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Wheat gliadin hydrolysates based nano-micelles for hydrophobic naringin: Structure characterization, interaction, and in vivo digestion
•Limited enzymatic hydrolysis improved the structure of WG.•WGH-9 exhibited better binding affinity with naringin and stable structure.•The micelles showed excellent storage and photothermal stability.•The micelles significantly enhanced the bioavailability of naringin. In this study, enzymatic hydr...
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Published in: | Food Chemistry: X 2024-03, Vol.21, p.101136, Article 101136 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | •Limited enzymatic hydrolysis improved the structure of WG.•WGH-9 exhibited better binding affinity with naringin and stable structure.•The micelles showed excellent storage and photothermal stability.•The micelles significantly enhanced the bioavailability of naringin.
In this study, enzymatic hydrolysis was used to fabricate wheat gliadin hydrolysates (WGHs) for the encapsulation and protection of naringin. The exposure of hydrophilic amino acids decreased the critical micelle concentration (from 0.53 ± 0.02 mg/mL to 0.35 ± 0.03 mg/mL) and improved solubility, which provided amphiphilic conditions for the delivery of naringin. The hydrolysates with a degree of hydrolysis (DH) of 9 % had the strongest binding affinity with naringin, and exhibited the smallest particle size (113.7 ± 1.1 nm) and the highest encapsulation rate (83.2 ± 1.3 %). The storage, heat and photochemical stability of naringin were improved via the encapsulation of micelles. Furthermore, the micelles made up of hydrolysates with a DH of 12 % significantly enhanced the bioavailability of naringin (from 19.4 ± 4.3 % to 46.8 ± 1.4 %). Our experiment provides theoretical support for the utilization of delivery systems based on water-insoluble proteins. |
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ISSN: | 2590-1575 2590-1575 |
DOI: | 10.1016/j.fochx.2024.101136 |