This study used an anti-solvent precipitation method combined with alkaline heat treatment to prepare hollow nanoparticles (HP) and solid nanoparticles (NP) from soy protein isolate-gliadin (SPI-Gli) mixtures at different ratios. The interactions and structural changes of SPI and Gli during the particle formation process were studied to clarify their functional characteristics and influence on the delivery of naringin (NAR). Results from FTIR, fluorescence spectroscopy, particle size, shell hydrophobicity, surface hydrophobicity, and TEM confirm that HP form hollow spheres with a distinctive hydrophilic-hydrophobic shell structure. Hydrogen bonds, disulfide bonds, and electrostatic interactions are all involved in the assembly process. In contrast, NP present as compact solid spheres, mainly stabilized by hydrophobic interactions, hydrogen bonds, and electrostatic interactions. The high specific surface area and porous hollow structure of HP enable more uniform dispersion in the solution, increase interface adsorption sites, promote the formation of a more uniform and ordered interfacial film, and significantly improve the emulsifying and foaming characteristics of SPI-Gli. When SPI:Gli = 2:1, HP showed the highest emulsifying activity (48.41%), emulsion stability (84.59%), foaming ability (66.67%) and foam stability (95.50%). The hydrophobic inner layer of HP provides hydrophobic binding sites for NAR, while an appropriate amount of Gli optimizes the porosity and mechanical stability of HP. The HP-SPI:Gli = 2:1 sample showed the highest encapsulation efficiency (92.35%), drug loading capacity (18.11 μg/mg), and bioaccessibility (73.93%). This research enhances the applicability of HP within the food domain, laying the groundwork for its implementation in nutrient delivery systems.

This study aimed to address the poor structural stability and limited tunability of the network structure in soy protein isolate (SPI) hydrogels. It systematically investigated the regulatory mechanisms by which the morphology and oxidative modification of different types of nanocellulose (BC, CNF, and CNC) affect SPI conformation and gel properties. The results showed that oxidation successfully introduced aldehyde groups into nanocellulose and altered its surface charge, crystallinity, molecular weight, and microstructure, with oxidized CNF (OCNF) exhibiting the highest aldehyde content (6.997 mmol/g). Compared with native nanocellulose, oxidized nanocellulose showed stronger interactions with SPI, as evidenced by the reduction in free amino group content, increased complex particle size, reduced surface hydrophobicity, and more pronounced protein conformational rearrangement. FTIR, 2D-COS, and XPS further confirmed that hydrogen bonding and Schiff base formation jointly contributed to the construction of the hydrogel network. The composite hydrogels constructed from oxidized nanocellulose and protein exhibited denser network structures and enhanced rheological, mechanical, and thermal stability properties. The S-OCNF hydrogel demonstrated the optimal comprehensive performance, with a compressive strength of 8.25 kPa and a hysteresis energy of 706 J/m3. This study provides a theoretical basis for the design of high-performance natural biopolymer complex hydrogels.

This article explored the effects of acid-heat treatment time (0-32 h) and pH value (2.0-7.0) on the morphological characteristics, aggregation behavior, and foam mechanism of soybean protein fibrils. The analysis results of FTIR, zeta-potential, surface hydrophobicity and free sulfhydryl group content indicated that hydrogen bonding, electrostatic interactions, hydrophobic interactions, and disulfide bonds drove the assembly of protein fibrils. Specifically, acid-heat treatment for 24 h was able to form a large number of high-aspect-ratio semi-flexible fibrils. After heating for 32 h, fibrils formed fibrillar cluster aggregates. With increasing pH, electrostatic interactions governed the structural and morphological evolution. When the pH was increased from 2.0 to 5.0, amorphous aggregation was triggered. At pH 7.0 (SPIF-pH7), electrostatic repulsion partially dissociated the fibrils into short fibrils. This structure enhanced the migration and adsorption efficiency of the protein interface (adsorption capacity, 27.96 %), which was conducive to the formation of a relatively thick viscoelastic film. The foam was evenly distributed, with low coalescence and disproportionation, promoting foam formation and stability. This discovery broke through the traditional understanding that an acidic environment (pH 2.0) was necessary to achieve excellent foaming properties. The application of angel cake showed that 12.5 % SPIF-pH7 instead of egg white could increase the specific volume from 2.37 mL/g to 2.64 mL/g, and the springiness (1.16) was close to that of the control group (1.28). This study provides a theoretical basis for the application of protein fibrils in aerated food system.

Lycii Cortex exhibits significant potential due to its diverse bioactivities and nutritional value; however, the limited research on its polysaccharides has constrained their development and application. To address this, our work focused on the objectives to establish an efficient extraction protocol for Lycii Cortex polysaccharides (LCPs) and evaluate their protective effects against cellular injury relevant to oxidative stress-associated bone loss. We employed ultrasound-assisted extraction and optimized the process using a comparative modeling approach. This involved testing response surface methodology (RSM), support vector regression (SVR), and Gaussian process regression (GPR), and finally integrating them into a Stacking ensemble model. The Stacking model achieved superior predictive accuracy (R2 > 0.95), identifying the optimal extraction parameters: 79 °C, 16 mL/g, 117 min of ultrasonic time, and 3 extraction times, yielding a maximum recovery of 34.97%. Structural analysis showed that the extracted LCPs is a heteropolysaccharide and the molecular weight determined to be 11.2 kDa. Its monosaccharide composition consisted of Man:Rha:GlcA:GalA:Glc:Gal:Ara, with molar ratio of 0.39:2.99:2.50:42.48:36.39:11.88:3.38, and the surface morphology was fragmented. Furthermore, LCPs intervention significantly protected osteoblasts from oxidative stress-induced apoptosis, attenuating oxidative stress-induced apoptosis, mitochondrial dysfunction, and lipid peroxidation. Collectively, this study provides an optimized extraction strategy for LCPs supported by machine learning, details its structural characterization, and establishes its antioxidant efficacy in a relevant cell model. These findings contribute a practical framework for the scalable production and further investigation of LCPs as a potential natural antioxidant agent.

The aim of this study was to investigate the effect of Maillard reaction (MR) and Lactobacillus casei fermentation on the network formation mechanism and structural properties of soybean protein gel (MFP). To achieve this, interaction force analysis, texture profile analysis, moisture distribution assessment, scanning electron microscopy (SEM), and multi-parameter rheological evaluations were employed. Results showed that after 8 h of heating, the grafting degree stabilized, and soy protein isolate (SPI) particle aggregation was most evident by covalent bond aggregation. Disulfide and hydrogen bonds significantly increased (P < 0.05), while hydrophobic interactions decreased. SEM showed that extracellular polysaccharides and other fermentation products, MR products and SPI skeleton formed a closely interconnected “spiderweb-like” network structure. Texture profile analysis, water-holding capacity, and low-field nuclear magnetic resonance indicated that hardness, springiness, and water retention improved with prolonged MR time, peaking at 8 h (103.20 ± 11.32 g, 3.89 ± 0.28, 82.83 ± 2.77%) alongside uniform water distribution. Rheological assessments demonstrated enhanced network continuity, with yield stress increasing from 123.83 Pa to 209.47 Pa. Lissajous curves in the nonlinear viscoelastic region revealed reduced energy dissipation, improved structural stability, and strain stiffening over time. These findings offer insights for optimizing soy protein processing and developing innovative food products.

Aqueous enzymatic extraction (AEE) can recover soybean oil, protein and peptides, but spontaneously formed AEE emulsions suffer from lipid oxidation instability. This work systematically explored the modification effects of (-)-epigallocatechin3gallate (EGCG, 0.2–1.2 mg/mL) on structural, physicochemical, multi-stress stability and digestive characteristics of AEE soybean protein emulsions. Spectroscopic results confirmed EGCG bound to interfacial proteins via hydrogen bonding and hydrophobic interactions, which facilitates the transition of ordered α-helix and β-sheet toward disordered β-turn and random coil. Increasing EGCG concentration elevated polyphenol binding equivalent, particle size, zeta potential and turbidity, while reducing surface hydrophobicity and protein flexibility, with binding saturation achieved at 1.0 mg/mL. Correlation analysis verified that interfacial structural properties jointly governed emulsion oxidative stability and EGCG bioaccessibility. EGCG modification enhanced emulsion resistance to heat, pH, ionic and freeze–thaw stresses and inhibited lipid oxidation during storage. After gastrointestinal digestion, the EGCG bioaccessibility of 1.0 mg/mL treated emulsion reached 69.20%, nearly double free EGCG (34.78%). Collectively, 1.0 mg/mL EGCG non-covalent modification optimizes the performance of AEE emulsions, promising for protein–polyphenol co-delivery.

Background: With the intensification of globalization challenges, plant proteins have gained significant attention as sustainable ingredients. Recent studies indicate that molecular flexibility is a key parameter reflecting dynamic structural adaptability of plant proteins during processing and plays a central role in determining their functional characteristics. Meanwhile, the inherently low flexibility of most plant proteins limits their functional properties and application. However, current research on plant protein molecular flexibility still faces challenges, including fragmented characterization methods and inconsistent results. Therefore, there is an urgent need to systematically summarize characterization techniques, establish effective flexibility regulatory strategies, and elucidate flexibility-function relationships to guide applications. Scope and approach: This review summarizes multi-scale characterization techniques for plant protein molecular flexibility and compares their advantages and limitations. The mechanisms by which physical, chemical, biological, and combined processing strategies modulate flexibility are critically analyzed. The intrinsic relationship between flexibility and key functional properties is elucidated, emerging flexibility-driven applications are explored, and major research challenges and future directions are discussed. Key findings and conclusions: No single technique can comprehensively and accurately characterize plant protein molecular flexibility; integrating multiple complementary approaches tailored to protein properties is essential. Combined processing strategies show significant potential for flexibility regulation, although industrial implementation must balance process complexity and cost-effectiveness. Moreover, flexibility plays a pivotal role in optimizing plant protein functionality and enabling emerging applications. Future research should focus on integrating cross-scale characterization methods, optimizing multi-level regulatory strategies, and further clarifying flexibility-function relationships to support broader application development.

To address the environmental sensitivity and low bioavailability of riboflavin, this study constructed a soybean protein isolate fibril (SPF)/κ-carrageenan (κC) composite gel delivery system. This study systematically investigated the effects of two independent variables (protein type: SPI/SPF; κC concentration: 2, 4, 6, 8 mg/mL) on the gel structural stability, riboflavin encapsulation performance, and in vitro digestive delivery characteristics of the system. Thioflavin T (ThT) fluorescence and ultraviolet (UV) absorption spectroscopy confirmed the successful preparation of SPF and verified specific intermolecular interactions between SPF and κC. Intermolecular forces, protein leaching rates, and differential scanning calorimetry (DSC) results indicated that compared with SPI-κC composite gels, κC regulates SPF molecular conformation via hydrogen bonding and hydrophobic interactions to exert a synergistic effect. This conformational regulation significantly reduced the protein leaching rates in SPF-κC composite gels, elevated the thermal denaturation temperatures (up to 79.82 °C), and enhanced the gel structural stability. As the κC concentration increased, the environmental stability of SPF-κC riboflavin-loaded composite gels were markedly enhanced, which effectively delayed the gel degradation during simulated gastrointestinal digestion. This was manifested as a reduced protein loss rate (reduced to 22.23%). At a κC concentration of 8 mg/mL, the in vitro release mechanism of riboflavin shifted from Fickian to non-Fickian diffusion.

Studies on the soybean-algae co-precipitated proteins remain limited, particularly regarding their nutritional quality. We investigated the differences in structure and nutritional characteristics of soy-phycocyanin co-precipitated protein (Co), soy-phycocyanin blended protein (BL), soy protein isolate (SPI), and phycocyanin (PC). Compared with BL, Co had higher α-helix and β-sheet content, smaller particle size and ζ-potential, with unique "chain network" structures. Co was mainly stabilized by hydrogen bonds, hydrophobic interactions, and electrostatic interactions. Compared with SPI, PC, and BL, the digestibility of Co was the highest (98.46%, intestinal). Furthermore, Co exhibited a more balanced amino acid composition, with significantly higher contents of essential amino acids (sulfur-containing amino acids: 43.60 mg/g; Histidine: 32.29 mg/g). Co showed more unique proteins (139 kinds) after digestion. In conclusion, the co-precipitation treatment could improve the nutritional quality of composite protein system. This study provides a new theoretical basis for developing composite protein products with enhanced nutritional quality.

Coconut protein isolate (CPI) exhibits weak thermogel properties, limiting its industrial development. In this study, we investigated the use of ultrasonic-assisted modification (100-500 W, 10-30 min) to regulate the structure, aggregation, and gel characteristics of coconut protein isolate. Low-field magnetic resonance imaging (LF-NMR), scanning electron microscopy (SEM), and rheological techniques revealed that ultrasonication optimized the order of β-sheets and α-helices, increased water retention capacity, and enhanced ionic and hydrophobic interactions (75.50 %). At 300 W and 20 min, the gel exhibited uniformly dense pores, 37 % increased water retention, and a storage modulus (G') of 91,006.211 Pa. Excessive power (>300 W) or duration (>20 min) caused protein over-aggregation, leading to network collapse. These findings demonstrate that ultrasound can enhance CPI gels and provide insights for structural design in plant-based foods.

Co-precipitated protein is a promising plant-based meat ingredient, but the effect of its compositional ratio on flavor is unclear. This study analyzed the flavor profiles of soybean-wheat co-precipitated protein extrudates (HME-SWCP) with varying protein ratios. Results showed extrudates with protein ratios of 7:3 and 5:5 exhibited a brighter, light-yellow color along with minimal bitterness and astringency. E-nose analysis revealed a significant increase (p < 0.05) in aldehydes and ketones in HME-SWCP. GC-MS analysis identified methyl compounds as primary aroma constituents, and Relative Odor Activity Value analysis indicated that compounds such as 2-pentylfuran and 1-octen-3-ol were key odorants in optimal-ratio samples. Compared to single-protein extrudates, the use of co-precipitated protein not only mitigated undesirable tastes like bitterness but also promoted a richer spectrum of flavor compounds. This study demonstrates that optimizing soybean-wheat protein ratios is an effective strategy for tailoring the flavor of plant-based meat analogues.

This article focused on the relationship between the structural differences of soybean protein fibril (SPF)/soybean protein isolate (SPI)-bacterial cellulose (BC) complexes based on different interactions and their emulsifying properties, with BC concentrations (0, 0.4, 1.2, 2.0, 2.8, 3.6 mg/mL) at different pH values (2.0, 7.0) as variables. Observed through transmission electron microscopy, the combination of SPF/SPI and BC formed complexes with structural features of "line-network", "dual-network" and "dot-line". The analysis of zeta-potential, surface hydrophobicity, Ultraviolet spectra and Fourier transform infrared spectra results showed that at pH 2.0, BC mainly bound to SPF/SPI through electrostatic and hydrogen bonding interactions, while at pH 7.0, BC mainly bound to SPF/SPI through hydrogen bonding, hydrophobic and electrostatic interactions. Emulsification, differential scanning calorimetry, solubility and other results indicated that fibrillation and the addition of BC significantly improved the functional properties of complexes, and the overall effect was optimal when the amount of BC added was 2.0 mg/mL. At pH 7.0, the "dual-network" structure of SPF and BC enhanced their emulsification and interfacial properties. The emulsifying activity index was 44.60 m2/g and the emulsifying stability index of 7F-2.0 was 53.37 min. Therefore, this study provides a theoretical basis for the regulation of dual-fibril structure complexes and the development of emulsion based food.

Background Tree nuts are common nutritional foods in daily life, but are also major allergenic foods, seriously affecting human health. Tree nut allergies are associated with allergens and epitopes. Thus, it is urgent to identify tree nut allergens and their epitopes, and to develop strategies to reduce allergenicity. Scope and approach The review summarizes the allergen composition, characteristics, and epitopes of ten types of tree nuts, especially almond, walnut, hazelnut, pecan and cashew. The impact of processing techniques on tree nut allergenicity is discussed. Future perspectives on addressing tree nut allergies are also provided. Key findings and conclusions Tree nut allergenicity is primarily determined by the properties, conformation, and epitopes of major allergens such as Pru du 6 for almond, Cor a 1, Cor a 8, Cor a 9 for hazelnut, Jug r 1∼Jug r 4 for walnut, Ana o 1∼Ana o 3 for cashew, Car i 1 and Car i 4 for pecan. The reduction of allergenicity in tree nuts mainly focuses on the thermal processing such as baking, boiling and autoclaving. However, thermal processing can generate advanced glycation end products, enhancing allergenic potential and harmful byproducts affecting human health. Thus, nonthermal processing (e.g., high-pressure, ultrasonication, fermentation, polyphenol modification, glycation, enzymatic hydrolysis, irradiation) and combined technologies should be comprehensively investigated to decrease tree nut allergenicity in the future. The correlation between “processing-structure-epitope-allergenicity” needs to be further elucidated to investigate the mechanism for decreasing tree nut allergenicity. Allergenicity alteration should be further verified through animal and clinical trials.

Dual proteins are created by combining two heterologous proteins to complement their respective capabilities. In this study, soybean protein and phycocyanin were co-precipitated under pH 4.0 to prepare co-precipitated protein (Co). The effects of interprotein binding mode (co-precipitation and blending) and protein ratio on the structure and function of the complex were investigated. According to the results of FTIR, CD, surface hydrophobicity, free sulfhydryl content analysis, molecular interaction, SDS-PAGE and molecular docking, blended protein (BL) primarily relied on hydrogen bonding and hydrophobic interactions to maintain its structure. Nevertheless, Co exhibited not only stronger hydrogen bonds and hydrophobic interactions but also the presence of disulfide bonds. In comparison to BL, co-precipitation treatment significantly altered the protein structure, resulting in increased negative charges, reduced hydrophobic groups, decreased particle size and higher levels of beta-sheets. As a result, Co exhibited superior solubility, antioxidant activity, emulsifying and foaming properties. When the ratio of PC and SPI is 3:1, Co demonstrated the best solubility (65.91%), emulsification activity (36.71%), emulsion stability (86.23%), foaming ability (50.28%), and foam stability (86.89%). In summary, coprecipitation treatment proved more efficacious in producing complexes with stable structures and significantly improved the functional characteristics of SPI-PC complexes. This provides a reference for the preparation of protein complexes with superior functional properties.

In this study, a composite gel system oriented by dysphagia diet was constructed by soy protein amyloid fibrils (SAF) crosslinking high methoxyl pectin (HMP). The interaction mode, structure and properties of composite gels at different pH values and composite ratios were investigated. Results showed that HMP enhanced the gel properties of SAF through non-covalent interaction and steric hindrance of its own polysaccharide chain. Among them, the network pores of the pH 7.0 group gel were smaller, and the structure was more uniform than those of pH 2.0 group gel. Moreover, the composite gel changed from protein-based to polysaccharide-based as the volume ratio of SAF and HMP decreased, and the size of the intermolecular interaction force and the three-dimensional network structure changed. In particular, pH 7.0-SAF-HMP-1:1 had the optimal water holding capacity (91.37 ± 2.14%), rheology, textural properties, and lubricating performance. pH 7.0-SAF-HMP-1:1 was classified as Level 5 according to the International Dysphagia Diet Standardization Initiative and can be considered as potential transition foods. Furthermore, when the curcumin was 3 mg/mL, it had the highest embedding rate (83.62 ± 1.27%), bioaccessibility (74.87 ± 0.82%), and stability. These studies provided a theoretical basis for the ideal gels for dysphagia and functional foods.

The milling degrees (MD) alters the composition and secondary/tertiary structure of rice proteins, which modulates edible quality of rice by influencing its water absorption behavior. This study systematically characterized the effect of protein structure on moisture migration pathways and cooking quality of rice. Results indicated that as MD increased, the length, width, and whiteness value of rice significantly decreased (P < 0.05). Scanning electron microscope (SEM) and Micro-Computed Tomography (Micro-CT) revealed minor differences in pericarp thickness between MD2 and MD3, while MD2 retained the embryo. Hydration kinetics analysis revealed a increase in both the rate constant (K1) and capacity constant (K2) of MD0-3. Low-Field Nuclear Magnetic Resonance (LF-NMR) and rupture strength analysis further demonstrated enhanced moisture penetrate into the internal structure with increasing MD, resulting in loose internal tissue. Proteins underwent a second structural shift from alpha-helices and beta-turns to beta-sheets and random coils as MD increased. 2D/3D fluorescence and hydrophobicity (H0) analyses indicated that the hydrophobic groups of the protein increased in MD0-3, after which the changes were no longer significant (MD4-5.5, P > 0.05). Proteomic analysis revealed that the number of unique proteins (MD4-5.5) ranged from 19 to 27 after MD2, substantially lower than the range of 45-57 observed in MD0-1. The protein profile of MD 2-3 resembled the adjacent MD and contained a comparable proportion of hydrophobic groups, which promoted the formation of cross-link by hydrophobic interactions during cooking. The improved eating quality of MD3 was correlated with higher in the volume expansion rate (300.92 +/- 4.77%) and water absorption rate (302.61 +/- 9.38%), respectively.

In this study, composite nanoparticles (SGCPs) and coacervates (SGCs) of soy protein isolate (SPI) and type A gelatin (GE) at different ratios were prepared. Their formation mechanisms, interfacial properties at the oil-water interface, and their influence on the performance of high internal phase Pickering emulsions (HIPPEs) were subsequently investigated. FTIR combined with 2D-COS analysis revealed distinct hydrogen-bonding mechanisms. For SGCPs, the -OH and -NH3+ groups of GE preferentially interacted with the C=O and -COO- groups of SPI, primarily perturbing the amide I band and facilitating the formation of a "sieve-like anchored" structure. For SGCs, the flexible chains of GE (-OH) dynamically interacted with the N-H groups of SPI, leading to N-H bond breakage and predominant perturbation of the amide A band and promoting the formation of a coacervate structure. Compared to the SGCs, the SGCPs were characterized by a smaller particle size, improved amphiphilicity, and a porous sieve-anchored structure. SGCPs-5:5 demonstrated optimal amphiphilicity (three-phase contact angle approximate to 89.6 degrees), the best emulsifying properties (EAI = 14.39 m(2)/g, ESI = 74.02%), and excellent O/W interfacial characteristics (K-diff = 0.4909, K-p = 7.6715 & times; 10(-4), K-r = 1.6171 & times; 10(-2), Gamma = 5.85 mg/m(2), AP = 84.13%). Observation using confocal laser scanning microscopy demonstrated that a mechanically strong membrane featuring a multi-layered 3D network was formed at the interface. HIPPEs stabilized by SGCPs-5:5 demonstrated outstanding results in both rheological and stability testing. This study investigates how dual-protein composite nanoparticles adsorb at the oil-water interface and explores their use in stabilizing high internal phase Pickering emulsions (HIPPEs).

In this study, oleogels were fabricated using soybean whey protein (SWP) and hyaluronic acid (HA), and the effects of their molecular interactions on the network structure, rheological properties, oxidative stability, and lipid digestion behavior were systematically investigated. The results indicated that SWP and HA formed complexes primarily through hydrogen bonding, hydrophobic interactions, and electrostatic forces, as evidenced by a significant increase in particle size and in the absolute value of the zeta-potential. Rheological analysis and macroscopic observations revealed that, as the HA content increased, the oleogel transitioned from a fluid state to a stable, self-supporting structure. CLSM images showed the formation of a "honeycomb-like" network structure within the SWP-HA oleogel. At an HA content of 0.8%, the oleogel exhibited the most homogeneous pore size distribution and a continuous oil phase. The oil binding capacity increased and eventually plateaued as HA content increased, reaching 86.14 f 1.61% at 0.8% HA. This formulation achieved the highest antioxidant performance in the 7-day accelerated oxidation test, with the lowest POV and TBARS values of 13.23 f 0.21 mmol/kg and 9.87 f 0.36 mu mol/kg, respectively. In vitro simulated digestion experiments demonstrated that this oleogel system slowed lipid digestion, as reflected by the lowest free fatty acid release rate (34.18 f 1.79%) at 0.8% HA. In addition, correlation analysis indicates that the protein secondary structure has a significant correlation with the performance of the oleogel. This study provides a new strategy for designing novel functional fat-based products.

This study developed novel high internal phase Pickering emulsions (HIPPEs) based on soy protein isolate microgel particles (SPIMP) and dextran (DEX) and systematically investigated the effects of pH and SPIMP/DEX ratios on their stabilization mechanisms and 3D printing performance. Multispectral and interfacial properties revealed that pH-induced conformational unfolding of SPIMP exposed more binding sites, and DEX displayed pH-dependent distribution within the system. Under acidic conditions (pH 3), the high aggregation and low adsorption efficiency (45.7 %) of SPIMP led to a predominantly “free” state of DEX. Under neutral and alkaline conditions (pH 7 and 9), SPIMP and DEX formed stable “core-shell” complexes, achieving optimal binding efficiency at pH 9. These complexes exhibited better interfacial wettability (Contact angle = 90° ± 5°). CLSM and rheological properties indicated that the acidic HIPPEs stabilized by solely SPIMP exhibited bridging flocculation structures. The depletion effect driven by “free” DEX optimized the viscoelastic balance of the system (G' > 1000 Pa, G" > 100 Pa). The neutral and alkaline HIPPEs leveraged the steric hindrance effect of SPIMP/DEX complex to form uniform small-sized droplets, enhancing their mechanical properties and shear recovery (Yield stress >170 Pa, Recovery rate > 80 %). Ultimately, high-precision 3D printing was achieved at SPIMP/DEX ratios of 1:1, 1:3, and 1:2 in acidic, neutral, and alkaline HIPPEs, respectively. The pH and DEX co-modulation strategy offered novel insights and technical pathways for designing advanced emulsifiers and expanding 3D printing applications.

This study aimed to investigate the effects of different concentrations of cellulose nanocrystals (CNC) and carboxylated CNC (CCNC) on gel properties and formation mechanisms of soybean isolate protein amyloid fibers (SAF). With the increase in CNC/CCNC concentration, the water-holding capacity and strength of SAF gels were enhanced, the mobility of water molecules decreased, and the apparent viscosity and modulus increased. The optimum gel properties were observed at 0.75 % polysaccharide concentration. The gel network was formed by CCNC and SAF, driven by electrostatic interactions and hydrogen bonding. Particle size, simultaneous rheology and Fourier transform infrared spectroscopy (SR-IR), and spectroscopic indicated that the polysaccharide improved gel properties mainly by inducing SAF particle size reduction, secondary and tertiary structure, degree of crystallinity, and surface hydrophobicity alteration. The SAF thermal start degradation temperature was increased from 228.08 °C to 233.61 °C (CCNC0.75). These findings are expected to expand the application potential of SAF hydrogel functional materials.