Fabrication of antioxidant emulsifiers from natural ingredients: Conjugation of egg white proteins with catechin and chlorogenic acid

Sun, Jun; Jing, Hui; Mu, Yang; McClements, David Julian; Dong, Shijian; Xu, Bin

doi:10.1016/j.foodhyd.2020.106019

Cited by 54 publications

(23 citation statements)

References 35 publications

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“…The following studies concluded that protein–polyphenol complexes exhibited stronger antioxidant activity than the unmodified proteins. Sun et al ( 40 ) showed that the antioxidant capacity of EWP was significantly improved when coupled with catechin (CT) and CA. Studies have shown that under the same protein concentration, the DPPH free radical scavenging capabilities of EWP-CT and EWP-CA are 38.0 and 67.7%, respectively, which were 2.5- and 4.5 fold than that of unmodified EWP ( 40 ).…”

Section: Effects Of Protein–polyphenols Interaction On the Protein Structure And Its Functional Propertiesmentioning

confidence: 99%

“…Sun et al ( 40 ) showed that the antioxidant capacity of EWP was significantly improved when coupled with catechin (CT) and CA. Studies have shown that under the same protein concentration, the DPPH free radical scavenging capabilities of EWP-CT and EWP-CA are 38.0 and 67.7%, respectively, which were 2.5- and 4.5 fold than that of unmodified EWP ( 40 ). As reported earlier, Staszewski et al ( 6 ) also concluded that the combination of tea polyphenols with β-LG could improve the oxidation stability of oil-in-water emulsions, while the complexes had stronger antioxidant activities than the pure β-LG.…”

Section: Effects Of Protein–polyphenols Interaction On the Protein Structure And Its Functional Propertiesmentioning

confidence: 99%

“…Quan et al ( 14 ) also showed that EWP enhances emulsion stability, and is often used in food as an emulsifier. In addition, Sun et al ( 40 ) found that the covalent complexes between EWP and polyphenols (CT or CA) can significantly improve the antioxidant activity and emulsifying performance of EWP, thus improving the oxidative and coalescence stability of emulsions. Moreover, LF is often used to interact with polyphenols, polysaccharides or other proteins to improve its emulsifying properties.…”

Section: Types Of Protein–polyphenol Complexesmentioning

confidence: 99%

“…The pI values of EWP–CT and EWP–CA complexes were mildly lower than those of EWP, suggesting that CT and CA complexes changed the surface charge characteristics of EWP. It can be explained that CT or CA complexes possibly decreased the number of exposed positive groups on the surfaces of the protein, or increased the number of exposed negative groups ( 40 ). This is consistent with the findings of Li et al ( 36 ).…”

Section: Effect Of Protein–polyphenol Complexes On Stability Of Emulsionsmentioning

confidence: 99%

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Recent Progress on Protein-Polyphenol Complexes: Effect on Stability and Nutrients Delivery of Oil-in-Water Emulsion System

Ritzoulis

et al. 2021

Front. Nutr.

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Oil-in-water emulsions are widely encountered in the food and health product industries. However, the unsaturated fatty acids in emulsions are easily affected by light, oxygen, and heat, which leads to oxidation, bringing forward difficulties in controlling emulsion quality during transportation, storage, and retail. Proteins are commonly used as emulsifiers that can enhance the shelf, thermal and oxidation stability of emulsions. Polyphenols are commonly found in plants and members of the family have been reported to possess antioxidant, anticancer, and antimicrobial activities. Numerous studies have shown that binding of polyphenols to proteins can change the structure and function of the latter. In this paper, the formation of protein–polyphenol complexes (PPCs) is reviewed in relation to the latters' use as emulsifiers, using the (covalent or non-covalent) interactions between the two as a starting point. In addition, the effects polyphenol binding on the structure and function of proteins are discussed. The effects of proteins from different sources interacting with polyphenols on the emulsification, antioxidation, nutrient delivery and digestibility of oil-in-water emulsion are also summarized. In conclusion, the interaction between proteins and polyphenols in emulsions is complicated and still understudied, thereby requiring further investigation. The present review results in a critical appraisal of the relevant state-of-the-art with a focus on complexes' application potential in the food industry, including digestion and bioavailability studies.

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Section: Effects Of Protein–polyphenols Interaction On the Protein Structure And Its Functional Propertiesmentioning

confidence: 99%

Section: Effects Of Protein–polyphenols Interaction On the Protein Structure And Its Functional Propertiesmentioning

confidence: 99%

Section: Types Of Protein–polyphenol Complexesmentioning

confidence: 99%

Section: Effect Of Protein–polyphenol Complexes On Stability Of Emulsionsmentioning

confidence: 99%

See 2 more Smart Citations

Recent Progress on Protein-Polyphenol Complexes: Effect on Stability and Nutrients Delivery of Oil-in-Water Emulsion System

Ritzoulis

et al. 2021

Front. Nutr.

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“…Possessing both emulsifying and antioxidant features, the PI 2.5–8.5 and PI 10.5–2.5 may belong to the group of natural antioxidant emulsifiers, a term being introduced by McClements and Decker [ 22 ]. Since the functional properties of the antioxidant emulsifiers are highly dependent on the type of the polyphenols and/or proteins [ 23 , 70 , 71 , 72 ], the compositional complexity of the PI 2.5–8.5 and PI 10.5–2.5 impose additional analyses to elucidate their synergistic effect on emulsion stability and lipid oxidation. Still, the current study outlined the two products as potential alternatives to synthetic emulsifiers and antioxidants currently used in the food and nutraceutical industries.…”

Section: Resultsmentioning

confidence: 99%

Multifunctionality of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation

Georgiev

Kalaydzhiev

Ivanova

et al. 2022

Foods

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Rapeseed meal is a by-product of the oil-producing industry with a currently underestimated application. Two protein isolates, PI2.5–8.5 or PI10.5–2.5, were obtained from industrial rapeseed meal after treatment with an aqueous ethanol solution. The alkaline-extracted proteins were sequentially precipitated by two different modes, from pH 10.5 to 2.5, and vice versa, from 2.5 to 8.5, with a step of 1 pH unit. The preparation approach influenced both the functional and antioxidant properties of the isolates. The PI10.5–2.5 exhibited higher water and oil absorption capacities than PI2.5–8.5, reaching 2.68 g H2O/g sample and 2.36 g oil/g sample, respectively. The emulsion stability of the PI2.5–8.5, evaluated after heating at 80 °C, was either 100% or close to 100% for all pH values studied (from 2 to 10), except for pH 6 where it reached 93.87%. For the PI10.5–2.5, decreases in the emulsion stability were observed at pH 8 (85.71%) and pH 10 (53.15%). In the entire concentration range, the PI10.5–2.5 exhibited a higher scavenging ability on 2,2-diphenyl-1-picryl hydrazyl (DPPH) and hydroxyl radicals than PI2.5–8.5 as evaluated by DPPH and 2-deoxyribose assays, respectively. At the highest concentration studied, 1.0%, the neutralization of DPPH radicals by PI10.5–2 reached half of that exhibited by synthetic antioxidant butylhydroxytoluene (82.65%). At the same concentration, the inhibition of hydroxyl radicals by PI10.5–2 (71.25%) was close to that achieved by mannitol (75.62%), which was used as a positive control. Established antioxidant capacities add value to the protein isolates that can thus be used as both emulsifiers and antioxidants.

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Chemical and thermodynamic characterization of antioxidant emulsifiers: The case of complex of sodium caseinate with EGCG

Tang

Ritzoulis

et al. 2023

Food Frontiers

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In this study, complexes formed by sodium caseinate (CS) and different concentrations of (−)‐epigallocatechin‐3‐gallate (EGCG) were successfully prepared. The structures of the CS–EGCG complexes were then analyzed by fluorescence spectroscopy, circular dichroism, and Fourier transform infrared spectroscopy (FTIR). Their thermodynamic features were also analyzed by Van't Hoff equation before evaluating antioxidant properties as well as emulsion stability. The results showed that EGCG grafting significantly altered the CS structure, primarily due to their interactions. However, besides the covalent bonding within CS–EGCG, thermodynamic analysis further highlighted the presence of slight interactions driven by hydrophobic and entropic changes. The EGCG grafting also decreased the surface hydrophobicity of CS while increasing its solubility, thus improving the stability of the protein in water. Finally, the grafting process significantly improved the thermal and emulsifying stability of CS as well as its antioxidant properties, especially 3‐ethylbenzothiazoline‐6‐sulfonic acid and 2,2‐diphenyl‐1‐picrylhydrazyl scavenging properties and ferric ion reducing power. These findings can contribute to the study of protein and polyphenol interactions in food fields.

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Fabrication of antioxidant emulsifiers from natural ingredients: Conjugation of egg white proteins with catechin and chlorogenic acid

Cited by 54 publications

References 35 publications

Recent Progress on Protein-Polyphenol Complexes: Effect on Stability and Nutrients Delivery of Oil-in-Water Emulsion System

Recent Progress on Protein-Polyphenol Complexes: Effect on Stability and Nutrients Delivery of Oil-in-Water Emulsion System

Multifunctionality of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation

Chemical and thermodynamic characterization of antioxidant emulsifiers: The case of complex of sodium caseinate with EGCG

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