Enzymatic Construction of Whey Protein-Arabinoxylan Conjugate Particles and Their Regulation on the Stability and Curcumin Delivery Property of High Internal Phase Pickering Emulsions

Chitosan–cinnamaldehyde–whey protein concentrate stabilized W1/O/W2 double emulsion for co-encapsulation of tea polyphenols and β-carotene

Development and Stability Evaluation of Oleogel-in-Water Emulsions Using Whey Protein Isolate–Ferulic Acid Nanoparticles for Ganoderma Lucidum Spore Oil Encapsulation

This work evaluated how ferulic acid (FA) impacted the conformational properties of whey protein isolate (WPI) and altered the environmental tolerance of oleogel/water (Og/W) emulsions formulated with Ganoderma lucidum spore oil (GLSO). Molecular dynamics simulation analyses revealed that FA interacted with α-lactalbumin via hydrogen bonding and hydrophobic interactions, whereas it bound into the hydrophobic cavity of β-lactoglobulin through a “lock-and-key” mode driven primarily by hydrophobic forces. Fourier transform infrared spectroscopy analysis verified that such non-covalent forces triggered the dissociation and structural extension of WPI, which was manifested as a significant loss of α-helix and β-sheet architectures along with a corresponding rise in random coils. FA addition increased the positive charge, mean droplet size, interfacial contact angle and antioxidant stability of WPI-FA nanoparticles when the WPI-to-FA ratio exceeded 1:2 (i.e., WPI was in excess relative to FA). The GLSO-based Og/W emulsions exhibited a weak gel structure with predominantly elastic characteristics. Furthermore, WPI-FA nanoparticles fabricated at a 2:1 ratio minimized emulsion droplet size and imparted optimal stability to the Og/W emulsions, demonstrating superior freeze–thaw and salt resistance, alongside suppressed GLSO flavor release. This work provides critical insights into tailoring protein-polyphenol interactions to stabilize GLSO-based Og/W emulsion delivery systems for food applications.

Pickering emulsions for intelligent curcumin delivery: Synergistic stabilization by starch nanocrystals and soy β-conglycinin or glycinin.

Starch nanocrystals (SNCs) derived from rice starch were complexed with soybean β-conglycinin (7S) or glycinin (11S) to develop food-grade Pickering emulsifiers for curcumin delivery. The effects of the SNC-to-protein mass ratio on particle structure, interfacial properties, emulsion stability, and gastrointestinal digestion were systematically evaluated. At an SNC-to-protein mass ratio of 1:1, the SNCs-7S and SNCs-11S complexes exhibited the smallest particle sizes of 110 ± 4 and 234 ± 6 nm, respectively. Their three-phase contact angles approached 90°, indicating favorable interfacial wettability. SNCs induced concentration-dependent fluorescence quenching of 7S and 11S, with maximum quenching efficiencies of 61.02 ± 1.41% and 37.51 ± 1.09%, respectively. Raman spectroscopy and molecular docking analyses indicated that complex formation involved rearrangements of the protein secondary structure and hydrogen bonding. All calculated binding energies were below -6.0 kcal/mol, with the lowest value of -6.5 kcal/mol observed for SNCs-11S. Pickering emulsions containing 60% soybean oil exhibited shear-thinning and predominantly elastic behavior (G' > G″). The 1:1 composite systems formed the strongest network structures and exhibited no evident creaming, flocculation, or oiling-off after storage at 4 °C for 30 days. The SNCs-7S emulsion achieved a curcumin encapsulation efficiency (EE) and loading capacity of 90% and 7.5%, respectively, exceeding the corresponding values of 86% and 6.0% obtained for the SNCs-11S emulsion. After intestinal digestion, free fatty acid release from the SNCs-7S and SNCs-11S emulsions reached 46.31 ± 2.71% and 40.68 ± 0.71%, respectively. Overall, the 1:1 SNCs-7S system exhibited the most favorable interfacial assembly, storage stability, curcumin encapsulation, and lipid digestibility.

Evaluation of the structure and function of whey protein concentrate combined with folic acid and l-ascorbyl 6-palmitate.

BACKGROUND Whey protein concentrate 80 (WPC80) represents a highly promising carrier for bioactive compounds; however, the structural and functional consequences resulting from its noncovalent interactions with folic acid (FA) and l-ascorbic acid 6-palmitate (LAP) remain incompletely understood. Hence, it is of practical importance to elucidate the effects of FA and LAP on the structural, functional, and physicochemical properties of WPC80, and to assess potential applications. RESULTS By constructing ternary complexes of WPC80-FA/LAP, the study characterized protein conformational changes using techniques including three-dimensional fluorescence spectroscopy, surface hydrophobicity, protein flexibility, free sulfhydryl content, and SDS-PAGE. In addition, foaming and emulsifying properties were measured, while processing stability and digestive release behavior were evaluated through spray drying and in vitro simulated gastrointestinal digestion. The results demonstrate that FA/LAP renders the structure of WPC80 more compact, reduces particle size, and promotes the conversion of tryptophan to N-formylkynurenine. Moreover, surface hydrophobicity was reduced by up to 63.07%, free sulfhydryl groups decreased by 14.07 μmol g-1 protein, and protein flexibility increased by 30.88%. Furthermore, FA and LAP significantly improved the interfacial properties of WPC80, enhancing its foaming capacity, emulsifying activity, and stability. In vitro digestion studies revealed FA release rates of 22.83-28.74% in the gastric phase and 62.86-84.69% in the intestinal phase, with strong antioxidant activity maintained post-digestion. CONCLUSION This research elucidates the molecular and functional mechanisms of ligand-protein interactions, providing crucial theoretical and technical insights for developing protein-based FA-fortified food systems. © 2026 Society of Chemical Industry.

Temperature-mediated assembly of quinoa protein-κ-carrageenan soluble complexes for stabilizing high internal phase emulsions to improve the intestinal targeted delivery of curcumin.

Temperature is a key factor regulating the assembly and functional properties of protein-polysaccharide complexes and appropriately heat-treated QPI-κC complexes offer a synergistic plant-based platform for the encapsulation, protection, and intestinal delivery of hydrophobic bioactives.

Kinetic and Oxidative Stability of Oil-in-Water Pickering Emulsions Stabilized by Lysozyme-Ferulic Acid Conjugates

The demand for ingredients with natural appeal has driven the development of multifunctional natural emulsifiers. This study aimed to synthesize covalent conjugates of lysozyme (LYS) and ferulic acid (FA) via a free radical reaction and investigate their application in stabilizing soybean oil Pickering emulsions. Conjugate formation was confirmed by SDS-PAGE and FTIR and UV-Vis spectroscopy, indicating alterations in the protein’s tertiary structure. The LYS-FA conjugate exhibited techno-functional properties superior to native lysozyme, including higher emulsifying capacity and antioxidant activity, with inhibition values above 74% for both DPPH and ABTS. Furthermore, in vitro digestion studies demonstrated that conjugation protected FA from degradation in the gastric phase. Oil-in-water Pickering emulsions were prepared with different conjugate concentrations from 2 to 4% w/w in the aqueous phase. The formulation with 4% LYS-FA resulted in an excellent kinetic stability, showing no creaming for 8 days. Rheology revealed pseudoplastic behavior with a predominantly elastic character, where G’ was higher than G’’, suggesting the formation of a robust network at the interface. In addition to physical stability, the Pickering emulsions significantly retarded the primary and secondary lipid oxidation of the encapsulated soybean oil compared to the control, attributed to the interfacial barrier and antioxidant action formed by the conjugate. These results suggest that LYS-FA conjugates are promising candidates as emulsifiers with good techno-functional properties and antioxidant capacity for applications in the food industry.