This study investigated the utilization of fresh wet soybean dregs and soy whey to replace low-temperature defatted soybean meal flour and water in textured soy protein production via single-screw extrusion. The formulation ratio was soy protein isolate:wheat gluten:fresh wet soybean dregs: soy whey = 8:4:8:7. Results indicated no significant changes in functional groups but a reduction in secondary structure content. Fresh wet soybean dregs increased the water absorption index by 3.57-10.00%, while soy whey enhanced elongation at break by 8.98-40.45%. Nutritionally, total dietary fiber increased by approximately 43%; soy whey elevated free isoflavone aglycone levels and reduced trypsin inhibitor content by 27%. Volatile flavor analysis revealed significant reduction or absence of key beany compounds such as hexanal. This study confirms the feasibility of valorizing soybean processing by-products for textured protein production.

This study aimed to investigate antifreeze activity of thawed drip membrane-separated components ( > 10 kDa and < 10 kDa) and their cryoprotective mechanism based on a myosin model. Both fractions exhibited stable hydroxyl structures and strong thermal hysteresis activity, significantly enhancing survival rate of Streptococcus thermophilus under freeze-thaw stress. Using myosin as a model system, both fractions suppressed freezing-induced increases in surface hydrophobicity, carbonyl and particle size, while mitigating decreases in free sulfhydryl and fluorescence intensity, thereby alleviating protein aggregation and conformational denaturation. Intermolecular force and molecular docking analyses revealed that > 10 kDa fraction interacted with myosin mainly through non-specific binding, while the peptide KELASQPDVDGFLVGGASLKPEFVDIINAK in < 10 kDa fraction bound to key myosin domains via hydrogen bonding and hydrophobic interactions. These findings offer new insights for developing natural cryoprotectants to enhance quality stability of frozen food products.

This study developed an oil-modified starch gel (OMSGs) as delivery system to modulate texture and control sodium release in low-sodium shrimp myofibrillar protein (SMP) gels. OMSGs prepared with 1% oil and 100 mg/mL starch formed a dense network with high water-holding capacity and gel strength. OMSGs containing varying NaCl (5-20%), denoted OMSGs-Na, were blended with SMP at a 10:1 ratio to obtain OMSGs-Na-SMP composites. Among these, the OMSGs-Na (15%, equivalent to 1.19% NaCl in SMP) exhibited uniform and dense microstructure, effectively delaying sodium ion release during simulated oral digestion (30 s). Its gel hardness (381.00 g), chewiness (214.38 g), and whiteness (52.97) matched those of SMP gels with 20% direct NaCl addition (1.52% in SMP). Rheological analysis further confirmed that viscoelastic properties were comparably enhanced to the high-salt control. This carrier system offers a novel strategy to overcome texture deterioration and insufficient saltiness perception in low-sodium aquatic gel products.

This study investigated the mechanisms of non-covalent interactions between (3-Conglycinin (7S) and rutin (Ru), and its effects on the protein conformation, emulsion stability and interfacial protein structure. 7S-Ru complexes with low Ru concentrations (0.02% to 0.08%) showed a significant increase in absolute potential value and protein flexibility. Both Fourier transform infrared (FTIR) spectroscopy and molecular docking revealed that the interaction between 7S and Ru is predominantly mediated by hydrophobic forces and hydrogen bonding. Furthermore, molecular dynamics (MD) simulations corroborated these findings, demonstrating tight association at the binding sites and consequent conformational stability. With the increase of Ru concentration (0.02% to 0.08%), the droplets size of the emulsions gradually decreased, while the apparent viscosity increased accordingly. The microrheological properties and multiple light scattering results indicated that the addition of Ru slowed down the droplet motion rate, enhanced the elastic behavior, and reduced droplet aggregation, thereby improving emulsion stability. While Ru binding in the bulk phase induced a more disordered 7S structure with increased flexibility (reduced a-helix/(3-sheet and increased (3-turn/random coil), upon adsorption at the interface, the complexes underwent a distinct "interface-induced rearrangement," adopting a more ordered configuration with increased a-helix content. The emulsion formation was primarily driven by hydrophobic interactions, and the structurally rearranged interfacial proteins formed a cohesive viscoelastic film that effectively prevented droplet coalescence. Consequently, this work offers crucial theoretical support for the application of such complexes in food processing.

This study aimed to develop a functional fat substitute by fabricating a novel hybrid gel system composed of a zein nanoparticles (ZNPs)/pectin/hydroxypropyl guar gum (HPG) co-stabilized Pickering emulsion gel integrated with a beeswax oleogel. Medium- and long-chain triacylglycerols (MLCTs)-enriched emulsion gels were synthesized using Pickering interfacial catalysis in the emulsion gel, yielding 64.6% MLCTs. The effects of pectin and HPG concentrations on emulsion gel properties were evaluated. At concentrations of 2.5% and 1.0%, respectively, the emulsion gel exhibited smaller droplets (29.5 ± 0.3 μm) and excellent thermal stability. Beeswax content and the emulsion gel-to-oleogel ratio significantly influenced the rheological properties and hardness of the hybrid gel. Higher beeswax concentration and oleogel ratio led to a denser network structure, enhanced stability, and increased hardness. Optimal structural integrity and stability were achieved at 10% beeswax and a 10:5 emulsion gel-to-oleogel ratio. Overall, the bicontinuous network formed between the ZNPs/pectin/HPG-stabilized emulsion gel and the oleogel underpins the hybrid gel stability. Additionally, the hybrid gel was rich in ω-3 polyunsaturated fatty acids and MLCTs, making it suitable as a functional fat substitute for ice cream. This work provides a promising strategy for designing structured fat substitutes with tailored nutritional and functional properties.

Legume proteins have become essential materials for developing plant-based foods due to their excellent functional properties. Intermolecular forces in legume protein hydrogels include non-covalent bonds such as hydrogen bonds, hydrophobic interactions, and covalent bonds such as disulfide bonds. Changes in gel intermolecular forces directly affect the gel food quality. This paper describes the types and determination of legume protein hydrogel intermolecular forces, and deeply explores the influencing factors, including gel preparation methods, protein pre-treatment ways (physical treatment, chemical treatment, enzymatic hydrolysis, and fibrillation), and the introduction of other active ingredients (polyphenols, polysaccharides, exogenous amino acids, and proteins from other sources). The preparation methods determine the textural properties of legume protein hydrogels. Pre-treatment (especially ultrasonic treatment) is an effective method for improving legume protein hydrogels. The incorporation of polyphenols, polysaccharides, and other substances, as well as fibrillation of proteins, further promotes the application of legume protein hydrogels in food and biomedical fields. Adjustment of gel intermolecular forces is expected to control the release of bioactive components from gel carriers as well as facilitate the development of foodstuffs with different applications. Undoubtedly, mastering the mechanisms and strategies for regulating intermolecular forces in hydrogels will further enhance the quality of legume protein hydrogel products and facilitate the development of new products that meet consumer demands.

Osmanthus fragrans has a pleasant aroma, and different varieties have different aromas and colors. This study systematically assessed how the inclusion of various Osmanthus fragrans cultivars influences critical beer attributes, including physicochemical parameters, sensory characteristics, antioxidant capacity, and volatile flavor profiles. The findings demonstrated that osmanthus addition markedly decreased beer turbidity (p < 0.05) and enhanced the TPC by as much as 30%. The content of monophenols in beer also increased significantly, especially catechins and gallic acid, which increased by an average of 25 and seven times (p < 0.05), respectively. Vanillic acid was established as a key determinant of the DSA in osmanthus beer through correlation and cluster analysis (r = 0.9, p < 0.01). GC-MS analysis identified 50 volatile compounds, with increase in dihydro-β-ionone and irisine content in the osmanthus beer, and sensory evaluation confirmed that the mix and aurantiacus varieties achieved the highest overall acceptability, demonstrating the effectiveness of osmanthus in enhancing the beer's overall flavor and functional properties.

Drying of Taraxacum mongolicum Hand.-Mazz (TMHM) was an effective approach for preventing spoilage and extending shelf life. Ten drying methods were systematically evaluated, among which ultrasonic-assisted hot-air drying (Us-HA-D) was identified as the most suitable technique. The drying kinetics analysis indicated that the Weibull model could offer the best fit to the experimental data, while the drying curves revealed that Us-HA-D increased the drying rate by approximately 25-30% compared to the conventional hot-air drying, leading to a reduction in total drying time of up to 40.3%. The microstructural observations confirmed that ultrasonic pretreatment induced the formation of microchannels, which facilitated moisture migration and resulted in a 25.4% rise in the effective moisture diffusivity. Us-HA-D method also significantly improved color preservation, exhibiting the lower total color difference (ΔE), and optimally maintained bioactive components, with the retention of chicoric acid, chlorogenic acid, and the total phenolic content enhanced by 40.2%, 55.6%, and 40.3%, respectively. The process of Us-HA-D was optimized using the response surface methodology under the following conditions: ultrasound power of 535 W, ultrasound duration of 30 min, air temperature of 60°C, and air velocity of 3.8 m/s, achieving an optimal balance between the product quality and drying efficiency. The findings supported that Us-HA-D was a promising industrial-scale technology for producing high-quality dried TMHM with well-preserved phytochemical profile, color integrity, and antioxidant properties, highlighting its potential for broad application in the drying of other food materials.

Plant proteins often suffer from structural limitations and poor interfacial performance, leading to low delivery efficiency of bioactive compounds. To overcome these challenges, this study developed a synergistic modification strategy combining alkaline pH-shifting and ultrasonication. By controlling the protein concentration (1, 2, 4

Ramped heating from 50 °C to 90 °C was applied to elucidate how temperature regulates the gelation behavior and hydrogel properties of myofibrillar proteins-capsaicin (MPs-CAP) blends. The hydrogels were characterized in terms of macroscopic properties, water status, microstructure, intermolecular forces, and rheological behavior. The results showed non-monotonic trends in whiteness, hardness, springiness, and water-holding capacity, with an initial increase followed by a decrease as temperature rose, and optimal performance was observed at 70 °C. At 50-70 °C, heating unfolded MPs and facilitated the integration of CAP through hydrophobic interactions, which likely reinforced the network structure. CAP appeared to participate in network formation; this association, in combination with hydrogen bonding, created a dense and uniform three-dimensional network. This network converted free water into immobilized water via capillary effects, endowing the hydrogels with favorable water-holding capacity and thermal stability (Tp = 138.33 °C). Above 70 °C, excessive and disordered aggregation of MPs, along with increased release of CAP, was accompanied by pore enlargement, implying possible dissociation of CAP from the network. These results reveal the non-monotonic temperature-dependent behavior of MPs-CAP gelation, providing a theoretical basis for precise thermal processing of protein gels containing hydrophobic bioactive ingredients.

This study addresses the poor quality of rice bread caused by gluten absence by investigating the effects of transglutaminase (TGase) on whey protein isolate (WPI)-fortified rice flour, dough, and bread. Results showed that TGase catalyzed crosslinking between WPI and rice proteins, significantly strengthening the dough network. The optimal dosage of 0.6% TGase increased water-holding capacity to 0.92 g/g and enhanced dynamic moduli. Microstructural analyses revealed a continuous protein–starch network, resulting in a uniform gas-cell distribution with a 26% reduction in diameter and a specific volume increase to 1.56 mL/g. Additionally, the crosslinked network reduced moisture loss, lowering bread hardness by 44.31%. These findings confirm that TGase-mediated crosslinking is essential for improving gluten-free rice bread quality.

The coagulation abnormalities, including complex and irregular bleeding surfaces and underlying coagulopathies in patients, are significant clinical cause of uncontrollable hemorrhage and death in accidental trauma. Herein, we have developed an ultra-expansible chitosan-silk fibroin miniaturized sponge (MS-GT) for delivering antifibrinolytic drug — tranexamic acid (TXA) to achieve in situ hemostasis of the first-aid wounds. TXA-modified gelatin was combined with the highly compressed functional chitosan-based sponge through strong hydrogen bonds, which stabilized sponge's compression state and made it easier to undergo thermosensitive dissolution to release its expansion potential. The MS-GT (∼ 3 mm3, thickness < 1 mm) could achieve a volume expansion of over 11 times within five seconds to seal complex and irregular deep wounds without the need for additional specialized instruments. In addition, the loaded TXA promoted the formation of fibrin to enhance hemostatic efficacy for overcoming the bleeding in coagulation disorders, including disseminated intravascular coagulation (DIC) and hemophilia B model, with significantly superior hemostatic effect comparing with bulk sponge and clinical collagen sponge. This chitosan-based MS-GT alleviated the formation of fibrous capsules in the liver during the post-hemostasis regeneration process, offering new insights for the development of emergency hemostatic materials.

This study systematically examined how pH-shifting pretreatment influences the formation mechanism of soy protein isolate (SPI) fibrils (SPF) across varying concentrations (10, 30, and 50 mg/mL). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that pH-shifting converts more macromolecular peptides in SPI into small-molecule peptides. ThT fluorescence revealed that increasing SPI concentration and applying pH-shifting pretreatment produced more β-sheet structures in SPF. FTIR and CD analyses demonstrated that pH-shifting promotes fibril formation through α-helix-to-β-sheet transitions, with minor contributions from disordered structures adopting β-sheet conformations. Fluorescence spectroscopy and surface hydrophobicity results indicated that hydrophobic interactions are critical for converting SPI into SPF. Analysis of average particle size and zeta potential revealed that pH-shifting treatment increased electrostatic repulsion, inducing structural unfolding and protein fibril conversion up to 72.61%. TEM analysis showed that pH-shifting treatment and higher SPI concentration enhanced the diameter and length of SPF, producing a more coiled and entangled morphology that formed a dense network, ultimately increasing system viscosity. Elevating SPI concentration combined with pH-shifting is therefore an effective pretreatment approach that not only facilitates SPF formation but also modulates its morphological characteristics, with their synergistic effects markedly enhancing SPF growth.

Water-boiled salted duck (WSD) is a classic traditional Chinese poultry product with a unique texture and savory aroma. Actually, the short term aging process is crucial to the development of the final flavor of WSD. In this study, duck carcasses were aged at six temperature gradients (0, 5, 10, 15, 20 and 25 ℃) for 2 days. Multiple complementary analytical approaches, including physicochemical determination, electronic nose (E-nose), gas chromatography-ion mobility spectrometry (GC-IMS), headspace solid-phase microextraction coupled with gas chromatography-mass spectrometry (HS-SPME-GC-MS), odor activity value (OAV) calculation and multivariate statistical analysis, were applied to elucidate temperature-induced variations in meat quality and volatile profiles. The aging temperature exerted significant effects on the physicochemical traits and volatile fingerprints of WSD. Samples aged at 10℃ exhibited superior comprehensive quality. A total of 54 volatile flavor compounds (VFCs) were identified via HS-SPME-GC-MS, among which aldehydes dominated the overall aroma pool. OAV analysis confirmed that (E, E)-2,4-decadienal was the core aroma-active compound responsible for temperature-dependent flavor discrepancies. From an industrial perspective, the precise temperature would contribute to the consistent flavor performance other than product yield. This study provides theoretical support for standardized temperature regulation during WSD aging and offers a multi-integrated flavor characterization strategy for traditional poultry products.

Protein fibrillation has great potential for enhancing the emulsification, foaming, and gelling properties of proteins. However, its effects on protein film-forming properties are less well understood. In this study, soy protein isolate (SPI) was subjected to fibrillation at pH 2.0 and 85 degrees C to prepare films plasticized with glycerol (2 %). Mature fibrils formed at 12 h, as confirmed by thioflavin T fluorescence assay, circular dichroism spectroscopy, and atomic force microscopy. Moreover, the structural changes of the fibrillar SPI were related to the resulting film characteristics. Rheological analysis confirmed that a dense gel network was formed during fibrillation. In addition, particle size increased, while the free sulfhydryl content and surface hydrophobicity decreased. Fourier transform infrared spectroscopy revealed strong hydrogen-bonded beta-sheets were dominant in the fibrillar SPI film. The dense network and exposed amino acids in the fibrillar SPI film resulted in high tensile strength (4.91 MPa) and good ultraviolet-blocking properties.

The effects of psyllium polysaccharides (PP) with different molecular weights (Mw) on the physicochemical characteristics, interaction forces, and digestibility of rice starch (RS) are methodically examined in this work. High-Mw PP (H-PP) (3.83 × 106 Da), medium-Mw PP (M-PP) (8.39 × 104 Da), and low-Mw PP (L-PP) (9.28 × 103 Da) were fractionated, characterized, and added to RS to clarify their effect on starch digestion. The results indicate that H-PP exhibited the most pronounced inhibitory effect on enzymatic hydrolysis, leading to a significant reduction in the estimated glycemic index (eGI) by enhancing the crystalline structure and short-range molecular order of RS. Mechanistic investigation revealed that PP molecules interact with RS through hydrogen bonding and electrostatic interactions, forming a structural barrier that impedes enzymatic accessibility. The intensity of these interactions was greatest in RS-H-PP and gradually decreased in RS-M-PP and RS-L-PP, corresponding with an increase in starch digestibility. These findings provide mechanistic insights into the molecular interactions regulating polysaccharide-starch systems and establish a theoretical basis for the development of functional starch-based foods with controlled glycemic responses.

This study investigated the interactions between soybean protein isolate (SPI) and β-cyclodextrin (β-CD), focusing on structural changes and functional enhancements. Results revealed that β-CD induces SPI conformational changes by decreasing α-helix, increasing β-structures, and enhancing flexibility via non-covalent interactions. Redshift in the negative peak from 203 to 214 nm as β-CD concentration increased from 0.1 to 1.0 mg/mL. Fluorescence quenching confirmed spontaneous complexation driven by hydrophobic forces. Moderate β-CD concentrations improved the functional and interfacial properties of SPI, whereas higher levels promoted aggregation and diminished performance. Increasing β-CD concentration elevated SPI-β-CD particle size from 197.6 to 310.7 nm and zeta potential from -15.52 to -24.27 mV. SEM confirmed structural rearrangement without compromising material integrity, while molecular docking showed stable complex formation through hydrogen bonding and van der Waals forces. These findings highlight the potential of SPI-β-CD complexes for enhanced functionality in emulsions, delivery systems, and various applications.

Heat facilitates aggregation and gel formation of soybean proteins. Ultrasonic reduces the size of protein aggregates. This study examined the impact of glycinin (11S) subunits on soybean lipophilic proteins (SLPs) gel formation and underlying mechanisms. Effects of protein dispersion pretreatment with 400 W ultrasonic and associated mechanisms were assessed. Addition of the A- and B-subunits before and after ultrasonic minimally affected SLP secondary structure. A-subunit addition before ultrasonic negligibly affected SLP tertiary structure. Addition of the B-subunit after ultrasonic reduced hydrophobic thermal aggregation. However, the small B-subunit size was unfavorable for the formation of a gel matrix, which led to poor gel properties. In contrast, solubility of the A-subunit after ultrasonic was increased to 31.06 ± 1.62 %). Particle size was decreased to 43.33 ± 1.36 nm for A:SLP (1:2). Endogenous fluorescence spectroscopy demonstrated increased protein unfolding after ultrasonic and decreased disulfide bonds. These changes improved the gel state. Rheological and microstructural analyses revealed increased energy storage modulus and yield strain, accompanied by a more homogeneous microstructure following ultrasonic. Microscopic improvement resulted in increased encapsulated water within interstitial spaces of the A-SLP gel matrix. This enhanced water mobility in B-SLP gels, in turn weakening gel stability. The changes observed in B-SLP were primarily due to reduced hydrophobic interactions between the proteins. The findings clarify the effect of ultrasonic treatment on the formation of soybean globulin-SLP hybrid gels at the subunit level. The data provide a theoretical basis for the synergistic utilization of soybean proteins among different components.

This study aimed to design novel protein-based ternary complexes and investigate their emulsion stability. The ternary complexes were prepared using soy protein hydrolysate (SPH)-L-arginine (Arg) /L-lysine (Lys) binary complexes as substrates by introducing tannic acid (TA) under alkaline conditions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and multiple spectral analyses confirmed ternary complexes formation. TA induced secondary and tertiary structure changes in SPH and the binary complexes, as evidenced by blue-shifted in amide I band, enhanced UV absorption, decreased fluorescence intensity, and reduced surface hydrophobicity. Compared with Lys, Arg significantly reduced the interfacial tension of SPH, while TA caused the interfacial tension to increase, indicating that the ternary complex SPH-Arg-TA promotes emulsion formation more readily than SPH-Lys-TA. During emulsion storage, both droplet size and zeta potential of the SPH-Arg-TA emulsion changed minimally, whereas the SPH-Lys-TA emulsion droplet increased from 11.96 μm to 24.38 μm, indicating poor stability. Accelerated oxidation experiments revealed that SPH-Arg-TA emulsions have excellent oxidative stability, while SPH-Lys-TA emulsions showed poor stability. Arg and TA synergistically enhance the physicochemical stability of emulsions. This study provided theoretical references for the designs of emulsions with tailored functions by utilizing proteins and bioactives.