2024.114605
pii:
doi:

Substances chimiques

Lipids 0
Amino Acids 0
Lysine K3Z4F929H6
Amino Acids, Branched-Chain 0
Tryptophan 8DUH1N11BX

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

114605

Informations de copyright

Copyright © 2024. Published by Elsevier Ltd.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Sharmitha Rajendrakumar (S)

INRAE, BIA, F-44316 Nantes, France.

Valérie Beaumal (V)

INRAE, BIA, F-44316 Nantes, France.

Alice Kermarrec (A)

INRAE, BIA, F-44316 Nantes, France.

Christelle Lopez (C)

INRAE, BIA, F-44316 Nantes, France.

Bruno Novales (B)

INRAE, BIA, F-44316 Nantes, France.

Hanitra Rabesona (H)

INRAE, BIA, F-44316 Nantes, France.

Aude Simongiovanni (A)

METEX ANIMAL NUTRITION, 32 rue Guersant, 75017 Paris, France.

Tristan Chalvon Demersay (TC)

METEX ANIMAL NUTRITION, 32 rue Guersant, 75017 Paris, France.

Sébastien Marze (S)

INRAE, BIA, F-44316 Nantes, France. Electronic address: sebastien.marze@inrae.fr.

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Classifications MeSH