Function, digestibility and allergenicity assessment of ovalbumin–EGCG conjugates

He, Wenqi; Xu, Haoxie; Lu, Yuqin; Zhang, Tingting; Li, Shuiming; Xiao, Lin; Xu, Bingqi; Wu, Xuli

doi:10.1016/j.jff.2019.103490

Cited by 76 publications

(45 citation statements)

References 38 publications

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“…The covalent conjugates of ovalbumin with EGCG formed by alkaline treatment methods did not migrate significantly. 7 This difference compared to our results as achieved with ovalbumin-EGCG conjugates might be a result of the different preparation methods. 31 As shown in Fig.…”

Section: Resultscontrasting

confidence: 86%

“…The difference between our results and those for other proteins might be attributed to the difference of structural characteristics and the preparation methods. Many studies have confirmed that covalent conjugation with polyphenols can reduce the allergenic capacity of protein, such as ⊎-lactoglobulin, 34 whey proteins, 37,38 ovalbumin 7 and soy protein isolate. 20 To this point, conjugation with polyphenols can reduce the allergenic capacity and random structure of protein.…”

Section: Secondary Structure Of Pcrpi-egcgmentioning

confidence: 99%

“…These results were in agreement with a previous study reporting that covalent modification of lactoferrin with polyphenols increased the denaturation temperature. 36 However, the thermal stability of ovalbumin was decreased after conjugation with EGCG, 7 which may be a result of the difference of the tertiary conformation of ovalbumin and pcRPI. In addition, the enthalpy (ΔH) of native-pcRPI, control-pcRPI and pcRPI-EGCG was 0.9, 1.4 and 1.8 J g −1 , respectively.…”

Section: Secondary Structure Of Pcrpi-egcgmentioning

confidence: 99%

“…In a redox initiative ascorbate acid-hydrogen peroxide system, the two ionizable hydroxyl groups in ascorbate acid are oxidized by hydrogen peroxide to form ascorbate radical and dehydroacorbic acid, simultaneously generating hydroxyl radicals. [5][6][7][8] These ascorbate radicals can attack the sensitive residues on the side chains of protein and thus produce macro radical species, and polyphenol is oxidized to its corresponding quinone. These macro radicals and certain amino acids can further conjugate with quinone compounds through a covalent link.…”

Section: Introductionmentioning

confidence: 99%

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Conjugation of (–)‐epigallocatechin‐3‐gallate and protein isolate from large yellow croaker (Pseudosciaena crocea) roe: improvement of antioxidant activity and structural characteristics

Han

Yin

et al. 2021

J Sci Food Agric

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BACKGROUND: Large yellow croaker (Pseudosciaena crocea) roe is the main by-product in the processing of large yellow croaker. Previous studies have found that its protein isolates are composed of vitellogenin, as well as vitellogenin B and C, having good functional properties. (-)-Epigallocatechin-3-gallate (EGCG) is a natural antioxidant component that can be combined with protein to improve antioxidant activity and structural characteristics of protein.RESULTS: EGCG was bound with the P. crocea roe protein isolate (pcRPI) by the free radical method to prepare the conjugate. The formation of pcRPI-EGCG conjugates was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel permeation chromatography, which showed that the calculated weight-average molar masses of native-pcRPI and pcRPI-EGCG conjugates were 86.9 and 215.3 kDa, respectively. The results of fluorescence, ultraviolet, circular and infrared spectra indicated that the conjugation of EGCG with native-pcRPI changed the secondary and tertiary structure of native-pcRPI. The pcRPI-EGCG conjugates exhibited higher thermal stability than native-pcRPI. The radical scavenging and reducing power of native-pcRPI were increased by 2.0-2.5-and 1.4-fold, respectively, after the EGCG-grafting reaction.CONCLUSION: These results indicate that the binding of pcRPI and EGCG effectively improved the antioxidant properties and structural characteristics of the pcRPI.

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Section: Resultscontrasting

confidence: 86%

Section: Secondary Structure Of Pcrpi-egcgmentioning

confidence: 99%

Section: Secondary Structure Of Pcrpi-egcgmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Conjugation of (–)‐epigallocatechin‐3‐gallate and protein isolate from large yellow croaker (Pseudosciaena crocea) roe: improvement of antioxidant activity and structural characteristics

Han

Yin

et al. 2021

J Sci Food Agric

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“…They found that the covalent complex of polyphenols and has a higher emulsifying ability than FPI [ 11 ]. When He studied the covalent binding of ovalbumin (OVA) and EGCG, he also found that the emulsification of OVA was improved [ 12 ]. The addition of phenol allows the protein to acquire phenolic hydroxyl groups, thereby changing the functional properties of the protein.…”

Section: Introductionmentioning

confidence: 99%

Hemp (Cannabis sativa L.) Seed Protein–EGCG Conjugates: Covalent Bonding and Functional Research

Pang

Yang

Bian

et al. 2021

Foods

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In order to make HPI have a wide application prospect in the food industry, we used EGCG to modify HPI. In this study, we prepared different concentrations (1, 2, 3, 4, and 5 mM) of (−)-epigallocatechin gallate (EGCG) covalently linked to HPI and use methods such as particle size analysis, circular dichroism (CD), and three-dimensional fluorescence spectroscopy to study the changes in the structure and functional properties of HPI after being covalently combined with EGCG. The particle size data indicated that the covalent HPI-EGCG complex was larger than native HPI, and the particle size was mainly distributed at about 200 μm. CD and three-dimensional fluorescence spectroscopy analyses showed that the conformation of the protein was changed by conjugation with EGCG. The β-sheet content decreased from 82.79% to 66.67% after EGCG bound to the protein, and the hydrophobic groups inside the protein were exposed, which increased the hydrophobicity of the protein and changed its conformation. After HPI and 1 mM of EGCG were covalently bonded, the solubility and emulsifying properties of the covalent complex were improved compared with native HPI. These results indicated that HPI-EGCG conjugates can be added in some foods.

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Impact of the Covalent Interaction Between Ferulic Acid and Ovalbumin on the Structure and Functional Properties of the Protein

Barbosa,

Araújo,

Cordeiro

et al. 2024

Food Biophysics

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Function, digestibility and allergenicity assessment of ovalbumin–EGCG conjugates

Cited by 76 publications

References 38 publications

Conjugation of (–)‐epigallocatechin‐3‐gallate and protein isolate from large yellow croaker (Pseudosciaena crocea) roe: improvement of antioxidant activity and structural characteristics

Conjugation of (–)‐epigallocatechin‐3‐gallate and protein isolate from large yellow croaker (Pseudosciaena crocea) roe: improvement of antioxidant activity and structural characteristics

Hemp (Cannabis sativa L.) Seed Protein–EGCG Conjugates: Covalent Bonding and Functional Research

Impact of the Covalent Interaction Between Ferulic Acid and Ovalbumin on the Structure and Functional Properties of the Protein

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