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The effects of the ratio change of SPI and WG (11: 1, 10: 2, 9: 3, 8: 4, 7: 5, 6: 6 and 5: 7) on the product characteristics of plant-based meat analogues (PBMAs) were investigated. The results show that the addition of WG significantly reduces the hardness and chewiness of PBMAs, but significantly improves the springiness and brightness of PBMAs. When the ratio of SPI to WG is 9: 3, PBMAs has the best fiber structure, storage modulus and apparent viscosity. Fourier transform infrared spectroscopy (FT-IR) results showed that the transition from α-helix to β-fold was an important reason for PBMAs fibers reinforcement. The intermolecular interaction of protein shows that the enhancement of fiber structure of PBMAs is related to the increase of disulfide bonds. In this study, low cost and high simulation degree PBMAs are provided as a reference for developing PBMAs.

This research investigated the viability of replacing milk protein with glycosylated soybean protein isolate (SPI) treated with different enzymatic hydrolysis times (0, 10, 20, 30, 40, and 50 min) in yogurt. The results showed that enzymatic hydrolysis pretreatment combined with glycosylation for SPI exhibited elevated grafting and solubility. Additionally, the high solubility of SPI (94.77 %) at 40 min facilitates the preparation of dual-protein yogurt (DPY). Compared to ESPI0-G, DPY that incorporates ESPI40-G through partial substitution of milk protein is capable of forming a denser and more stable gel matrix. Especially, the syneresis of DPY40 was reduced by 7.61 % compared to DPY0, which more closely approximates the texture properties of traditional yogurt. Meanwhile, glycosylated SPI treated with enzymatic hydrolysis can effectively degrade the beany flavor and slightly bitter taste in DPY. This study could provide a solid theoretical basis for the broader application and industrialization of plant-based yogurt.

The stability of diabetes formula food for special medical purposes (D-FSMP) was improved by high-pressure homogenization (HPH) at different homogenization pressures (up to 70 MPa) and number of passes (up to 6 times). The process at 60 MPa/4 times was the best. Casein had the highest surface hydrophobicity in this condition. The casein–polysaccharide complexes were endowed with the smallest size (transmission electron microscopy images). The complex particles exhibited nearly neutral wettability (the three-phase contact angle was 90.89°), lower interfacial tension, and the highest emulsifying activity index (EAI) and emulsifying stability index (ESI). The prepared D-FSMP system exhibited the narrowest particle size distribution range, the strongest interfacial deformation resistance and the best storage stability. Therefore, an appropriate intensity of HPH could enhance the stability of D-FSMP by improving the interfacial and emulsifying properties of casein–polysaccharide complexes. This study provides practical guidance on the productions of stable D-FSMP.

Inadequate fibrous attributes and prohibitive pricing are pivotal barriers to the broader market penetration of meat analogs (MAs). This research endeavors to address these impediments by formulating a blend of cost-effective soybean meal (SM) and pea protein isolate (PPI) across a spectrum of ratios (PPI:SM = 1:0, 8:2, 6:4, 4:6, 2:8, and 0:1). The analysis of textural properties elucidated that the integration of SM markedly diminished the textural rigidity and mastication resistance of MAs. Employing scanning electron microscopy (SEM) and fibrillation degree metrics, it was ascertained that the most favorable fibrous architecture of MAs was attained at a PPI to SM ratio of 6:4. Further experimental evidence underscored that the synergistic interaction between SM and PPI catalyzed the conversion of free sulfhydryl groups into disulfide linkages, a pivotal mechanism in the augmentation of MAs’ fibrous matrices. The conclusions drawn from this study provide substantive contributions to the formulation of superior-quality, economically viable MAs, and could potentially accelerate their market acceptance.

At present, there have been many research articles reporting that plant-based protein Pickering particles from different sources are used to stabilize Pickering emulsions, but the reports of corresponding review articles are still far from sufficient. This study focuses on the research hotspots and related progress on plant-based protein Pickering particles in the past five years. First, the article describes the mechanism by which Pickering emulsions are stabilized by different types of plant-based protein Pickering particles. Then, the extraction, preparation, and modification methods of various plant-based protein Pickering particles are highlighted to provide a reference for the development of greener and more efficient plant-based protein Pickering particles. The article also introduces some of the most promising applications of Pickering emulsions stabilized by plant-based protein Pickering particles in the food field. Finally, the paper also discusses the potential applications and challenges of plant-based protein Pickering particles in the food industry.

The primary significance of this work is that the commercial yeast proteins particles were successfully used to characterize the high internal phase Pickering emulsions (HIPPEs). The different sonication time (0,3,7,11,15 min) was used to modulate the structure and interface characteristics of yeast proteins (YPs) that as Pickering particles. Immediately afterward, the influence of YPs particles prepared at different sonication time on the rheological behavior and coalescence mechanism of HIPPEs was investigated. The results indicate that the YPs sonicated for 7 min exhibited a more relaxed molecular structures and conformation, the smallest particle size, the highest H0 and optimal amphiphilicity (the three-phase contact (θ) was 88.91°). The transition from extended to compact conformations of YPs occurred when the sonication time exceeded 7 min, resulting in an augmentation of size of YPs particles, a reduction in surface hydrophobicity (H0), and an elevation in hydrophilicity. The HIPPEs stabilized by YPs particles sonicated for 7 min exhibited the highest adsorption interface protein percentage and a more homogeneous three-dimensional (3D) protein network, resulting in the smallest droplet size and the highest storage (G′). The HIPPEs sample that stabilized by YPs particles sonicated for 15 min showed the lowest adsorption protein percentage. This caused a reduction in the thickness of its interface protein layer and an enlargement in the droplet diameter (D [3,2]). It was prone to droplet coalescence according to the equation used to evaluate the coalescence probability of droplets (Eq (2)). And the non-adsorbed YPs particles form larger aggregation structures in the continuous phase and act as “structural agents” in 3D protein network. Therefore, mechanistically, the interface protein layer formed by YPs particles sonicated 7 min contributed more to HIPPEs stability. Whereas the “structural agents” contributed more to HIPPEs stability when the sonication time exceeded 7 min. The present results shed important new light on the application of commercial YPs in the functional food fields, acting as an available and effective alternative protein.

A protein mixture was prepared using a blend of soybean protein isolate, soybean protein concentrate, and wheat protein through high-moisture extrusion. This study investigated the effects of soybean oil/coconut oil additions (2%, 5%, and 8%) on the physiochemical properties of a soy protein–wheat protein mixture subjected to high-moisture extrusion. The protein extrudates underwent assessment for textural properties, fiber degree, sensory evaluation, microstructure, protein solubility, and protein secondary structure. The findings indicated that plant oils significantly reduced the hardness, springiness, and chewiness of the extrudates, and 5% plant oil significantly increased the fiber degree of the extrudates. In addition, the highest fiber degree and sensory evaluation score were achieved with 5% coconut oil. Observation of the macro- and microstructure indicated that the presence of unsaturated fatty acids in soybean oil did not benefit the improvement of the fibrous structure of protein extrudates during high-moisture extrusion processing. SDS-PAGE and FTIR results revealed that coconut oil, rich in saturated fatty acids, caused the clustering of medium- and low-molecular-weight subunits in texturized protein. Additionally, coconut oil elevated the ratio of 11S protein subunits containing sulfur-based amino acids and facilitated a shift from β-turn to β-sheet. The inclusion of plant oils increased the development of hydrogen and disulfide bonds, resulting in a denser, fibrous structure. DSC demonstrated that plant oils reduced the thermal stability of the texturized proteins but enhanced the order of protein structure.

The low rehydration properties of commercial soy protein powder (SPI), a major plant−based food ingredient, have limited the development of plant−based foods. The present study proposes a treatment of soy lecithin modification combined with Alcalase hydrolysis to improve the rehydration of soy protein powder, as well as other processing properties (emulsification, viscosity). The results show that the soy protein–soy lecithin complex powder, which is hydrolyzed for 30 min (SPH–SL−30), has the smallest particle size, the smallest zeta potential, the highest surface hydrophobicity, and a uniform microstructure. In addition, the value of the ratio of the α−helical structure/β−folded structure was the smallest in the SPH–SL−30. After measuring the rehydration properties, emulsification properties, and viscosity, it was found that the SPH–SL−30 has the shortest wetting time of 3.04 min, the shortest dispersion time of 12.29 s, the highest solubility of 93.17%, the highest emulsifying activity of 32.42 m2/g, the highest emulsifying stability of 98.33 min, and the lowest viscosity of 0.98 pa.s. This indicates that the treatment of soy lecithin modification combined with Alcalase hydrolysis destroys the structure of soy protein, changes its physicochemical properties, and improves its functional properties. In this study, soy protein was modified by the treatment of soy lecithin modification combined with Alcalase hydrolysis to improve the processing characteristics of soy protein powders and to provide a theoretical basis for its high−value utilization in the plant−based food field.

This article explored the effect of insoluble okara fiber (IOF) on the properties of okara protein (SOP) emulsion. The effects of different concentrations of IOF (0.25 wt%, 0.50 wt%, 0.75 wt% and 1.00 wt%) on the microstructure, interfacial activity, emulsifying activity and stability of SOP emulsion were studied with sunflower oil as oil phase. The results showed that with the increase of the IOF concentration, the particle size of the SOP/IOF emulsion showed a trend of gradual increase. The laser confocal microscope observation experiment showed that the emulsion droplets change in the same trend, and the absolute value of the zeta potential presents an increasing trend. The content and concentration of interfacial protein showed an increasing trend, and the change of rheological index showed that the trend of shear thinning was increasing, and high concentration of IOF could significantly enhance the long-term storage stability, acid resistance stability and salt resistance stability of SOP emulsion. This provides a theoretical basis for the further application of IOF in the protein emulsion gel system.

The effects of lipid peroxidation on rice bran protein (RBP) structure was examined through Raman Spectroscopy. 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH), acrolein, and malondialdehyde (MDA) are chosen for lipid peroxidation. Incubation of RBP with the increasing concentration of three oxidants resulted in a gradual generation of protein carbonyl derivatives. It can be deduced from the Raman spectra that a low concentration of AAPH and acrolein both decreased the percentage of α-helix and β-sheet, which increased with MDA concentration. The Raman intensities of tryptophan residues of oxidized RBP by AAPH and acrolein, both initially increased and then decreased with oxidation concentration. After MDA treatment, the Raman intensities corresponding to Trp residues and Tyr doublet ratio of RBP were increased and then decreased, and decreased and then increased with oxidation concentration, respectively. The structural change induced by RBP oxidation with the Raman Spectroscopy can aid in refining the function of RBP characteristics and control the adjustment of the storage condition.

In order to improve the quality of high-temperature defatted soybean meal, which is the raw material for producing soybean protein powder, and improve the stability and reliability of process control. Under the condition of microwave power of 20 kW, wind speed of 2.5 m/s, and material thickness of 20 mm, the effects of microwave treatment for 4 to 6 min on the moisture content, temperature, total number of colonies, color after water-dissolving and the secondary structure of soybean protein in high-temperature defatted soybean meal were analyzed. It could be used to guide the production and application of high temperature defatted soybean meal for soybean protein powder production. The results showed that: When the microwave treatment time was between 4 and 6 min, the water content decreased at a rate of 1.51%/min; when the microwave treatment time was 5.45 min, the temperature could be controlled at 103 ℃, the killing rate of microorganisms reached 96.8%, and the total number of colonies reached 100 CFU/g; when the microwave treatment time was between 4.62 and 5.45 min, the red value of the aqueous solution were relatively stable, the brightness and yellow value changed slightly, and the color was good; when the microwave time was ≥5 min, the urease activity was negative, which met the requirements of food for infants and children; microwave treatment had a significant effect on the secondary structure of the protein. When the microwave time was between 4.29 and 5.45 min, the α-helix transformed to the β-turn and then disappeared, and the amount of the β-turn increased rapidly; when the microwave time was between 5.45 and 6 min, the β-turn was rapidly transformed to the α-helix; the β-sheet changed only in small amplitudes and was relatively stable during the entire microwave treatment process. Microwave treatment can effectively control the moisture, color, total number of colonies, urease activity of high-temperature defatted soybean meal, and improve the secondary structure of soybean protein, which is of positive significance for improving the quality of high-temperature defatted soybean meal and expanding the application field.

This research explored microwave treatment impact on the structuro-functional aspects of oxidized soy protein aggregates (OSPI). Data showed that oxidative treatment promoted the formation of high molecular weight aggregates through hydrophobic interactions, thereby disrupting the structure of natural soy protein isolates (SPI). Microwave treatment for an appropriate time (≤30 s) caused the molecular structure of OSPI to open up and reduction in molecular weight and disulfide bond content, while absolute zeta potential increased. These modifications increased emulsifying capacity of OSPI, as well as the interfacial adsorption of protein. Longer microwave treatment times (>30 s) caused OSPI to exhibit a tendency to aggregate in TEM and CLSM images. It indicated the appropriate microwave electromagnetic field effect and microwave heating effect could coordinatively regulate soy protein functional properties by modifying their aggregation behavior. The results provided new ideas for reducing resource waste, and further expanding soy protein application in the food industry.

In this study, the purpose was to investigate the effects with different concentrations of carrageenan (CG, 0–0.30%) on the gel properties and freeze–thaw stability of soy protein isolate (SPI, 8%) cold-set gels. LF-NMR, MRI, and rheology revealed that CG promoted the formation of SPI-CG cold-set gel dense three-dimensional network structures and increased gel network cross-linking sites. As visually demonstrated by microstructure observations, CG contributed to the formation of stable SPI-CG cold-set gels with uniform and compact network structures. The dense gel network formation was caused when the proportion of disulfide bonds in the intermolecular interaction of SPI-CG cold-set gels increased, and the particle size and zeta potential of SPI-CG aggregates increased. SG20 (0.20% CG) had the densest gel network in all samples. It effectively hindered the migration and flow of water, which decreased the damage of freezing to the gel network. Therefore, SG20 exhibited excellent gel strength, water holding capacity, freeze–thaw stability, and steaming stability. This was beneficial for the gel having a good quality after freeze–thaw, which provided a valuable reference for the development of freeze–thaw-resistant SPI cold-set gel products.

ABSTRACT A simple model of alternative microbiota in the developing intestinal environment has been highly desirable for the study of health and disease in the gut. The pattern of antibiotic depletion of natural gut microbes is necessary for this model. However, the effects and loci of antibiotic deletion of gut microbes remain unclear. In this study, a mixture of three proven broad-spectrum antibiotics was selected to study their effects on microbial deletions in the jejunum, ileum, and colon of mice. The 16S rRNA sequencing results showed that antibiotics significantly reduced colonic microbial diversity, with limited effects on the jejunum and ileum. At the level of microbial genera, only 93.38% of Burkholderia-Caballeronia-Paraburkholderia and 5.89% of Enterorhabdus were present in the colon after antibiotic treatment. However, such changes were not observed in the microbial composition of the jejunum and ileum. Our results suggest that the antibiotics depleted intestinal microorganisms by acting primarily in the colon and not in the small intestine (jejunum and ileum). IMPORTANCE Many studies have applied antibiotics to delete intestinal microbes to shape pseudosterile mouse models and further used for fecal microbial transplantation. However, few studies have explored the spatial location of antibiotic action in the intestine. This study shows that the selected antibiotics effectively deleted microbiota in the colon of mice, with limited effects on microbes in the jejunum and ileum. Our study provides guidance for the application of a mouse model of antibiotic deletion of intestinal microbes.

The protein conformation of soymilk is the key to affecting the instant solubility of soymilk flour. This study aimed to evaluate the effect of cavitation jet treatment time (0, 2, 4, 6, and 8 min) on the instant solubility of soymilk flour based on the conformational changes of protein in soymilk. The results showed that the cavitation jet treatment for 0–4 min significantly unfolded the protein structure of soymilk and increased the content of soluble protein, which reduced the particle size and increased the electrostatic repulsion and the viscosity of soymilk. This was beneficial for soymilk droplets fully atomized and repolymerized in the spray drying tower, forming soymilk flour particles with large size, smooth surface, and uniform distribution. When the cavitation jet treatment time was 4 min, the wettability (from 127.3 ± 2.5 s to 84.7 ± 2.1 s), dispersibility (from 70.0 ± 2.0 s to 55.7 ± 2.1 s), and solubility (from 56.54% to 78.10%) of soymilk flour were significantly improved. However, when the time of the cavitation jet treatment was extended to 8 min, the protein of soymilk aggregated and the stability of soymilk decreased, which reduced the particle size and hurt the surface characteristics of soymilk flour after spray drying. It resulted in a decrease in the instant solubility of soymilk flour. Therefore, the cavitation jet treatment with proper time increases the instant solubility of soymilk flour by improving the protein conformation of soymilk.

The identification model of chlorpyrifos pesticide residues in wheat was established based on near infrared spectroscopy and stoichiometry. Wheat samples with different chlorpyrifos residues were prepared by spraying method. Near infrared diffuse reflectance spectra of samples were collected, and qualitative prediction models of factorization method, Euclidean distance method and quantitative prediction model of partial least squares method were established. The results showed that: The qualitative discrimination rate of factorization method was higher than that of Euclidean distance method, the characteristic bands of construction conditions were 5543.68~4643.72, 7582.43~6510.28 cm−1, the preprocessing method was second derivative+vector normalization+5-point smoothing, the discrimination rate could reach 96%. The characteristic bands of the construction conditions of partial least squares quantitative discrimination model were 5543.68~4643.72 cm−1, 7582.43~6510.28 cm−1, the preprocessing method was to eliminate the constant offset, the main component fraction was 7, the cross validation coefficient (R2) was 99.46, and the mean square residual (RMSECV) was 1.15. The correlation between the actual value and the predicted value was good, and the minimum detection limit was 1 mg/kg, which could accurately determine the pesticide of Chlorpyrifos in wheat. The above results showed that the discrimination rate of the qualitative analysis model established by the factorization method was as high as 96%, which could realize the qualitative analysis and identification of chlorpyrifos pesticide residues in wheat, and the partial least squares method could realize the quantitative analysis and identification with good reproducibility.

This paper investigates the effect on the physicochemical and functional properties of soybean protein concentrate (SPC) by using Alcalase protease and high-pressure homogenization (HPH) (0, 20, 40, 60, 80, and 100 MPa) for the combined modification. The results showed that the degree of hydrolysis of SPC was 4.1% and the antigen protein was degraded after Alcalase hydrolysis, when the homogenization pressure (HP) was 6 0Mpa, the particle size of the SPC was the smallest, the zate potential absolute value up to 33.45 mV, the secondary structure has the lowest β-sheet content, the highest random coil content, and the highest surface hydrophobicity (H0), the size of protein fragments on the microstructure surface is the smallest, the lowest denaturation temperature (Td) and enthalpy (△H) are 72.59°C and 1.35 J/g, the highest solubility is 80.54%, and the highest water and oil holding capacities are 7.73 g/g and 6.51 g/g, respectively. The best emulsifying activity and emulsifying stability were 43.46 m2/g and 190.35 min, the most even distribution of emulsion droplets. This indicates that the HPH treatment destroys the structure of enzymatic hydrolyzed SPC, changes its physicochemical properties, and improves its functional properties. In this study, SPC was modified by HPH and enzyme combined treatment, in order to improve the functionality and application range of SPC, and provide a theoretical basis for its high-value utilization in the food field.

The emulsifying activity of soy protein would decrease after long-term storage, which caused huge economic losses to food processing plants. This study explored the temporal evolution mechanism of oxidation on the structure and function of soy protein aggregates, which would improve the application of soy protein in food industry. Decreased α-helix and increased random coil were observed at the initial oxidation stage (0–4 h), which induced increases in hydrophobicity and disulfide bond content. In addition, emulsibility increased significantly. However, when the oxidation time extended to 6–12 h, the soluble aggregates transformed into insoluble aggregates with large particle size, low solubility, and molecular flexibility. Surface hydrophobicity and emulsifying activity were reduced, resulting in bridging flocculation of emulsion droplets. Mutual transformation between components is affected by factors that include spatial conformation and intermolecular forces, which eventually lead to functional changes in the protein molecules.

Ulcerative colitis (UC) is challenging to treat and severely impacts patients and families. A previous study reported immunomodulatory and reduction of pro-inflammatory properties for the Lactiplantibacillus plantarum L15. This study aimed to analyze the preventive properties and mechanistic actions in an in vivo colitis model. The histopathological alteration, inflammation cytokines, and intestinal barrier function were analyzed. Subsequently, the cecal gut microbiota contents and products from different groups were detected. Finally, gene expressions related to the NF-κB signaling process were evaluated. L. plantarum L15 significantly decreased disease activity index (DAI), myeloperoxidase activity (MPO), pro-inflammatory cytokine (TNF-α, IL-1β, and IL-6) level, and increased weight change, colon length, and production of inflammation-suppressing cytokines. Furthermore, this strain supplementation substantially increased ZO-1, Occludin, and Claudin-1, and MUC2 mRNA expression levels with a corresponding decrease in serum lipopolysaccharide and D-lactic acid contents. In addition, L. plantarum L15 improved gut microbiota composition and increased short-chain fatty acid (SCFAs) in the colon content, which significantly reduced the transfer of NF-κB p65 to the nucleus. Our findings provide a theoretical basis for L. plantarum L15 as a preventive candidate for UC.

The combination of protein and flavonoids can ameliorate the problems of poor solubility and stability of flavonoids in utilization. In this study, soybean protein isolate pretreated by ultrasonication was selected as the embedding wall material, which was combined with luteolin to form a soybean protein isolate-luteolin nanodelivery system. The complexation effect and structural changes of soybean protein isolate (SPI) and ultrasonic pretreatment (100 W, 200 W, 300 W, 400 W and 500 W) of soybean protein isolate with luteolin (LUT) were compared, as well as the changes in digestion characteristics and antioxidant activity in vitro. The results showed that proper ultrasonic pretreatment increased the encapsulation efficacy, loading amount and solubility to 89.72%, 2.51 μg/mg and 90.56%. Appropriate ultrasonic pretreatment could make the particle size and the absolute value of ζ-potential of SPI-LUT nanodelivery system decrease and increase respectively. The FTIR and fluorescence results show that appropriate ultrasonic pretreatment could reduce α-helix, β-sheet and random coil, increase β-turn, and enhance fluorescence quenching. The thermodynamic evaluation results indicate that the ΔG 0 and ΔS > 0, so the interaction of LUT with the protein was spontaneous and mostly governed by hydrophobic interactions. The XRD results show that the LUT was amorphous and completely wrapped by SPI. The DSC results showed that ultrasonic pretreatment could improve the thermal stability of SPI-LUT nanodelivery system to 112.66 ± 1.69 °C. Digestion and antioxidant analysis showed that appropriate ultrasonic pretreatment increased the LUT release rate and DPPH clearance rate of SPI-LUT nanodelivery system to 89.40 % and 55.63 % respectively. This study is a preliminary source for the construction of an SPI nanodelivery system with ultrasound pretreatment and the deep processing and utilization of fat-soluble active substances.

Native soy protein isolate (N-SPI) has a low denaturation point and low solubility, limiting its industrial application. The influence of different industrial modification methods (heat (H), alkaline (A), glycosylation (G), and oxidation (O)) on the structure of SPI, the properties of the gel, and the gel properties of soy protein isolate (SPI) in myofibril protein (MP) was evaluated. The study found that four industrial modifications did not influence the subunit composition of SPI. However, the four industrial modifications altered SPI’s secondary structure and disulfide bond conformation content. A-SPI exhibits the highest surface hydrophobicity and I850/830 ratio but the lowest thermal stability. G-SPI exhibits the highest disulfide bond content and the best gel properties. Compared with MP gel, the addition of H-SPI, A-SPI, G-SPI, and O-SPI components significantly improved the properties of the gel. Additionally, MP-ASPI gel exhibits the best properties and microstructure. Overall, the four industrial modification effects may impact SPI’s structure and gel properties in different ways. A-SPI could be a potential functionality-enhanced soy protein ingredient in comminuted meat products. The present study results will provide a theoretical basis for the industrialized production of SPI.

Oxidative attack leads to the oxidative aggregation and structural and functional feature weakening of soybean protein. We aimed to investigate the impact of ultrasonic treatment (UT) with different intensities on the structure, emulsifying features and interfacial features of oxidized soybean protein aggregates (OSPI). The results showed that oxidative treatment could disrupt the native soy protein (SPI) structure by promoting the formation of oxidized aggregates with β1-sheet structures through hydrophobic interactions. These changes led to a decrease in the solubility, emulsification ability and interfacial activity of soybean protein. After low-power ultrasound (100 W, 200 W) treatment, the relative contents of β1-sheets, β2-sheets, random coils, and disulfide bonds of the OSPI increased while the surface hydrophobicity, absolute ζ-potential value and free sulfhydryl content decreased. Moreover, protein aggregates with larger particle sizes and poor solubility were formed. The emulsions prepared using the OSPI showed bridging flocculation and decreased protein adsorption and interfacial tension. After applying medium-power ultrasound (300 W, 400 W, and 500 W) treatments, the OSPI solubility increased and particle size decreased. The α-helix and β-turn contents, surface hydrophobicity and absolute ζ-potential value increased, the structure unfolded, and the disulfide bond content decreased. These changes improved the emulsification activity and emulsion state of the OSPI and increased the protein adsorption capacity and interfacial tension of the emulsion. However, after a high-power ultrasound (600 W) treatment, the OSPI showed a tendency to reaggregate, which had a certain negative effect on the emulsification activity and interfacial activity. The results showed that UT at an appropriate power could depolymerize OSPI and improve the emulsification and interfacial activity of soybean protein.

The impacts of industrial phosphorylation on the structural changes, microstructure, functional, and rheological features of soybean protein isolate (SPI) were spotlighted. The findings implied that the spatial structure and functional features of the SPI changed significantly after treatment with the two phosphates. Sodium hexametaphosphate (SHMP) promoted aggregation of SPI with a larger particle size; sodium tripolyphosphate (STP) modified SPI with smaller particle size. SDS–polyacrylamide gel electrophoresis (SDS-PAGE) results showed insignificant alterations in the structure of SPI subunits. Fourier transform infrared (FTIR) and endogenous fluorescence noted a decline in α-helix quantity, an amplification in β-fold quantity, and an increase in protein stretching and disorder, indicating that phosphorylation treatment fluctuated the spatial structure of the SPI. Functional characterization studies showed that the solubility and emulsion properties of the SPI increased to varying degrees after phosphorylation, with a maximum solubility of 94.64% for SHMP-SPI and 97.09% for STP-SPI. Emulsifying activity index (EAI) and emulsifying steadiness index (ESI) results for STP-SPI were better than those for SHMP-SPI. Rheological results showed that the modulus of G’ and G″ increased and the emulsion exhibited significant elastic behavior. This affords a theoretical core for expanding the industrial production applications of soybean isolates in the food and various industries.

A cavitation jet can enhance food proteins’ functionalities by regulating solvable oxidized soybean protein accumulates (SOSPI). We investigated the impacts of cavitation jet treatment on the emulsifying, structural and interfacial features of soluble soybean protein oxidation accumulate. Findings have shown that radicals in an oxidative environment not only induce proteins to form insoluble oxidative aggregates with a large particle size and high molecular weight, but also attack the protein side chains to form soluble small molecular weight protein aggregates. Emulsion prepared by SOSPI shows worse interface properties than OSPI. A cavitation jet at a short treating time (6 min) would cause soluble oxidized aggregates to reaggregate through an anti-parallel intermolecular β-sheet, which resulted in lower EAI and ESI, and a higher interfacial tension (22.44 mN/m). The results showed that suitable cavitation jet treatment could adjust the structural and functional features of SOSPI by targeted regulated transformation between the soluble and insoluble components.

In this study, pea residue reserve insoluble diet fiber (hereinafter referred to as pea fiber) was used as a raw material. The effects of γ-irradiation doses (0, 0.5, 1, 2, 3, and 5 kGy) on the structural properties (main composition, particle size and specific surface area, scanning electron microscope (SEM) microstructure, Fourier transform infrared spectroscopy, and X-ray diffraction) and functional properties (oil-holding capacity, swelling and water-holding capacity, and adsorption properties) of pea fiber were explored. The results show that, when the γ-irradiation dose was 2 kGy, compared with the untreated sample, the contents of cellulose, hemicellulose and lignin in pea fiber decreased by 1.34 ± 0.42%, 2.56 ± 0.03% and 2.02 ± 0.05%, respectively, and the volume particle size of pea fiber decreased by 17.43 ± 2.35 μm. The specific surface area increased by 23.70 ± 2.24 m2/kg and the crystallinity decreased by 7.65%. Pore and irregular particles appeared on the microstructure surface of the pea fiber treated with γ-irradiation. The results of the infrared spectrum showed that the hemicellulose and lignin in pea fiber were destroyed by γ-irradiation. These results indicate that γ-irradiation can significantly affect the structural properties of pea fiber. When the γ-irradiation dose was 2 kGy, the highest oil-holding capacity, swelling capacity and water-holding capacity of pea fiber were 8.12 ± 0.12 g/g, 19.75 ± 0.37 mL/g and 8.35 ± 0.18 g/g, respectively, and the adsorption capacities of sodium nitre, cholesterol and glucose were also the strongest. These results indicate that the functional properties of pea fiber are improved by γ-irradiation. In this study, γ-irradiation technology was used as pretreatment to provide a theoretical basis for the application of pea fiber in food processing.

Plant-based meat analogues (PBMs) are increasingly interesting to customers because of their meat-like quality and contribution to a healthy diet. The single-screw extruder is an important method for processing PBMs, and the characteristics of the product are directly affected by the composition of the raw materials; however, little research focuses on this issue. To explore the effect of protein composition on the quality characteristics of PBMs produced by a single-screw extruder, four soybean varieties used in China (Heihe 43 (HH 43), Jiyu 86 (JY 86), Suinong 52 (SN 52), and Shengfeng 5 (SF 5)) were selected. The 11S/7S ratios for these varieties ranged from 1.0: 1 to 2.5: 1 in order to produce PBMs with different protein compositions. The structure, processing, nutrition, and flavor characteristics were explored to analyze their differences. The results showed that protein composition affected the structure of PBMs, but the correlation was not significant. Meanwhile, a lower 11S/7S ratio (HH 43) did not prove to be a favorable characteristic for the processing of PBMs. From the perspective of nutrition and flavor, it seems acceptable to use a moderate 11S/7S ratio (JY 86 and SN 43) to produce PBMs. This study proved that the protein composition of raw materials affects the characteristics of PBM products produced by a single-screw extruder. To produce PBMs of higher quality, soybeans with a markedly different 11S/7S ratio should not be selected.

Chiba tofu is a new type of vegetarian food prepared with soy protein isolate (SPI). According to factory feedback, the SPI stored in the factory storeroom in summer undergoes reactive oxidation, which changes the structure of SPI and further affects the quality of Chiba tofu. Consequently, the main objective of this study was to prepare Chiba tofu with SPI with different storage periods and evaluate the effect of different degrees of oxidation on structural characteristics of SPI and rheology, texture, microstructure and sensory properties of Chiba tofu. The carbonyl content and turbidity of SPI significantly increased, and the contents of free sulfhydryl (SH) and disulfide bond (S-S) simultaneously decreased with storage time. The oxidation changes the SPI conformation, leading to a transition of α-helix and β-turn to β-sheet and random coil during the storage periods. In the SDS–PAGE analysis, oxidation promoted the SPI molecules crosslinked and aggregated, which affected the quality of Chiba tofu. In short storage periods (0–12 days), SPI was relatively moderately oxidized when the carbonyl content was between 4.14 and 6.87 mmol/g. The storage and loss modulus of Chiba tofu both increased, the network was compact, and the hardness and springiness of Chiba tofu showed an increasing trend. Moreover, in longer storage periods (12–30 days), the SPI was relatively severely oxidized when the carbonyl content was between 7.24 and 9.14 mmol/g, which had an adverse effect on Chiba tofu rheological and texture properties, microstructure, and sensory properties. In sensory evaluation, Chiba tofu stored 12 days had the highest overall quality score than that stored on other days. This study is expected to provide an argument for the better industrial production of Chiba tofu.