The non-covalent interaction between two polyphenols and caseinate as affected by two types of enzymatic protein crosslinking

Zhang, Yanjie; Zhang, Na; Zhao, Xin‐Huai

doi:10.1016/j.foodchem.2021.130375

Cited by 22 publications

(3 citation statements)

References 44 publications

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“…It is worth noting that although AGH has a greater capacity to inhibit 3-DG than CLE, it significantly increased the production of GO, which was notably higher than the control group. Similar results were reported by Zheng and Sun (2021), who showed that AGH had a significant inhibitory effect on 3-DG while showing an opposite effect on GO. AGH can react with 3-DG and other dicarbonyl compounds to form stable hydrazones, leading to decreases in dicarbonyl compounds in the BSA-Glu glycation system (Kukreja, 2023).…”

Section: Inhibitory Effect Of Cle On Dicarbonyl Compoundssupporting

confidence: 90%

Coffee leaf extract inhibits advanced glycation end products and their precursors: A mechanistic study

Sun,

Xie,

Huang

et al. 2024

Journal of Food Science

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Excessive accumulation of advanced glycation end products (AGEs) in the body is associated with diabetes and its complications. In this study, we aimed to explore the potential and mechanism of coffee leaf extract (CLE) in inhibiting the generation of AGEs and their precursors in an in vitro glycation model using bovine serum albumin and glucose (BSA–Glu) for the first time. High‐performance liquid chromatography analysis revealed that CLE prepared with ultrasound pretreatment (CLE‐U) contained higher levels of trigonelline, mangiferin, 3,5‐dicaffeoylquinic acid, and γ‐aminobutyric acid than CLE without ultrasound pretreatment (CLE‐NU). The concentrations of these components, along with caffeine and rutin, were dramatically decreased when CLE‐U or CLE‐NU was incubated with BSA–Glu reaction mixture. Both CLE‐U and CLE‐NU exhibited a dose‐dependent inhibition of fluorescent AGEs, carboxymethyllysine, fructosamine, 5‐hydroxymethylfurfural, 3‐deoxyglucosone, glyoxal, as well as protein oxidation products. Notably, CLE‐U exhibited a higher inhibitory capacity compared to CLE‐NU. CLE‐U effectively quenched fluorescence intensity and increased the α‐helix structure of the BSA–Glu complex. Molecular docking results suggested that the key bioactive compounds present in CLE‐U interacted with the arginine residues of BSA, thereby preventing its glycation. Overall, this research sheds light on the possible application of CLE as a functional ingredient in combating diabetes by inhibiting the generation of AGEs.

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Section: Inhibitory Effect Of Cle On Dicarbonyl Compoundssupporting

confidence: 90%

Coffee leaf extract inhibits advanced glycation end products and their precursors: A mechanistic study

Sun,

Xie,

Huang

et al. 2024

Journal of Food Science

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show abstract

“…Additionally, there was no new band was observed in Figure 5, indicating there was no covalent bond formed in the complex systems in this study. The results of SDS-PAGE corroborated the conclusion of Section Fluorescence Spectrum Analysis, which revealed that the bonds between SPI and quercetin were mainly non-covalent (50).…”

Section: Sds-page Analysis Of Spi and Quesupporting

confidence: 80%

Changes on the conformational and functional properties of soybean protein isolate induced by quercetin

Zhang

Hou²,

Zhu³

et al. 2022

Front. Nutr.

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The conformational changes and functional properties of SPI induced by quercetin was investigated via fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy and molecular docking. A decrease in the fluorescence intensity and a blue shift in the maximum wavelength were observed due to the binding process with fluorescent residues. The analysis of Stern-Volmer equation showed that the fluorescence quenching induced by quercetin took the form of static quenching, and the binding stoichiometry between SPI and quercetin was 1:1. The values of ΔH and ΔS were both positive illustrating that hydrophobic interaction was the primary binding force between quercetin and SPI. Results of FTIR and CD indicated that the binding with quercetin changed the secondary structure of SPI, resulting in a partially unfolded and more flexible structure. SDS-PAGE confirmed there was no covalent interaction between the two constituents. Molecular docking demonstrated that there were stable configurations and high matching degrees in both 11S and 7S proteins with quercetin via hydrogen bonds and hydrophobic interactions. Meanwhile, modification by quercetin enhanced the foaming and emulsifying capacities of SPI. These findings might provide theory reference for elucidation the mechanism of polyphenols-proteins interaction and development of related food additive products in future.

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“…It can be observed that enzymatic hydrolysis promotes the amphiphilic properties of proteins. For example, the binding affinity of proteins for ligands can be promoted achieved byenzymatic hydrolysis due to the noncovalent interaction, regarded to be induced by hydrophobic interaction and then stabilized by hydrogen bonds …”

Section: Introductionmentioning

confidence: 99%

The Effect of Whey Protein Isolate Hydrolysate on Digestive Properties of Phytosterol

Zhao,

Sun,

et al. 2024

J. Agric. Food Chem.

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Phytosterol (PS) is a steroid, and its bioavailability can be enhanced by interacting with protein in the C-24 hydroxyl group. The interaction between sterols and amino acid residues in proteins can be enhanced by enzymatic hydrolysis. Phytosterol and whey insulation hydrolysates (WPH1−4) fabricated by the Alcalase enzyme at different enzymatic hydrolysis times were selected as delivery systems to simulate sterol C-24 hydroxyl group interaction with protein. Increasing hydrolysis time can promote the production of β-Lg, which raises the ratio of β-turn in the secondary structure and promotes the formation of interaction between WPH and PS. The correlation coefficient between hydrogen bonds and encapsulation efficiency (EE) and bioaccessibility is 0.91 and 0.88 (P < 0.05), respectively, indicating that hydrogen bonds of two components significantly influenced the combination by concealing the hydrophobic amino acids and some residues, which improved PS EE and bioavailability by 3.03 and 2.84 times after PS was combined with the WPI hydrolysate. These findings are expected to enhance the absorption of PS and other macromolecules by protein enzymatic hydrolysis to broaden their applications for food.

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The non-covalent interaction between two polyphenols and caseinate as affected by two types of enzymatic protein crosslinking

Cited by 22 publications

References 44 publications

Coffee leaf extract inhibits advanced glycation end products and their precursors: A mechanistic study

Coffee leaf extract inhibits advanced glycation end products and their precursors: A mechanistic study

Changes on the conformational and functional properties of soybean protein isolate induced by quercetin

The Effect of Whey Protein Isolate Hydrolysate on Digestive Properties of Phytosterol

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