Aug 2026· Food Chemistry· Vol 527, pp.
150861
· 0 citations· 49 references
Medicine
Abstract
This study elucidates the non-covalent interaction mechanism between hemp seed globulin (GLB), a plant protein rich in arginine, and tannic acid (TA) via combined multispectral analysis and molecular simulations. TA adopts an amphipathic binding mode within a defined GLB pocket, driven mainly by hydrophobic forces and supplemented by hydrogen bonds and arginine-mediated cation-π interactions, which collectively drive an entropy-favorable spontaneous binding process (ΔH > 0, ΔS > 0). TA binding drives localized secondary structural adjustments and enhances conformational compactness of GLB. The resulting GLB-TA complex exhibits significantly improved antioxidant activity and emulsifying properties, alongside reduced in vitro digestibility. This work elucidates a specific interaction paradigm between high-arginine plant globulins and hydrolysable polyphenols, providing a mechanistic basis for clean-label plant protein modification and supporting sustainable functional food development, aligned with UN SDGs 3 (Good Health and Well-being) and 12 (Responsible Consumption and Production).
Interactions between food processing-derived components and food proteins can markedly alter protein conformation and functional properties. Among them, cooking oil fume particles (COFPs) are widespread contaminants from high-temperature Chinese cooking. This study first compared the effects of COFPs from four common edible oils (rapeseed, RCOFPs; soybean, SCOFPs; corn, CCOFPs; and lard, LCOFPs) on the OVA structure and function. Physicochemical assays showed that all COFPs triggered OVA aggregation (particle size increased from 0.48 to 896.86 nm) and reduced zeta potential, driving an ordered secondary structure remodeling with distinct component-specific patterns. RCOFPs enriched in polycyclic aromatic hydrocarbons (especially fluoranthene, stably binding OVA at -7.9 kcal mol-1 through hydrophobic bonds) may be related to β-sheet enrichment, which directly promoted allergenic epitope exposure and resulted in enhanced IgE/IgG binding and KU812 cell degranulation. High-peroxide LCOFPs promoted disulfide bond formation and α-helix elevation, inducing compact conformational remodeling that enhanced OVA's gastrointestinal digestion resistance. Pearson analysis revealed a potential structure-function relationship. Soybean oil and corn oil exhibited weaker effects on the nutritional functionality of OVA than the other tested oils under the present experimental conditions. These findings clarify the regulatory effects of thermal processing contaminants on the health-related properties of food proteins, providing scientific guidance for the selection of edible oil in Chinese cooking and the nutritional and safety control of thermally processed egg products.
This study utilized ultrasound-assisted technology to form non-covalent complexes of polyphenols with Millettia speciosa by-product protein, offering a sustainable strategy for its use in functional foods and biomaterials.
Meng Wang, Jiexi Li, Feng Li et al.· Food Chemistry· 0 citations
Fungal proteins face poor processing functionality and low digestibility limiting their use in emulsified and structured foods. Here, Morchella esculenta protein (MP) was modified by ferulic acid (FA) and chlorogenic acid (CA) at 0.0375-1 mg/mL. Both phenolics bound MP concentration-dependently, CA exhibited stronger binding affinity (Ka = 3.242 × 106 L/Mol) and deeper conformational rearrangement, while FA relied on hydrophobic and π-π interactions. Moderate phenolic addition maximized MP performance: EAI rose from 2.44 to 3.99 m2/g and digestibility from 45.33% to 58.31%, with CA delivering superior antioxidant capacity (DPPH scavenging 69.67%). Excess phenolics triggered severe protein aggregation and weakened interfacial stability. This work clarifies structure-dependent differential regulation of MP by two phenolics, defines optimal concentration thresholds, and provides theoretical support for clean-label fungal protein food ingredients.
Ying He, Z. Rao, Ziang Tian et al.· Food Research International· 0 citations
Plant protein fibrils have gained increasing attention as promising delivery carriers for hydrophobic bioactive compounds. In this study, perilla seed protein fibrils (PSPF) prepared via acid-heat induced self-assembly were used to systematically investigate the non-covalent interactions with four structurally different polyphenols (quercetin, luteolin, naringenin, and curcumin) at pH 3.5. The functional properties and delivery potential of the non-covalent complexes were also evaluated. Thermodynamic analysis and molecular docking demonstrated that hydrogen bonds, van der Waals forces, and hydrophobic interactions dominated the non-covalent binding of PSPF toward polyphenols. Particle size and transmission electron microscopy demonstrated polyphenol complexation mediated PSPF assembly and facilitated the formation of network structures, and the PSPF-quercetin complex (PSPF-Q) possessed the maximum particle size of 690.53 nm. Fourier transform infrared spectroscopy suggested that non-covalent binding of polyphenols strengthened structural ordering of PSPF and promoted the transition from intermolecular (decreased from 72.07% to 54.77%-70.18%) to intramolecular hydrogen bonds (increased from 27.93% to 29.82%-45.23%). Furthermore, quercetin exhibited strong binding affinity toward PSPF (-7.645 kcal/mol) owing to its abundant phenolic hydroxyl groups. For PSPF-Q, the emulsifying activity index and emulsifying stability index increased by 28.91% and 33.60%, respectively; foaming capacity and foaming stability were elevated by 18.23% and 208.68%; and DPPH, ABTS and FRAP antioxidant capacities were enhanced by 296.97%, 267.26% and 170.20%. In vitro digestion results revealed that PSPF effectively achieved sustained intestinal controlled release of encapsulated polyphenols. These findings offer theoretical and experimental support for the design and application of protein fibrils in polyphenol delivery systems.
Xiquan Li, Shaohua Chen, Guangyu Xu et al.· Food Research International· 0 citations
A supramolecular pigment (Croc-Na2GA) was developed by the self-assembly of crocetin and disodium glycyrrhizinate using resonant acoustic mixing (RAM) technology for meat-coloring applications. The resulting complex formed stable nanomicelles (197.30 nm) that exhibited enhanced solubility and robust stability across pH 8–13 and under thermal processing conditions. Molecular docking confirmed strong binding affinities with myofibrillar proteins, including myoglobin, actin, and myosin, thereby facilitating pigment retention within meat matrices. Application in chicken patties produced a stable golden-yellow hue with sensory attributes comparable to those of commercial gardenia yellow. Notably, Croc-Na2GA demonstrated potent antioxidant capacity and significantly reduced the formation of hazardous Maillard reaction byproducts, decreasing 5-HMF and NDMA levels by approximately 50% after reheating. This bio-based nanosystem provides a multifunctional, clean-label colorant for enhanced meat products.
Lotus rhizome starch (LS) has limited application owing to its high digestibility and pronounced retrogradation tendency. To elucidate how hydrocolloid molecular architecture regulates LS functionality after gelatinization, fully gelatinized LS was blended with pre-hydrated xanthan gum (XG), flaxseed gum (FG), guar gum (GG), or carrageenan (CA). Multiscale structural and functional analyses, including microstructure, nanoscale morphology, rheology, and water distribution, were performed to evaluate the ability of hydrocolloids to spatially integrate with the gelatinized LS matrix and organize coherent networks. XG formed a highly integrated interpenetrating network that effectively restricted molecular mobility and enzyme accessibility, resulting in improved control of starch digestion. FG generated a heterogeneous yet stable network that enhanced structural confinement and water regulation, leading to the strongest inhibition of retrogradation and increased resistant starch formation. In contrast, GG formed a weaker network with limited effects on digestion regulation, whereas CA exhibited poor integration with the LS matrix because of phase separation. These findings demonstrate that the functional performance of hydrocolloids is determined by the combined effects of molecular architecture and their ability to integrate with the gelatinized starch matrix, providing a structural basis for designing starch-based foods with improved storage stability and tailored digestibility.
Rui-Bing Duan, Yassin Haran, Jie Li et al.· International Journal of Bio...· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.
