Wheat gliadin hydrolysates based nano-micelles for hydrophobic naringin: Structure characterization, interaction, and in vivo digestion

Wang, Zhiyong; Cheng, Xiaoyi; Meng, Fanda; Guo, Haotong; Liu, Zhengqin; Wang, Huan; Xu, Jing; Jin, Hua; Jiang, Lianzhou

doi:10.1016/j.fochx.2024.101136

Cited by 4 publications

(6 citation statements)

References 42 publications

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“…Cavitation and shear pressure generated by ultrasound expose the buried hydrophobic groups of proteins and enhance the H 0 (Figure 1F). 33 Compared to SPI, H 0 was significantly higher for SPI-U (p < 0.05). There are two main reasons for these changes: (i) the addition of ethanol disrupted the internal structure of the proteins and the looser structure was more favorable for the exposure of hydrophobic groups; (ii) the reaggregation of proteins after the removal of ethanol proceeds in an increased (more stable) direction of H 0 .…”

Section: Resultsmentioning

confidence: 85%

“…H 0 is a key indicator to evaluate the degree of protein denaturation as well as the amount of exposure of hydrophobic groups. Cavitation and shear pressure generated by ultrasound expose the buried hydrophobic groups of proteins and enhance the H 0 (Figure F) . Compared to SPI, H 0 was significantly higher for SPI-U ( p < 0.05).…”

Section: Results and Discussionmentioning

confidence: 97%

“…Around 3300 cm –1 is the amide A band which represents the O–H and N–H stretching vibrations . Compared to SPI, the peaks of all the samples were redshifted to varying degrees, implying the enhancement of hydrogen bonding between the hydroxyl and amino molecules . In addition, the band that represents the asymmetric stretching vibration of CH 2 is located at 2800–3100 cm –1 .…”

Section: Results and Discussionmentioning

confidence: 99%

“…41 Compared to SPI, the peaks of all the samples were redshifted to varying degrees, implying the enhancement of hydrogen bonding between the hydroxyl and amino molecules. 33 In addition, the band that represents the asymmetric stretching vibration of CH 2 is located at 2800−3100 cm −1 . 40 In particular, samples treated with ethanol showed a greater degree of redshift, which indicates that hydrophobic interactions play a key role.…”

Section: Ftir Spectroscopy Measurementmentioning

confidence: 99%

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Development of Novel Nanocarriers by Ultrasound and Ethanol-Assisted Soy Protein Isolate: Enhancing the Resistance of Lutein to Environmental Stress

Cheng,

Meng,

Lou

et al. 2024

J. Agric. Food Chem.

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The aim of this work was to investigate the effects of the processing sequence of ultrasound and ethanol on the physicochemical properties of soy protein isolate (SPI), which were further evaluated for the morphology and stability of SPI–lutein coassembled nanoparticles. The results showed that the sequence of ultrasound followed by ethanol treatment was the optimal one. The samples were subjected to ultrasonication followed by subunit disassembly and reassembly induced by 40% (v/v) ethanol, with the resulting molecular unfolding and subsequent aggregation being attributed to intramolecular hydrogen bonds. The recombined nanoparticles had smaller particle size (142.43 ± 2.91 nm) and turbidity (0.16 ± 0.01), and the exposure of more hydrophobic groups (H 0 = 6221.00 ± 130.20) induced a shift of SPI structure toward a more ordered direction. The homogeneous and stable particle provided excellent stability for the loading of lutein. The bioaccessibility (from 25.48 ± 2.35 to 65.85 ± 1.78%) and release rate of lutein were modulated in gastrointestinal digestion experiments. Our discoveries provide a new perspective for the development of combined physicochemical modification of proteins as nanocarriers in functional foods.

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Section: Resultsmentioning

confidence: 85%

Section: Results and Discussionmentioning

confidence: 97%

Section: Results and Discussionmentioning

confidence: 99%

Section: Ftir Spectroscopy Measurementmentioning

confidence: 99%

See 2 more Smart Citations

Development of Novel Nanocarriers by Ultrasound and Ethanol-Assisted Soy Protein Isolate: Enhancing the Resistance of Lutein to Environmental Stress

Cheng,

Meng,

Lou

et al. 2024

J. Agric. Food Chem.

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“…The frozen samples were mixed with potassium bromide (1:100, w/w) and scanned for infrared spectra using an FTIR spectrometer (Nexus 470, Thermo Nicolet Co., Ltd., USA) in the wavelength range of 4000–400 cm –1 at a resolution of 4 cm –1 and a scanning frequency of 64 times …”

Section: Methodsmentioning

confidence: 99%

Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

Cheng,

Li,

Peng

et al. 2024

J. Agric. Food Chem.

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The objective of this work was to investigate the effect of succinylation treatment on the physicochemical properties of black bean proteins (BBPI), and the relationship mechanism between BBPI structure and gel properties was further analyzed. The results demonstrated that the covalent formation of higher-molecular-weight complexes with BBPI could be achieved by succinic anhydride (SA). With the addition of SA at 10% (v/v), the acylation of proteins amounted to 92.53 ± 1.10%, at which point there was a minimized particle size of the system (300.90 ± 9.57 nm). Meanwhile, the protein structure was stretched with an irregular curl content of 34.30% and the greatest processable flexibility (0.381 ± 0.004). The dense three-dimensional mesh structure of the hydrogel as revealed by scanning electron microscopy was the fundamental prerequisite for the ability to resist external extrusion. The thermally induced hydrogels of acylated proteins with 10% (v/v) addition of SA showed excellent gel elastic behavior (1.44 ± 0.002 nm) and support capacity. Correlation analysis showed that the hydrogel strength and stability of hydrogels were closely related to the changes in protein conformation. This study provides theoretical guidance for the discovery of flexible proteins and their application in hydrogels.

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Effect of amorphous chrysin loading in hydrophobically modified Pluronic F68 nanomicelles on its anticancer activity, stability and oral bioavailability

Narayan,

Jangid,

Sharma

et al. 2024

RSC Pharm.

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Wheat gliadin hydrolysates based nano-micelles for hydrophobic naringin: Structure characterization, interaction, and in vivo digestion

Cited by 4 publications

References 42 publications

Development of Novel Nanocarriers by Ultrasound and Ethanol-Assisted Soy Protein Isolate: Enhancing the Resistance of Lutein to Environmental Stress

Development of Novel Nanocarriers by Ultrasound and Ethanol-Assisted Soy Protein Isolate: Enhancing the Resistance of Lutein to Environmental Stress

Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

Effect of amorphous chrysin loading in hydrophobically modified Pluronic F68 nanomicelles on its anticancer activity, stability and oral bioavailability

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