The effects of conjugation of walnut protein isolate with polyphenols on protein solubility, antioxidant activity, and emulsifying properties

Huang, Xuan; Yan, Chunjun; Lin, Ming Tsan; He, Changwei; Xu, Yan; Huang, Yukun; Zhou, Zheng

doi:10.1016/j.foodres.2022.111910

Cited by 47 publications

(7 citation statements)

References 56 publications

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“…Although the coupling of polyphenols can introduce nonpolar hydrophobic benzene rings into proteins, the introduction of hydrophilic hydroxyl groups of phenolic compounds can enhance the hydrophilicity of proteins, which is considered to be an essential factor affecting the hydrophobicity of proteins. 37 Ke et al also obtained similar research results, and they found that after covalently bonding quercetin and casein, hydrophilic hydroxyl groups may be introduced, thus reducing the surface hydrophobicity of the protein. 38 We inferred that, after covalent modification, some previously buried hydrophilic regions may be exposed and some hydrophobic residues blocked, resulting in changes in ferritin conformation, thus improving the hydrophilicity of ferritin.…”

Section: Surface Hydrophobicity Analysis Surface Hydrophobicity (S Omentioning

confidence: 68%

“…So when the caffeic acid addition level was 1:80 (ferritin/caffeic acid molar ratio). Although the coupling of polyphenols can introduce nonpolar hydrophobic benzene rings into proteins, the introduction of hydrophilic hydroxyl groups of phenolic compounds can enhance the hydrophilicity of proteins, which is considered to be an essential factor affecting the hydrophobicity of proteins . Ke et al also obtained similar research results, and they found that after covalently bonding quercetin and casein, hydrophilic hydroxyl groups may be introduced, thus reducing the surface hydrophobicity of the protein .…”

Section: Resultsmentioning

confidence: 91%

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Dual Decoration of Ferritin Nanocages by Caffeic Acid and Betanin with Covalent and Noncovalent Approaches: Structure and Stability Analyses

Sha,

Zhang,

et al. 2024

J. Agric. Food Chem.

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Ferritin is a cage-like protein with modifiable outer and inner surfaces. To functionalize ferritin with preferable carrier applications, caffeic acid was first covalently bound to the soybean ferritin outer surface to fabricate a caffeic acid−ferritin complex (CFRT) by alkali treatment (pH 9.0). A decreased content of free amino acid (0.34 μmol/mg) and increased polyphenol binding equivalent (63.76 nmol/mg) indicated the formation of CFRT (ferritin/caffeic acid, 1:80). Fluorescence and infrared spectra verified the binding of caffeic acids to the ferritin structure. DSC indicated that the covalent modification enhanced the thermal stability of CFRT. Besides, CFRT maintained the typically spherical shape of ferritin (12 nm) and a hydration radius of 7.58 nm. Moreover, the bioactive colorant betanin was encapsulated in CFRT to form betanin-loaded CFRT (CFRTB), with an encapsulation rate of 15.5% (w/w). The betanin stabilities in CFRTB were significantly improved after heat, light, and Fe 3+ treatments, and its red color retention was enhanced relative to the free betanin. This study delves into the modifiable ferritin application as nanocarriers of dual molecules and gives guidelines for betanin as a food colorant.

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Section: Surface Hydrophobicity Analysis Surface Hydrophobicity (S Omentioning

confidence: 68%

Section: Resultsmentioning

confidence: 91%

Dual Decoration of Ferritin Nanocages by Caffeic Acid and Betanin with Covalent and Noncovalent Approaches: Structure and Stability Analyses

Sha,

Zhang,

et al. 2024

J. Agric. Food Chem.

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“…Protein solubility is affected by its physiochemical properties, including particle size [ 25 ], net charge [ 26 ], surface hydrophobicity [ 27 ], etc. The hydrodynamic diameter of irradiated CPC was generally less than unirradiated CPC ( Figure 2 B).…”

Section: Resultsmentioning

confidence: 99%

Electron Beam Irradiation Alters the Physicochemical Properties of Chickpea Proteins and the Peptidomic Profile of Its Digest

Zhang,

Kong,

et al. 2023

Molecules

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Irradiation can be used for the preservation of chickpea protein as it can destroy microorganisms, bacteria, virus, or insects that might be present. However, irradiation may provoke oxidative stress, and therefore modify the functionality and nutritional value of chickpea protein. In order to study the effects of irradiation on the physicochemical properties and digestion behaviour of chickpea protein, chickpea protein concentrate (CPC) was treated with electron beam irradiation (EBI) at doses of 5, 10, 15, and 20 kGy. After irradiation, protein solubility first increased at 10 kGy and 15 kGy, and then decreased at the higher dose of 20 kGy. This was supported by SDS-PAGE, where the intensity of major protein bands first increased and then decreased. Increased doses of EBI generally led to greater oxidative modification of proteins in CPC, indicated by reduced sulfhydryls and increased carbonyls. In addition, the protein structure was modified by EBI as shown by Fourier transform infrared spectroscopy analysis, where α-helix generally decreased, and β-sheet increased. Although the protein digestibility was not significantly affected by EBI, the peptidomic analysis of the digests revealed significant differences among CPC irradiated with varying doses. A total of 337 peptides were identified from CPC irradiated with 0 kGy, 10 kGy, and 20 kGy, with 18 overlapping peptides and 60, 29, and 40 peptides specific to the groups of 0, 10, and 20 kGy respectively. Theoretical calculation showed that the distribution of peptide length, hydrophobicity, net charge, and C-terminal residues were affected by irradiation. The 2, 2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity showed a marginal decrease with an increasing dose of irradiation. In conclusion, EBI led to oxidative modification and structural changes in chickpea protein, which subsequently affected the physicochemical properties of peptides obtained from in-vitro digestion of CPC, despite similar digestibility.

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“…Meanwhile, the higher hydrophobic interaction functioned as a safeguard against the aggregation of the emulsion droplets. The covalent interaction between proanthocyanins and proteins potentially bolstered the protein emulsification attributes, promoting uniform droplet distribution [40,41]. The representative cryo-scanning electron microscopy (cryo-SEM) images, along with magnified images, are employed to provide deeper insights into the microstructure of the emulsion in Figure 4d-f.…”

Section: Microstructure Observationmentioning

confidence: 99%

Egg White Protein–Proanthocyanin Complexes Stabilized Emulsions: Investigation of Physical Stability, Digestion Kinetics, and Free Fatty Acid Release Dynamics

Zhang,

Li,

Yang

et al. 2024

Molecules

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Egg white proteins pose notable limitations in emulsion applications due to their inadequate wettability and interfacial instability. Polyphenol-driven alterations in proteins serve as an effective strategy for optimizing their properties. Herein, covalent and non-covalent complexes of egg white proteins-proanthocyanins were synthesized. The analysis of structural alterations, amino acid side chains and wettability was performed. The superior wettability (80.00° ± 2.23°) and rigid structure (2.95 GPa) of covalent complexes established favorable conditions for their utilization in emulsions. Furthermore, stability evaluation, digestion kinetics, free fatty acid (FFA) release kinetics, and correlation analysis were explored to unravel the impact of covalent and non-covalent modification on emulsion stability, dynamic digestion process, and interlinkages. Emulsion stabilized by covalent complex exhibited exceptional stabilization properties, and FFA release kinetics followed both first-order and Korsmeyer–Peppas models. This study offers valuable insights into the application of complexes of proteins-polyphenols in emulsion systems and introduces an innovative approach for analyzing the dynamics of the emulsion digestion process.

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The effects of conjugation of walnut protein isolate with polyphenols on protein solubility, antioxidant activity, and emulsifying properties

Cited by 47 publications

References 56 publications

Dual Decoration of Ferritin Nanocages by Caffeic Acid and Betanin with Covalent and Noncovalent Approaches: Structure and Stability Analyses

Dual Decoration of Ferritin Nanocages by Caffeic Acid and Betanin with Covalent and Noncovalent Approaches: Structure and Stability Analyses

Electron Beam Irradiation Alters the Physicochemical Properties of Chickpea Proteins and the Peptidomic Profile of Its Digest

Egg White Protein–Proanthocyanin Complexes Stabilized Emulsions: Investigation of Physical Stability, Digestion Kinetics, and Free Fatty Acid Release Dynamics

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