Characterization of binding interactions between green tea flavanoids and milk proteins

Yüksel, Zerrin; Avcı, Elif; Erdem, Yaşar Kemal

doi:10.1016/j.foodchem.2009.12.064

Cited by 241 publications

(131 citation statements)

References 19 publications

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“…This reduction may be due to the degradation of phenolic components during refrigerated storage or an increase in milk protein and phenolic component interaction. Continued growth of the bacteria during storage caused changes in phenolic components, which led to a significant increase in antioxidant activity and inhibition of DPPH (Yuksel et al, 2010). Muniandy et al (2016) studied the influence of adding green, white and black tea on the antioxidant activity of probiotic yogurt during 21 days of storage at 4°C and reported similar results.…”

Section: Aciditymentioning

confidence: 84%

Investigating the effect of aqueous extracts of basil and savory on antioxidant activity, microbial and sensory properties of probiotic yogurt

Mosiyani

Pourahmad

Eshaghi

2017

Acta Sci Pol Technol Aliment

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Section: Aciditymentioning

confidence: 84%

Investigating the effect of aqueous extracts of basil and savory on antioxidant activity, microbial and sensory properties of probiotic yogurt

Mosiyani

Pourahmad

Eshaghi

2017

Acta Sci Pol Technol Aliment

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“…5a and b), suggesting that not only the ferritin cage but also the EGCG molecules decorating the ferritin cage may improve the rutin storage stability, because the observed differences between FR and FRE are mainly associated with EGCG binding in FRE complex. Data also reveals that EGCG-FR interactions are mainly van der Waals interactions or due to hydrogen bonds, which may influence the degree of ferritin folding, contributing to the overall ferritin structure and quality [35], thus providing a better protective environment for rutin storage.…”

Section: Rutin Stability During Storagementioning

confidence: 98%

Epigallocatechin Gallate (EGCG) Decorating Soybean Seed Ferritin as a Rutin Nanocarrier with Prolonged Release Property in the Gastrointestinal Tract

Yang

Sun

Zhang

et al. 2016

Plant Foods Hum Nutr

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The instability and low bioavailability of polyphenols limit their applications in food industries. In this study, epigallocatechin gallate (EGCG) and soybean seed ferritin deprived of iron (apoSSF) were fabricated as a combined double shell material to encapsulate rutin flavonoid molecules. Firstly, due to the reversible assembly characteristics of phytoferritin, rutin was successfully encapsulated within apoSSF to form a ferritin-rutin complex (FR) with an average molar ratio of 28.2: 1 (rutin/ferritin). The encapsulation efficiency and loading capacity of rutin were 18.80 and 2.98 %, respectively. EGCG was then bound to FR to form FR-EGCG composites (FRE), and the binding number of EGCG was 27.30 ± 0.68 with a binding constant K of (2.65 ± 0.11) × 10(4) M(-1). Furthermore, FRE exhibited improved rutin stability, and displayed prolonged release of rutin in simulated gastrointestinal tract fluid, which may be attributed to the external attachment of EGCG to the ferritin cage potentially reducing enzymolysis in GI fluid. In summary, this work demonstrates a novel nanocarrier for stabilization and sustained release of bioactive polyphenols.

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“…However, tea polyphenols may reduce food digestibility by inhibiting digestive enzymes. Studies have shown that phenolic compounds from plants have a strong ability to interact with food proteins and show strong complexing abilities with enzymes (SPENCER et al, 1988;DUBEAU et al, 2010;YUKSEL et al, 2010;BANDYOPADHYAY et al, 2012). The binding interactions of tea catechins with digestive enzymes were found to denature the catalytic activity of enzymes, which reduced food digestibility (HE et al, 2006).…”

mentioning

confidence: 99%

Binding interaction between (−)-epigallocatechin-3-gallate (EGCG) of green tea and pepsin

Feng

et al. 2016

Acta Alimentaria

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Analysis of the binding interaction of (−)-epigallocatechin-3-gallate (EGCG) and pepsin is important for understanding the inhibition of digestive enzymes by tea polyphenols. We studied the binding of EGCG to pepsin using fl uorescence spectroscopy, Fourier transform infrared spectroscopy, isothermal titration calorimetry, and protein-ligand docking. We found that EGCG could inhibit pepsin activity. According to thermodynamic parameters, a negative ΔG indicated that the interaction between EGCG and pepsin was spontaneous, and the electrostatic force accompanied by hydrophobic binding forces may play major role in the binding. Data from multi-spectroscopy and docking studies suggest that EGCG could bind pepsin with a change in the native conformation of pepsin. Our results provide further understanding of the nature of the binding interactions between catechins and digestive enzymes.Keywords: EGCG, green tea, pepsin, digestion, interactionGreen tea has many potential health benefi ts attributed to tea polyphenols, in particular catechins, which have strong antioxidative activity (SABU et al., 2010). Major te a catechins include (−)-epigallocatechin-3-gallate (EGCG), (−)-epigallocatechin, (−)-epicatechingallate and (−)-epicatechin. EGCG is the most potent constituent of green tea and represents 50% of the total catechins (KILMARTIN & HSU, 2003). Tea polyphenols are soluble in water and can be added to various foods as natural antioxidants. However, tea polyphenols may reduce food digestibility by inhibiting digestive enzymes. Studies have shown that phenolic compounds from plants have a strong ability to interact with food proteins and show strong complexing abilities with enzymes (SPENCER et al., 1988;DUBEAU et al., 2010;YUKSEL et al., 2010;BANDYOPADHYAY et al., 2012). The binding interactions of tea catechins with digestive enzymes were found to denature the catalytic activity of enzymes, which reduced food digestibility (HE et al., 2006). Pepsin is a proteinase present in animals and has a signifi cant role in the digestive process. Therefore, studying the interactions of EGCG and pepsin are important to understand its mechanism of action to inhibit pepsin.Pepsin contains 2 tryptophans (Trp) and 4 tyrosines (Tyr) therefore, fl uorescence quenching can be used with the intrinsic tryptophan of Trp and Tyr to determine the binding affi nities of EGCG and pepsin and characterise the nature of the EGCG-pepsin complex.In this study, we detected the inhibitory effect of EGCG on pepsin activity by studying the interaction of EGCG and pepsin with fl uorescence spectroscopy, Fourier transform infrared (FTIR) spectroscopy, and isothermal titration calorimetry (ITC). To substantiate our experimental studies, docking studies were performed. Important information, such as the change in protein secondary structure and association constant, are reported. We aimed to help understand the nature of binding between catechins and digestive enzymes.

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Characterization of binding interactions between green tea flavanoids and milk proteins

Cited by 241 publications

References 19 publications

Investigating the effect of aqueous extracts of basil and savory on antioxidant activity, microbial and sensory properties of probiotic yogurt

Investigating the effect of aqueous extracts of basil and savory on antioxidant activity, microbial and sensory properties of probiotic yogurt

Epigallocatechin Gallate (EGCG) Decorating Soybean Seed Ferritin as a Rutin Nanocarrier with Prolonged Release Property in the Gastrointestinal Tract

Binding interaction between (−)-epigallocatechin-3-gallate (EGCG) of green tea and pepsin

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