The nanomicelles consisting of lotus root amylopectin and quinoa protein: Construction and encapsulation for quercetin. (1st September 2022)
- Record Type:
- Journal Article
- Title:
- The nanomicelles consisting of lotus root amylopectin and quinoa protein: Construction and encapsulation for quercetin. (1st September 2022)
- Main Title:
- The nanomicelles consisting of lotus root amylopectin and quinoa protein: Construction and encapsulation for quercetin
- Authors:
- Liu, Kang
Zhang, Hai-Lin
Pan, Li-Hua
Li, Qiang-Ming
Luo, Jian-Ping
Zha, Xue-Qiang - Abstract:
- Highlights: LRA-coated Que-QP nanomicelles were constructed via self-assembly. Hydrophobic interaction and hydrogen bonding were the main driving forces. Que-QP-LRA nanomicelles exhibited a core-shell structure. The addition of LRA changed the secondary structure of QP. The composite nanomicelles enhanced stability and sustained release property of Que. Abstract: To improve the water solubility, stability and bioavailability of quercetin, the quercetin (Que)-quinoa protein (QP)-lotus root amylopectin (LRA) nanomicelles (Que-QP-LRA) were constructed via self-assembly in the present study. Results showed that a uniform and stable Que-QP-LRA nanomicelles was formed when the mass ratio of Que/QP/LRA was 2.5:6:24. Under this condition, the particle size, polydispersity index and zeta potential of the nanomicelles were 157.3 nm, 0.289 and −16.7 mV, respectively. Transmission electron microscopy exhibited that the Que-QP-LRA nanomicelles have a core-shell structure. The analysis of molecular interaction indicated that hydrogen bonding and hydrophobic interaction were the main driving forces to maintain stable structure of Que-QP-LRA nanomicelles. Additionally, the in vitro simulated digestion experiments suggested that Que-QP-LRA nanomicelles can enhance the stability of quercetin in the stomach and enable it to be sustained release in the intestine. These results suggested that Que-QP-LRA nanomicelles were beneficial for improving the bioavailability of quercetin.
- Is Part Of:
- Food chemistry. Volume 387(2022)
- Journal:
- Food chemistry
- Issue:
- Volume 387(2022)
- Issue Display:
- Volume 387, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 387
- Issue:
- 2022
- Issue Sort Value:
- 2022-0387-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-09-01
- Subjects:
- Quinoa protein -- Lotus root amylopectin -- Self-assembly -- Encapsulation -- Quercetin
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2022.132924 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
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- 21467.xml