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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.

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.

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.

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.

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.