Fabrication of curcumin-loaded pea protein-pectin ternary complex for the stabilization and delivery of β‑carotene emulsions

Jiang, Yi; Hu, Haitao; Liu, Yuexiang; Lü, Yujuan; Fan, Yuting; Zhang, Yuzhu

doi:10.1016/j.foodchem.2019.126118

Cited by 74 publications

(13 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although S‐C emulsion contained the larger particles compared with S emulsion, but the S‐C emulsion did not cream rapidly at high salt concentration due to the formation of a three‐dimensional network of aggregated droplets to inhibit their movement (McClements, 2015; Liu et al ., 2017). On the contrary, β‐glucan could markedly increase the emulsion stability due to the weakening of the electrostatic screening effect and enhancement of the viscosity (Yi et al ., 2020). Moreover, no significant change in the mean droplet size of the S‐G‐C emulsion with different NaCl concentration was observed, indicating that the S‐G‐C emulsion were stable to flocculation and coalescence in the presence of salt, which may have been due to the strong steric repulsion and three‐dimensional network between the droplets (Liu et al ., 2016; Yi et al ., 2020).…”

Section: Resultsmentioning

confidence: 99%

“…Compared with S‐C, Z‐ average diameter of S‐G‐C decreased, which was in line with previous reports (Chen et al ., 2020). Interestingly, CM and SW treatment did not obviously change the particle size of S‐G, which was contrary to the previous report (Yi et al ., 2020). This discrepancy was ascribed to non‐covalent bonding between SPI and CM.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Investigation of physical stability of Pickering emulsion based on soy protein/β‐glucan/coumarin ternary complexes under subcritical water condition

Liang

et al. 2021

Int J of Food Sci Tech

View full text Add to dashboard Cite

The binding of proteins and polysaccharides/polyphenols can modify the interfacial properties of proteins. Therefore, this study aimed to explore the feasibility of soy protein-glucan-coumarin complex (S-G-C) fabricated by subcritical water treatment as novel emulsifiers with decent physicochemical stability. The addition of b-glucan and coumarin (CM) led to partial unfolding of soy proteins, the corresponding particles decreased and structure became tighter, and thereby the ternary complexes, which were formed mainly through hydrogen bonding and hydrophobic interaction exhibited more suitable three-phase contact angles (92.6°) compared with soy protein alone and binary complexes. CM might increase hydrophobic effect while b-glucan attached to the outer layer might provide steric repulsion, which effectively improve physical stability of Pickering emulsion against environmental stresses and retard droplet aggregation and creaming during the 28 days storage. This study provides a reference for the preparation of novel emulsifier with improved physicochemical and functional performance.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Investigation of physical stability of Pickering emulsion based on soy protein/β‐glucan/coumarin ternary complexes under subcritical water condition

Liang

et al. 2021

Int J of Food Sci Tech

View full text Add to dashboard Cite

show abstract

“…Active self-assembled protein-based coatings with antioxidant properties have also been developed by Yang et al (2020) and Yi et al (2020). In these research papers, lactoferrin/oat β-glucan/curcumin and pea protein isolate/methoxyl pectin/curcumin were self-assembled using spray-dried and emulsion stabilization approaches, respectively.…”

Section: Coatingsmentioning

confidence: 99%

“…In general, hydrophobic interactions and H-bonding were the main driving forces for the formation of ternary complexes. These self-assembly ternary systems could be used as natural antioxidant coatings to reduce oxidation of food lipids (Yang et al, 2020;Yi et al, 2020).…”

Section: Coatingsmentioning

confidence: 99%

Self-assembled proteins for food applications: A review

Tomadoni

Capello

Valencia

et al. 2020

Trends in Food Science & Technology

View full text Add to dashboard Cite

This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

show abstract

“…Therefore, HIPEs may be the promising healthy alternatives of converting liquid oils . As a special emulsion system with an oil volume fraction greater than 0.74, HIPEs exhibit tunable viscoelasticity with the droplets squeezing to form a 3D network structure and superior microbiological stability with a low water activity. , …”

Section: Introductionmentioning

confidence: 99%

Self-Assembled Micellar Nanoparticles by Enzymatic Hydrolysis of High-Density Lipoprotein for the Formation and Stability of High Internal Phase Emulsions

Liu

et al. 2021

J. Agric. Food Chem.

View full text Add to dashboard Cite

In this study, the influence of pH on the conformational state of EHT, which was obtained from the enzymatic hydrolysis of trypsin, and the stabilizing properties of high internal phase emulsions have been demonstrated. Critical micelle concentration and transmission electron microscopy results exhibited the formation of micellar nanoparticles with mean diameters ranging from 108 to 1359.5 nm. The results of solubility, surface hydrophobicity, and conformations indicated that EHT tended to act as particulate emulsifiers at pH 3, 5, and 7, while at alkaline pH, it was more like a polymeric emulsifier, which could be proven by confocal laser scanning microscopy. The EHT at pH 7 exhibited better stabilizing properties than those at pH 9 and 11 as influenced by storage, temperature, and ionic strength. These findings might be of great importance for broadening the range of sustainable applications of amphiphilic peptides in foods and pharmaceuticals.

show abstract

Fabrication of curcumin-loaded pea protein-pectin ternary complex for the stabilization and delivery of β‑carotene emulsions

Cited by 74 publications

References 39 publications

Investigation of physical stability of Pickering emulsion based on soy protein/β‐glucan/coumarin ternary complexes under subcritical water condition

Investigation of physical stability of Pickering emulsion based on soy protein/β‐glucan/coumarin ternary complexes under subcritical water condition

Self-assembled proteins for food applications: A review

Self-Assembled Micellar Nanoparticles by Enzymatic Hydrolysis of High-Density Lipoprotein for the Formation and Stability of High Internal Phase Emulsions

Contact Info

Product

Resources

About