To broaden the utilization of soybean protein isolate (SPI), electroactivation-treated SPI (EAP) was combined with naringin (NAR) to form protein-polyphenol complexes (EAP-N), and their structural and functional properties were investigated. EA treatment induced SPI unfolding, reduced particle size, and increased absolute zeta potential. After NAR addition, relatively stable EAP-N complexes were formed. At 0.6 mg/mL NAR, the complex showed the highest solubility (77.01%). Compared with SPI, EAP-N complexes also exhibited enhanced antioxidant activity and improved interfacial properties. Molecular forces and Molecular docking revealed that the modified EAP increased the binding sites with NAR, and the interactions between them were manly non-covalent (hydrogen bonds/hydrophobic interactions). These findings indicate that EAP-N complexes have potential as functional protein-polyphenol ingredients for emulsion and foam-based food systems.
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
Macadamia protein isolate (MPI) is a promising plant-based protein but its poor emulsifying functionality limits broader applications. This study investigated the interaction mechanisms between MPI and procyanidin dimer (PA2) and their synergistic effect on the stabilization of high internal phase Pickering emulsions (HIPPEs). Spectroscopic and physicochemical analyses demonstrated that MPI and PA2 formed complexes through a spontaneous binding process mainly driven by hydrogen bonding, accompanied by hydrophobic interactions. These interactions induced notable conformational changes in MPI, leading to a reduced particle size, enhanced surface charge, and modified hydrophobicity. Moreover, MPI-PA2 complexes significantly enhanced interfacial activity by efficiently adsorbing at the oil-water interface. Consequently, HIPPEs stabilized by the complexes exhibited smaller droplet sizes, improved physical stability, and superior viscoelastic properties. Overall, this work highlights the potential of MPI-PA2 complexes as a promising bio-based emulsifier and functional delivery system, providing new insights into the value-added utilization of plant proteins in food applications.
This study investigated betacyanin stabilization from red dragon fruit peel using integrated computational and experimental approaches. HPLC identified betanin and phyllocactin as primary components. Density Functional Theory (DFT) screened molecular interactions, identifying sodium alginate (SA) and low-methoxyl pectin (LMP) as wall materials due to strong binding affinities. Consequently, maltodextrin (MD) composites with SA or LMP (1-3% w/v) were freeze-dried. Experimental results support the DFT screening trends; MD-SA2 and MD-LMP2 achieved higher betacyanin content (93.81 and 88.00 mg/100 g, respectively) than the MD control (77.93 mg/100 g). FTIR confirmed interactions consistent with optimized DFT structures. Thermal degradation (60-80 °C) followed first-order kinetics (R2 > 0.98). Encapsulated betacyanins showed high stability at 80 °C (t₁/₂ = 26.41-26.87 min), outperforming the non-encapsulated betacyanins. High retention (>94%) was maintained during pasteurization (72 °C, 15 s). These findings demonstrate that molecularly guided ionic hydrocolloid systems show potential to protect sensitive pigments during thermal food processing.
Nuttamon Artharn, R. Chanajaree, S. Puangpraphant· Food Chemistry· 0 citations
Population aging has made sarcopenia a growing concern in geriatric health. Protein–polyphenol non-covalent complexes can serve as carrier systems that improve the stability and bioactivity of natural antioxidants. This study refined the preparation parameters for the non-covalent complex of whey protein isolate (WPI) and resveratrol (RES), achieving protein digestibility of 83.60 ± 0.50% and DPPH scavenging of 52.41 ± 0.58% at pH 7.0, a WPI:RES molar ratio of 1:1, and a reaction time of 1.5 h. Relative to free WPI, the complex improved DPPH scavenging by 21.66% while preserving protein digestibility. The binding mode, interaction forces, and conformational evolution were investigated via spectroscopic experiments, docking studies and molecular dynamics simulations. RES selectively bound to the surface of β-lactoglobulin in WPI through hydrophobic interactions and hydrogen bonding, with a docking score of −6.366 kcal/mol and an MM-GBSA binding free energy of −30.48 kcal/mol. The complex maintained a highly stable conformation throughout the 100 ns molecular dynamics simulation. In conclusion, this study elucidated the structural changes of WPI upon non-covalent resveratrol binding. The WPI-RES complex exhibited enhanced DPPH radical scavenging activity while preserving protein digestibility, with potential implications for functional food development in sarcopenia management.
This study aimed to explore benzoic acid (BA) as a ligand for interaction with soy protein isolate (SPI) by molecular docking. First, BA‐incorporated SPI films were prepared by the solution casting method with different contents of BA (1% to 5% w.r.t. 7% SPI) followed by structural characterization by FTIR spectroscopy. FTIR results showed change in the intensity of the peaks at around 802 and 1540 cm
−1
. X‐ray diffraction analysis showed that BA‐incorporated SPI films primarily have an amorphous structure with no observable crystalline peaks of BA. From the material properties data, it can be concluded that 2% BA content is optimum for uniform dispersion. Thermal analysis revealed improved stability at lower BA concentration and transmittance studies of the films indicated better optical clarity and UV‐resistance. In silico docking analysis was carried out by BIOVIA Discovery Studio Client to evaluate the roles of covalent and non‐covalent forces acting between BA and SPI. Additionally, CB‐Dock2 was used to predict the 3D structure of a protein and a ligand and also to validate the docking results. Molecular dynamics simulation over 100 ns further validated the docking findings, with Hit_C3 identified as the most stable binding complex based on RMSD, RMSF, and SASA analysis.
Dibyankar Barik, P. Rani, P. Yadav et al.· ChemistrySelect· 0 citations
Soy protein isolate (SPI) is widely used as a plant protein ingredient. This study modified SPI by ultrasound-assisted laccase treatment (U + La; 150, 300, 450, and 600 W), evaluated its functional properties, and further analyzed the related physicochemical and structural changes. SPI treated with 300 W ultrasound and laccase (UL3) showed the best overall functionality, with the highest water-holding capacity (93.39%), emulsion stability index (42.60 ± 2.24 min), and foaming capacity (169.29%). UL3 also showed a relatively small particle size (362.80 nm) and the highest absolute zeta potential (27.78 mV). Electrophoretic and chromatographic analyses indicated increased high-molecular-weight aggregates after U + La treatment. Spectroscopic and microstructural results suggested that moderate U + La treatment was associated with SPI conformational changes and a compact gel network. Overall, UL3 improved SPI model functionality and showed application potential as a modified plant protein ingredient.
Jiaxin Guo, Qinggang Xie, Yilin Sun et al.· Food Research International· 1 citation
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.
