Protein Polyphenol Research Articles

Soy protein isolate-catechin non-covalent and covalent complexes: Focus on structure, aggregation, stability and in vitro digestion characteristics

Studies on soybean protein–polyphenol complexes mainly focus on the effects of non-covalent/covalent interactions on the structure and function of the complexes, and there are few studies on the stability and in vitro digestion mechanism of these complexes. We investigated the effects of non-covalent/covalent binding of catechin with soy protein isolate (SPI) on the structure, aggregation, stability and digestive characteristics of the SPI-Catechin complexes. SPI-Catechin non-covalent/covalent complexes were prepared under neutral (pH 7.0) or alkaline (pH 9.0) conditions, and the protein:polyphenol ratio was optimized. The interaction of SPI and catechin disordered the secondary structure and exposed more hydrophobic residues to a hydrophilic microenvironment. SPI-Catechin covalent complexes exhibited higher thermal stability, storage stability, and antioxidant activity compared to non-covalent complexes. Results of in vitro digestion showed that SPI-Catechin covalent complexes can substantially (up to ∼86%) improve the bioaccessibility of catechin. The stronger anti-digestion ability of the covalent complex might be due to the more complete structure of 7S and 11S subunits in the digestion products. This study provides a theoretical basis for the application of SPI-Catechin non-covalent/covalent complexes as functional components of plant protein drinks. • The degree of binding between catechin and SPI was affected by the ratio and pH value. • SPI-Catechin covalent complexes were more stable than non-covalent complexes. • Non-covalent/covalent binding of SPI improved the bioaccessibility of catechin. • SPI-Catechin covalent complexes had stronger anti-digestive ability.

Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol-Protein Interaction Approach.

The preparation of the interaction between polyphenols and protein is of great significance for increasing added value and promoting the application of egg yolk immunoglobulin (IgY). This study systematically investigated the effect of catechin on yolk immunoglobulin structural characteristics and functional properties. The binding conditions, force types, molecular conformation, and residual microenvironment of the interaction between catechin and IgY were analyzed by molecular docking technology, UV-vis absorption and fluorescence spectroscopy studies. The results showed that the main binding forces in the complex were hydrogen bonding and van der Waals forces. After the interaction, fluorescence quenching occurred and the maximum emission wavelength was redshifted. The results showed that the microenvironment around IgY increased polarity, increased hydrophilicity and decreased hydrophobicity, and the structure of the peptide chain changed. The bacteriostatic thermal stability of the compound against Escherichia coli and Staphylococcus aureus was lower than that of catechin IgY. The bacteriostatic acid and base stability were higher than that of catechin and IgY. The antioxidant activity was catechin, complex, and IgY, in descending order. The antioxidant activity of catechin and complex was significantly higher than that of IgY. At the same concentration, the apparent viscosity of the three samples was complex, IgY and catechin, in descending order. G' was greater than G" indicating that elastic properties dominate in G". The G' and G" values of the complex were higher than those of the other groups. Rheological results indicated that the complex may have high physical stability. This study provides theoretical support for broadening the application field of IgY and suggest its properties change in the machining process. It also provides new ideas for the development of functional foods from poultry eggs.

A model study on the site-specificity of (−)-epicatechin-induced reactions in β-lactoglobulin by high-resolution mass spectrometry in combination with bioinformatics

Polyphenol–protein reactions in model solutions of β-lactoglobulin (β-LG) incubated with (−)-epicatechin at 37 °C and 60 °C were monitored by microLC–timsTOF Pro-MS/MS combined with bioinformatics strategies. The addition of (−)-epicatechin to the model solutions resulted in changes in tryptic peptide profiles. Covalent bond formation between (−)-epicatechin o-quinones and β-LG was identified for the residues S27, S30, K60, C66, K69, and C160, with C160 being the predominant binding site. Furthermore, the incubation of β-LG with (−)-epicatechin significantly promoted oxidation, especially for the residues M7 and M24. The reaction of monomeric (−)-epicatechino-quinone at C160 was also identified in the milk chocolate sample. The adaptation of this study by extending the scope of the reaction products offers significant potential for comprehensive food profiling strategies.

Phenolic compounds in walnut pellicle improve walnut (Juglans regia L.) protein solubility under pH-shifting condition

This study focused on the interaction of walnut protein with phenolic extracts of walnut pellicle (PEWP) under alkaline condition, leading to enhancement of protein solubility under neutral condition. First, the change of PEWP under alkaline condition was determined by RP-HPLC and mass spectrometry, and the results showed that most ellagitannins in PEWP could be retained under alkaline condition within 3 h. Interaction between PEWP and walnut protein under pH-shifting condition resulted in the remarkable increase of protein solubility (above 90%) at neutral pH. The results from SDS-PAGE and SEC showed that the improved solubility lied in the formation of large and soluble protein aggregates due to the covalent interaction among walnut protein and polyphenols. A significant change in tertiary structure of protein–phenolic complex was witnessed by fluorescence spectrum and near-UV circular dichroism. Meanwhile, walnut protein–polyphenol interaction led to a slight increase in β-turn while a slight decrease in β-sheet. Combined with amino acid composition, it could be illustrated that the covalent bonding for walnut protein with polyphenol mainly occurred at Lysine residues.

Soy protein–phlorizin conjugate prepared by tyrosinase catalysis: Identification of covalent binding sites and alterations in protein structure and functionality

Tyrosinase-catalyzed synthesis of soy 7S/11S–phlorizin conjugates was performed, and the reaction sites, conformation alterations and functional properties of complexes were evaluated using proteomic, in combination with multispectral technologies. Phlorizin was conjugated to 7S/11S primarily via residues of Lys, Cys, His and Arg residues. The phlorizin binding equivalents and decreased contents of free and total sulfhydryl groups and free amino groups confirmed the covalent interaction in the 7S/11S–phlorizin complexes. Conjugation with phlorizin promoted the conversion of α-helix to β-sheet and β-turn, with simultaneous transformation of the microenvironments around Trp and Tyr residues to hydrophilic and hydrophobic microenvironments, respectively, and lowering of the surface hydrophobicity of 7S/11S. The DPPH and ABTS radical scavenging abilities and α-glucosidase inhibitory activities of 7S/11S were increased by three–, two– and three–fold after the covalent binding of phlorizin. The study provided an ideal tyrosinase-catalyzed approach to fabricate custom–tailored nutritional soy protein–polyphenol products.

Investigating the role of tartaric acid in wine astringency

Previous studies acknowledged that tartaric acid-imparted low-pH contributed to the enhancement of astringency, but in-depth studies are lacking and the underlying mechanisms are not clearly understood. This work introduced new insight into the effect of tartaric acid on astringency perception from the perspectives of complex formation, protein secondary structure, chemical bond type and salivary layer fluidity by establishing models using proteins (α-amylase, salivary proteins) and tannic acid. Results demonstrated that tartaric acid affects wine astringency by two mechanisms: a) Tartaric acid compound directly affects the wine astringency by forming ternary complexes and causing the protein structure to stretch by changing the hydrogen bond and hydrophobic bond between protein–polyphenol complexes. b) pH affected astringency by increasing the fluidity of the salivary layer rather than increasing the consumption of the salivary layer. The findings provide valuable information to the wine industry to regulate wine astringency by the management of tartaric acid.

Molecular interaction mechanism and structure–activity relationships of protein–polyphenol complexes revealed by side-directed spin labeling-electron paramagnetic resonance (SDSL-EPR) spectroscopy

Deciphering interactions between bioactive protein and polyphenols are critical for designing and controlling functional protein–polyphenol complexes. Herein, using the site-directed spin labeled T4 lysozyme (T4L) and rosmarinic acid (RA) as a model system, we combined electron paramagnetic resonance spectra to investigate molecular interaction mechanism of the protein–polyphenol complexes in structural or conformational details. Experimental results show that molecular interactions between T4L and RA are a process from order to disorder. TEM images display that the complexes finally assemble into quasi-spherical colloidal particles. When T4L/RA ratio is 1:1, the complexes exhibit the optimized enzymatic and antioxidant dual-functionalities due to the synergetic effect and protection mechanism. However, with excess addition of RA, the enzymatic and antioxidant activities of the complexes started to attenuate because the catalytic active site and bioactive hydroxyl groups were buried. The revealed high-resolution interaction process could help better understand the corresponding alterations between structure and functionalities.

Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate-EGCG Molecular Complexes.

Highlights Pea protein isolate (PPI) and EGCG spontaneously formed complexes.Protein–polyphenol complexation was mainly driven by hydrogen bonding.The binding of EGCG influenced the structure and functionality of PPI.PPI-EGCG complexes had better emulsifier properties than PPI. There is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein isolate (PPI) dispersions using a combined pH-shift/heat treatment method, and then, prepared PPI-epigallocatechin-3-gallate (EGCG) complexes under neutral conditions. Spectroscopy, calorimetry, molecular docking, and light scattering analysis demonstrated that the molecular complexes formed spontaneously. This was primarily ascribed to hydrogen bonds and van der Waals forces. The complexation of EGCG caused changes in the secondary structure of PPI, including the reduction in the α-helix and increase in the β-sheet and disordered regions. These changes slightly decreased the thermal stability of the protein. With the accretion of EGCG, the hydrophilicity of the complexes increased significantly, which improved the functional attributes of the protein. Optimization of the PPI-to-EGCG ratio led to the complexes having better foaming and emulsifying properties than the protein alone. This study could broaden the utilization of pea proteins as functional ingredients in foods. Moreover, protein–polyphenol complexes can be used as multifunctional ingredients, such as antioxidants or nutraceutical emulsifiers.

Physicochemical Characterization of Interactions between Blueberry Polyphenols and Food Proteins from Dairy and Plant Sources.

Polyphenols are widely known for their benefits to human health; however, dietary intake of this class of compounds is low in the United States due to low intake of fruits and vegetables. Dairy foods (i.e., milk, yogurt) have been shown to increase polyphenol bioavailability via protein–polyphenol interactions, which may have important implications for human health. Increasing consumer interest in sustainability and health has led to the introduction of a variety of novel plant-based proteins and related food products as dairy alternatives. This study compared whey, a popular dairy-based food protein, to pea and hemp proteins for their abilities to form complexes with polyphenols from blueberries, which are a widely consumed fruit in the US with demonstrated health effects. Physical and chemical characteristics of each protein extract in the presence and absence of blueberry polyphenols were investigated using a variety of spectroscopic methods. The influence of polyphenol complexation on protein digestion was also assessed in vitro. While all proteins formed complexes with blueberry polyphenols, the hemp and pea proteins demonstrated greater polyphenol binding affinities than whey, which may be due to observed differences in protein secondary structure. Polyphenol addition did not affect the digestion of any protein studied. Solution pH appeared to play a role in protein–polyphenol complex formation, which suggests that the effects observed in this model food system may differ from food systems designed to mimic other food products, such as plant-based yogurts. This study provides a foundation for exploring the effects of plant-based proteins on phytochemical functionality in complex, “whole food” matrices, and supports the development of plant-based dairy analogs aimed at increasing polyphenol stability and bioavailability.

Inhibitory Effect of Guava Leaf Polyphenols on Advanced Glycation End Products of Frozen Chicken Meatballs (-18 °C) and Its Mechanism Analysis.

The inhibitory effect of guava leaf polyphenols (GLP) on advanced glycation end products (AGEs) of frozen chicken meatballs (−18 °C) and its possible inhibitory mechanism was investigated. Compared with control samples after freezing for 6 months, acidic value (AV), lipid peroxides, thiobarbituric acid reactive substance (TBARS), A294, A420, glyoxal (GO), Nε-carboxymethyl-lysine (CML), pentosidine, and fluorescent AGEs of chicken meatballs with GLP decreased by 11.1%, 22.3%, 19.5%, 4.30%, 8.66%, 8.27%, 4.80%, 20.5%, and 7.68%, respectively; while free sulfhydryl groups the content increased by 4.90%. Meanwhile, there was no significant difference between meatballs with GLP and TP in AV, A294, GO, and CML (p > 0.05). Correlation analysis indicated that GO, CML, pentosidine, and fluorescent AGEs positively correlated with AV, TBARS, A294, and A420, while GO, CML, pentosidine, and fluorescent AGEs negatively correlated with free sulfhydryl groups. These results manifested GLP could inhibit AGEs formation by inhibiting lipid oxidation, protein oxidation, and Maillard reaction. The possible inhibitory mechanism of GLP on the AGEs included scavenging free radicals, capturing dicarbonyl compounds, forming polyphenol–protein compounds, and reducing the formation of glucose. Therefore, the work demonstrated that the addition of plant polyphenols may be a promising method to inhibit AGEs formation in food.

Encapsulation of β-carotene in high internal phase Pickering emulsions stabilized by soy protein isolate – epigallocatechin-3-gallate covalent composite microgel particles

• Covalently conjugated SPI-EGCG microgel particles were used to stabilize HIPPEs. • EGCG addition improved the functional properties of β-carotene-loaded HIPPEs. • Thick particle layer and gel network jointly promoted the stability of HIPPEs. • Encapsulation of β-carotene enhanced the chemical stability and bioaccessibility. In the current study, soy protein isolate (SPI) and epigallocatechin-3-gallate (EGCG) covalent composite microgel particles with antioxidant capacity were prepared and the particles was used as β-carotene-loaded high internal phase Pickering emulsions (HIPPEs) stabilizers. The covalent binding of SPI-EGCG altered the structures of the SPI through an unfolding of the polypeptide chain. Moreover, compared to HIPPEs stabilized by SPI alone, HIPPEs stabilized by SPI-EGCG microgel particles showed smaller particle size, higher apparent viscosity, and better stability. Microstructure of the fabricated HIPPEs results revealed that SPI-EGCG covalent conjugates promoted the formation of a thick and dense protective layer on the surfaces of oil droplets. Furthermore, β-carotene-loaded HIPPEs stabilized by SPI-2% EGCG microgel particles exhibited a higher retention rate after 42 days of storage and better bioaccessibility (86.64 ± 0.27% and 54.43 ± 0.50%, respectively) compared to HIPPEs stabilized by SPI (75.80 ± 0.49% and 38.31 ± 0.93%, respectively). The current study illustrated that the design of HIPPEs stabilized with protein–polyphenol composite particles were of great importance for the delivery of lipophilic bioactive compounds.

Ultrasound-assisted preparation of lactoferrin-EGCG conjugates and their application in forming and stabilizing algae oil emulsions

The aim of this study was to prepare lactoferrin-epigallocatechin-3-gallate (LF–EGCG) conjugates and to determine their ability to protect emulsified algal oil against aggregation and oxidation. LF–EGCG conjugates were formed using an ultrasound-assisted alkaline treatment. The ultrasonic treatment significantly improved the grafting efficiency of LF and EGCG and shortened the reaction time from 24 h to 40 min. Fourier transform infrared spectroscopy and circular dichroism spectroscopy analyses showed that the covalent/non-covalent complexes could be formed between LF and EGCG, with the CO and CN groups playing an important role. The formation of the conjugates reduced the α-helix content and increased the random coil content of the LF. Moreover, the antioxidant activity of LF was significantly enhanced after conjugation with EGCG. LF–EGCG conjugates as emulsifiers were better at inhibiting oil droplet aggregation and oxidation than LF alone. This study demonstrates that ultrasound-assisted formation of protein–polyphenol conjugates can enhance the functional properties of the proteins, thereby extending their application as functional ingredients in nutritionally fortified foods.

Insights into Polyphenol-Lipid Interactions: Chemical Methods, Molecular Aspects and Their Effects on Membrane Structures.

Plant polyphenols have many potential applications, for example, in the fields of chemical ecology and human and animal health and nutrition. These biological benefits are related to their bioavailability, bioaccessibility and interactions with other biomolecules, such as proteins, lipids, fibers and amino acids. Polyphenol–protein interactions are well-studied, but less is known about their interactions with lipids and cell membranes. However, the affinity of polyphenols for lipid bilayers partially determines their biological activity and is also important from the usability perspective. The polyphenol–lipid interactions can be studied with several chemical tools including, among others, partition coefficient measurements, calorimetric methods, spectroscopic techniques and molecular dynamics simulation. Polyphenols can variably interact with and penetrate lipid bilayers depending on the structures and concentrations of the polyphenols, the compositions of the lipids and the ambient conditions and factors. Polyphenol penetrating the lipid bilayer can perturb and cause changes in its structure and biophysical properties. The current studies have used structurally different polyphenols, diverse model lipids and various measuring techniques. This approach provides detailed information on polyphenol–lipid interactions, but there is much variability, and the results may even be contradictory, for example, in relation to the locations and orientations of the polyphenols in the lipid bilayers. Nevertheless, by using well-characterized model polyphenols and lipids systematically and combining the results obtained with several techniques within a study, it is possible to create a good overall picture of these fascinating interactions.

Effects of modified atmosphere packaging on the postharvest quality of mulberry leaf vegetable

Fresh mulberry leaf vegetable is nutritive and becoming popular. However, available preservation technologies are deficient. In present work, the effects of two kinds of modified atmosphere packaging on postharvest quality of fresh mulberry leaf vegetable stored at 4 °C were evaluated. The respiration rate of samples in the modified polyethylene packages (MP20) was 12.88–22.65% lower than that in normal polyethylene packaging (CK). The content of total soluble solids, soluble protein, and total polyphenol in MP20 was less changed than that in CK, and the vitamin C retention was higher as well. Moreover, the lignin content in MP20 was lower than that in CK during storage (19.79% vs 13.38% at day 8), and that was significantly positively related to the polyphenol oxidase and peroxidase activities inhibition. Taken together, a packaging with moderate gas permeability (MP20) is suitable for nutrition maintenance and lignification inhibition of fresh mulberry leaf vegetable during cold storage.

Effect of Lonicera edulis polysaccharide on reducing oral dyeing of lonicera edulis juice

Fluorescence spectroscopy, particle size determination, and potential analysis were exploited to elucidate the effect of Lonicera edulis polysaccharide on polyphenol protein. The results revealed that Lonicera edulis polysaccharides mediated the binding of polyphenols and proteins through competition and formation of ternary complexes and were also able to enhance the stability of the polyphenol-protein complex solution system. A certain electrostatic effect was also present in the process simultaneously. As confirmed by the dyeing test, to improve oral dyeing, the optimum conditions of adding polysaccharide, pectin, and casein were as follows: the dosage of the polysaccharide group was 1.2 mg/mL, coloring time was 100 min, pH value was 4.0. Pectin group added 0.8 mg/mL with coloring time 80 min, pH 5.0. The addition of casein was 1.2 mg/mL; the coloring time was 100 min with pH 5.0. The sample juice substantiated a significant improvement in the dyeing of porcine tongue mucosa. Under the optimal conditions, microscopic observation validates that the mucosal color of the porcine tongue epidermis was closer to that of unstained porcine tongue epidermis, which significantly improved astringency and oral staining.

Characterisation of whey protein–polyphenol conjugates prepared by the noncovalent and covalent methods for their effect on the functional properties of whey proteins

Whey proteins were conjugated with polyphenols (caffeic and ferulic acid) using different methods viz. noncovalent (pH 3, 5 and 7) and covalent (alkaline, chemical coupling and free radical grafting method). The binding of polyphenols was higher in the covalent conjugates (maximum in free radical grafting) than the noncovalent conjugates (maximum seen at pH 7). The conjugation was confirmed by decreased intrinsic fluorescence intensity (>30%), increased UV–visible absorbance and changed intensity of peaks in amide I region of Fourier transform infrared spectroscopy (FTIR). The conjugates that were prepared by the covalent (free radical grafting) and noncovalent (pH 7) methods exhibited much better emulsifying activity and emulsion stability than the alkaline conjugates for both caffeic and ferulic acid.

Crumpled Globule-Heterotextured Polyamide Membrane Interlayered with Protein–Polyphenol Nanoaggregates for Enhanced Forward Osmosis Performance

Surface modulation of polyamide structures and the development of nanochanneled membranes with excellent water transport properties are crucial for the separation performance enhancement of thin-film composite membranes. Here, we demonstrate the fabrication of a modular nanochannel-integrated polyamide network on a nanoporous interlayer membrane comprising Mxene-reinforced protein-polyphenol nanoaggregates. The research indicates that the confined growth of the polyamide matrix inside this hydrophilic sub-10 nm nanochannel nanoporous intermediate layer stiffened the interfacial channels, leading to the formation of a polyamide layer with a spatial distribution of a network of unique 3D crumpled globule-like nanostructures. The high specific surface area of such a morphology bestowed the membrane with increased filtration area while facilitating the nanofluidic transport of water molecules through the nanochanneled membrane structure, leading to enhanced water flux of up to 26.6 L m-2 h-1 (active layer facing the feed solution) and 41.0 L m-2 h-1 (active layer facing the draw solution) using 1.0 M NaCl as the draw solution. The membrane equally exhibited good treatment for organic solvent forward osmosis filtration and typical seawater desalination. Moreover, the hierarchical nanostructures induced antimicrobial activity by effectively reducing the biofilm formation of Gram-negative Escherichia coli bacteria. This work provides significant insights into the interfacial engineering and compatibility of the nanomaterials and the polymers in interlayer mixed-matrix membranes, which are environmentally sustainable and cost-effective for the fabrication of advanced forward osmosis membranes for water purification and osmotic energy applications.

Synergy between machine learning and natural products cheminformatics: Application to the lead discovery of anthraquinone derivatives.

Cheminformatics utilizingmachine learning (ML) techniques have opened up a new horizon in drug discovery. This is owing to vast chemical space expansion with rocketing numbers of expected hits and lead compounds that match druggable macromolecular targets, in particular from natural compounds. Due to the natural products' (NP) structural complexity, uniqueness, and diversity, they could occupy a bigger space in pharmaceuticals, allowing the industry to pursue more selective leads in the nanomolar range of binding affinity. ML is an essential part of each step of the drug design pipeline, such as target prediction, compound library preparation, and lead optimization. Notably, molecular mechanic and dynamic simulations, induced docking, and free energy perturbations are essential in predicting best binding poses, binding free energy values, and molecular mechanics force fields. Those applications have leveraged from artificial intelligence (AI), which decreases the computational costs required for such costly simulations. This review aimed to describe chemical space and compound libraries related to NPs. High-throughput screening utilized for fractionating NPs and high-throughput virtual screening and their strategies, and significance, are reviewed. Particular emphasis was given to AI approaches, ML tools, algorithms, and techniques, especially in drug discovery of macrocyclic compounds and approaches in computer-aided and ML-based drug discovery. Anthraquinone derivatives were discussed as a source of new lead compounds that can bedeveloped using ML tools for diverse medicinal uses such as cancer, infectious diseases, and metabolic disorders. Furthermore, the power of principal component analysis in understanding relevant protein conformations, and molecular modeling of protein-ligand interaction were also presented. Apart from being a concise reference for cheminformatics, this review is a useful text to understand the application of ML-based algorithms to molecular dynamics simulation and in silico absorption, distribution, metabolism, excretion, and toxicity prediction.

Ultrasound-assisted assembly of β-lactoglobulin and chlorogenic acid for non covalent nanocomplex: fabrication, characterization and potential biological function

It is essential to understand the ultrasound-induced changes in assembly of proteins and polyphenols into non covalent nanocomplex. β-Lactoglobulin (LG) and chlorogenic acid (CA) with various biological activities can be combined to form food-grade nanocomplexes. This study systematically explored the role of high-intensity ultrasound pretreatment on the binding mechanisms of LG and CA, and the potential biological function for embedding curcumin (Cur). The scanning electron microscopy (SEM) revealed that ultrasound treatment could destroy the structure of LG, and the particle size of the protein was reduced to<50 nm. The change in secondary structure of the protein by ultrasound treatment could be revealed by the fourier transform infrared (FTIR) and fluorescence spectra. Besides, it was found that LG and CA were combined to form a complex under the hydrophobic interaction, and CA was bound in the internal cavity of LG with a relatively extended conformation. The result demonstrated that the ratio of Cur embedded in the ultrasonic sample could be effectively increased by 7% − 10%, the particle size in the emulsion was smaller, and the dispersion was more stable. This work contributes to the development of protein–polyphenol functional emulsion systems with the ability to deliver Cur.

Insights into interactions between food polyphenols and proteins: An updated overview

Polyphenols are widely distributed natural products, investigated intensively due to their health-beneficial effects and prevention of several human diseases. It is well known that polyphenols can easily form complexes with proteins in food processing and human digestion, leading to changes in the conformation and functionality of polyphenols and proteins. On the basis of dividing the common polyphenols into flavonoids, phenolic acids, and tannins, this paper reviews the progress and application of polyphenol–protein interactions during the past decade. Accordingly, this review might provide a better understanding on the mechanism of polyphenol–protein interactions, which is expected to provide guidance for food processing and studying on health effects of polyphenol compounds in the future. Novelty impact statement The interactions of flavonoids, phenolic acids, and tannins with proteins were reviewed. Reversible interactions are the main form of polyphenol–protein interactions, which are mainly attributed to hydrogen and hydrophobic bonding. Besides, the health effects of polyphenol–protein complexes mainly include the inhibition of protease and toxic protein aggregation.