Effects of covalent binding of different polyphenols on structure, rheology and functional properties of whey protein isolate

Tian, Ruijun; Han, Xiue; Tian, Bo; Li, Guolong; Sun, Lei; Tian, Songfan; Qin, Lanxia; Wang, Song

doi:10.1016/j.lwt.2023.114968

Cited by 25 publications

(2 citation statements)

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“…The covalent interaction between polyphenols (epigallocatechin gallate, procyanidin, apple polyphenol, and puerarin) and whey protein isolates showed rheological changes as well as improved foaming and emulsifying properties of the whey proteins; however, its surface hydrophobicity was greatly decreased. The particle sizes of conjugates and their surface were changed, which were observed via scanning electron microscopy [30].…”

Section: Protein-polypeptide Interactionsmentioning

confidence: 99%

“…Most of the available scientific data focuses on polyphenolic compounds commonly found in e.g., coffee, green tea such as epigallocatechin-3-gallate (EGCG) and chlorogenic acid [21] and dairy-derived proteins [29,30]. One important goal of such a combination is to reduce the allergenicity of milk proteins, which is an important issue in view of the continuing need to develop targeted nutrients for allergy sufferers [31].…”

Section: Introductionmentioning

confidence: 99%

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Bioactive Dairy-Fermented Products and Phenolic Compounds: Together or Apart

Wróblewska,

Kuliga,

Wnorowska

2023

Molecules

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Fermented dairy products (e.g., yogurt, kefir, and buttermilk) are significant in the dairy industry. They are less immunoreactive than the raw materials from which they are derived. The attractiveness of these products is based on their bioactivity and properties that induce immune or anti-inflammatory processes. In the search for new solutions, plant raw materials with beneficial effects have been combined to multiply their effects or obtain new properties. Polyphenols (e.g., flavonoids, phenolic acids, lignans, and stilbenes) are present in fruit and vegetables, but also in coffee, tea, or wine. They reduce the risk of chronic diseases, such as cancer, diabetes, or inflammation. Hence, it is becoming valuable to combine dairy proteins with polyphenols, of which epigallocatechin-3-gallate (EGCG) and chlorogenic acid (CGA) show a particular predisposition to bind to milk proteins (e.g., α-lactalbumin β-lactoglobulin, αs1-casein, and κ-casein). Reducing the allergenicity of milk proteins by combining them with polyphenols is an essential issue. As potential ‘metabolic prebiotics’, they also contribute to stimulating the growth of beneficial bacteria and inhibiting pathogenic bacteria in the human gastrointestinal tract. In silico methods, mainly docking, assess the new structures of conjugates and the consequences of the interactions that are formed between proteins and polyphenols, as well as to predict their action in the body.

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Section: Protein-polypeptide Interactionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Bioactive Dairy-Fermented Products and Phenolic Compounds: Together or Apart

Wróblewska,

Kuliga,

Wnorowska

2023

Molecules

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Encapsulation of rutin in protein nanoparticles by pH‐driven method: impact of rutin solubility and mechanisms

Luo,

Fu,

et al. 2023

J Sci Food Agric

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BackgroundThe use of rutin in the food industry is limited by its poor solubility. Encapsulation can be used as an effective way to improve polyphenol solubility. Proteins with high safety, biocompatibility and multiple binding sites are known as the most promising encapsulated carriers. Therefore, the improvement of rutin solubility by pH‐driven to encapsulate of rutin in SPI nanoparticles, as well as the form of rutin after encapsulation and rutin‐protein binding index were investigated.ResultsSPI had a high encapsulation efficiency (87.5 %) and loading amount (10.6%) for rutin. When the mass ratio of protein to rutin was 5:1, the highest concentration of rutin in solution was 3.27 g L‐1, which was a 51.57‐fold increase compared to the original rutin. At this situation, rutin transformed from crystalline to amorphous form. During the formation of nanoparticles, SPI was in a dynamic change of unfolding and refolding. Rutin deprotonated in alkaline conditions increased its solubility and bind to proteins to form nanoparticles during the process of backing to neutral. Hydrophobic interactions and hydrogen bond promoted the formation of the nanoparticles and there were at least 1‐2 bind sites between rutin and SPI molecule.ConclusionThese results suggested that encapsulation rutin in protein nanoparticles can effectively increase the solubility of rutin. This study may provide important information for the effective utilization of polyphenol functional foods.This article is protected by copyright. All rights reserved.

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