Synergistic modification of structural and functional characteristics of whey protein isolate by soybean isoflavones non-covalent binding and succinylation treatment: A focus on emulsion stability

Wang, Ningzhe; Ma, Zihan; Ma, Lei; Zhang, Ye; Zhang, Kaida; Ban, Qingfeng; Wang, Xibo

doi:10.1016/j.foodhyd.2023.108994

Cited by 16 publications

(8 citation statements)

References 25 publications

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“…In addition, it was also found that the EDP had a maximum fluorescence intensity at 329.6 nm. When flavonoids were assembled with EDP, the maximum fluorescence emission wavelengths of Gal-EDP (330.7 nm), Kae-EDP (330.6 nm), and Que-EDP (329.9 nm) were all red-shifted, indicating that the microenvironment polarity of tryptophan residues was increased and thus induced the enhancement of hydrophilicity . In contrast, the maximum fluorescence emission wavelength of Myr-EDP (328.8 nm) was blue-shifted, demonstrating that the hydrophobicity of the tryptophan residue microenvironment was enhanced and hydrophobic interaction was the main driving force during the self-assembly of Myr and EDP.…”

Section: Resultsmentioning

confidence: 99%

“…These data indicated that the incorporation of Myr induced the conversion of α-helix and β-turn to a random coil in the EDP. In summary, the incorporation of flavonoids can enable the secondary structure of EDP to be more disordered, which is of benefit for the intermolecular recombination …”

Section: Resultsmentioning

confidence: 99%

“…Accordingly, the surface tension was decreased with the increase of the phenolic hydroxyl number in the flavonoid's B ring. 27 Fluorescence Spectra. The effect of flavonoid compounds on the fluorescence quenching of EDP was investigated.…”

Section: T H Imentioning

confidence: 99%

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Regulation Mechanism of Phenolic Hydroxyl Number on Self-Assembly and Interaction between Edible Dock Protein and Hydrophobic Flavonoids

Wang,

Zhou,

et al. 2023

J. Agric. Food Chem.

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In this study, galangin (Gal), kaempferol (Kae), quercetin (Que), and myricetin (Myr) were chosen as the representative flavonoids with different phenolic hydroxyl numbers in the B-ring. The edible dock protein (EDP) was chosen as the new plant protein. Based on this, the regulation mechanism of the phenolic hydroxyl number on the self-assembly behavior and molecular interaction between EDP and flavonoid components were investigated. Results indicated that the loading capacity order of flavonoids within the EDP nanomicelles was Myr (10.92%) > Que (9.56%) > Kae (6.63%) > Gal (5.55%). Moreover, this order was consistent with the order of the hydroxyl number in the flavonoid's B ring: Myr (3) > Que (2) > Kae (1) > Gal (0). The micro morphology exhibited that four flavonoid-EDP nanomicelles had a core−shell structure. In the meantime, the EDP encapsulation remarkably improved the flavonoids' water solubility, storage stability, and sustained release characteristics. During the interaction of EDP and flavonoids, the noncovalent interactions including van der Waals forces, hydrophobic interaction, and hydrogen bonding were the main binding forces. All of the results demonstrated that the hydroxyl number of bioactive compounds is a critical factor for developing a delivery system with high loading ability and stability.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Regulation Mechanism of Phenolic Hydroxyl Number on Self-Assembly and Interaction between Edible Dock Protein and Hydrophobic Flavonoids

Wang,

Zhou,

et al. 2023

J. Agric. Food Chem.

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“…Limited data on aroma binding in protein-mucin mixtures exists, but synergistic behavior has been observed in protein systems. − Ahmad et al demonstrated cooperative effects between mucin and β-lactoglobulin, modulating the latter’s affinity and accessibility to binding sites. Similarly, Wang et al noted synergistic effects of soy isoflavones in Whey Protein Isolate by inducing its unfolding.…”

Section: Resultsmentioning

confidence: 99%

“… 62 − 64 Ahmad et al 62 demonstrated cooperative effects between mucin and β-lactoglobulin, modulating the latter’s affinity and accessibility to binding sites. Similarly, Wang et al 64 noted synergistic effects of soy isoflavones in Whey Protein Isolate by inducing its unfolding.…”

Section: Resultsmentioning

confidence: 99%

Drivers of the In-Mouth Interaction between Lupin Protein Isolate and Selected Aroma Compounds: A Proton Transfer Reaction–Mass Spectrometry and Dynamic Time Intensity Analysis

Barallat-Pérez,

Pedrotti,

Oliviero

et al. 2024

J. Agric. Food Chem.

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Plant proteins often carry off-notes, necessitating customized aroma addition. In vitro studies revealed protein−aroma binding, limiting release during consumption. This study employs in vivo nose space proton transfer reaction-time-of-flight−mass spectrometry and dynamic sensory evaluation (time intensity) to explore in-mouth interactions. In a lupin protein-based aqueous system, a sensory evaluation of a trained "green" attribute was conducted simultaneously with aroma release of hexanal, nonanal, and 2-nonanone during consumption. Results demonstrated that enlarging aldehyde chains and relocating the keto group reduced maximum perceived intensity (I max _R) by 71.92 and 72.25%. Protein addition decreased I max _R by 30.91, 36.84, and 72.41%, indicating protein−aroma interactions. Sensory findings revealed a perceived intensity that was lower upon protein addition. Aroma lingering correlated with aroma compounds' volatility and hydrophobicity, with nonanal exhibiting the longest persistence. In vitro mucin addition increased aroma binding four to 12-fold. Combining PTR-ToF-MS and time intensity elucidated crucial food behavior, i.e., protein−aroma interactions, that are pivotal for food design.

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Study on the binding interaction and stability of whey protein concentrate-80 with folic acid

Wang,

Tang

et al. 2024

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Synergistic modification of structural and functional characteristics of whey protein isolate by soybean isoflavones non-covalent binding and succinylation treatment: A focus on emulsion stability

Cited by 16 publications

References 25 publications

Regulation Mechanism of Phenolic Hydroxyl Number on Self-Assembly and Interaction between Edible Dock Protein and Hydrophobic Flavonoids

Regulation Mechanism of Phenolic Hydroxyl Number on Self-Assembly and Interaction between Edible Dock Protein and Hydrophobic Flavonoids

Drivers of the In-Mouth Interaction between Lupin Protein Isolate and Selected Aroma Compounds: A Proton Transfer Reaction–Mass Spectrometry and Dynamic Time Intensity Analysis

Study on the binding interaction and stability of whey protein concentrate-80 with folic acid

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