Soy Protein Research Articles

Facile synthesis of olive oil-incorporated oleofilms via high-power ultrasonic emulsification: A sustainable packaging model.

This study aimed to construct oleofilms containing a binary mixture of proteins (soy protein hydrolysate and gelatin) and lipids (olive oil, stearic acid, and lecithin) using various ultrasonic emulsification processes. Initially, oleogels (OG20, OG40, OG60, OG80, and OG100) were fabricated with different sonication powers (20%-100%), along with control (OG) without sonication. Macrostructure, FTIR, DSC, stability coefficient (57.27%-79.52%), oil-binding capacity (68.38%-97.47%), and particle size (1364-3532nm) tests were performed on the oleogels. Oleofilms (OF, OF20, OF40, OF60, OF80, and OF100) were then formulated using the respective oleogels. Their visual, surface, and cross-sectional images were evaluated. The thickness (0.18-0.25mm) and water content (7.32%-11.73%) of oleofilms were investigated. Alterations in color and opacity (3.50-5.49) of the oleofilms were apparent. OF80 exhibited lower water (0.44g.mm/m2.h.kPa)/oxygen permeability (peroxide value: 2.31-14.30meq O2/kg), along with improved mechanical properties (tensile strength: 3.25MPa; elongation at break: 128.23%). OF80-coated pineapples demonstrated the highest resistance to spoilage.

Impact of soy/pea protein isolate-oil interactions on the physicochemical and structural properties of high-moisture texturized proteins under different oil concentrations.

This study investigated the effects of oil addition on the physical and chemical properties of high-moisture texturized proteins (HMTPs), focusing on soy protein isolate (SPI) and pea protein isolate (PPI). Rheological analysis revealed contrasting behaviors: SPI exhibited decreased rheological parameters at low oil concentrations (1, 3 %), followed by a significant increase at higher concentrations (5, 10 %), whereas PPI showed a consistent decline across all oil concentrations. The superior emulsifying and gelling abilities of SPI resulted in stronger protein-protein interactions and greater hardness at higher oil concentrations. In contrast, PPI exhibited minimal protein-oil interactions, reducing hardness and weakening textural properties. Further analysis showed that SPI-based and PPI-based HMTP exhibited structural changes upon oil addition, with contrasting directional shifts due to differing degrees of protein-oil interactions. These results emphasize the critical role of protein selection in optimizing oil-containing HMTP formulations, with SPI demonstrating clear advantages in achieving desirable texture due to its superior functional properties. This study provides valuable insights for developing sustainable plant-based meat analogs, particularly those requiring oil incorporation to replicate the textural and structural characteristics of traditional meat products.

Investigating gum arabic and soy protein isolate as wall material for encapsulation of five strains of Lactobacillus.

Encapsulation technology is a suitable tool to protect probiotics in carrier food products and gastrointestinal tract. In the current investigation, the potential of gum arabic, soy protein isolate and their blend as wall material for the encapsulation of five Lactobacillus spp. viz. L. acidophilus, L. bulgaricus, L. casei, L. plantarum and L. rhamnosus by freeze drying was studied. The impact of various encapsulating materials on the encapsulation efficiency, water activity, particle size, thermal properties and morphology of encapsulates was investigated. The results revealed that microparticles have low water activity (0.25-0.37), high encapsulation efficiency (81.94 to 93.03%) and particle size ranged between 112.34 and 147.79μm. Scanning electron microscopy indicated a porous morphology and irregular shape of probiotic powder. The absorption bands in the FT-IR spectra between 2854 and 1088cm-1, 2927-109cm-1 and 2930-1071cm-1 confirm the successful encapsulation of probiotics. The encapsulated probiotics showed high lysozyme tolerance (76.00 to 92.16%) and high cell surface hydrophobicity (58 to 85%) as compared to free cells. This improves probiotic stability, survivability, and functional properties, making them ideal for developing functional food products. These encapsulated probiotics are well-suited to withstand gastrointestinal conditions and deliver health benefits to consumers.

Physicochemical and rheological characterization of plant-based proteins, pectin, and chitin nanofibers for developing high internal phase Pickering emulsions as potential fat alternatives.

This study evaluated the properties of lentil protein, pea protein, quinoa protein, and soy protein as natural nanoparticle stabilizers and their interactions with pectin and chitin nanofiber in preparing high internal phase Pickering emulsions (HIPPEs). The globular plant proteins interact with polysaccharides through hydrogen bonding and electrostatic interactions, transforming the structure into complex morphologies, including fibrous and elliptical shapes. These complex nanoparticles exhibited enhanced thermal decomposition stability, and the HIPPEs constructed by them demonstrated significantly improved apparent viscosity and elastic modulus, with a yield stress of 931.9Pa, showing gel-like viscoelastic characteristics. The complex system not only reduced droplet size but also formed a compact network structure, which enabled the emulsion to maintain excellent stability under heat treatment, long-term storage and high-speed centrifugation. Our findings revealed the promising potential of utilizing plant-based proteins with polysaccharides to prepare HIPPEs for developing fat alternatives.

Phased characterization of soy protein gel modified by lactobacillus plantarum JYLP-326 in cooperation with acidic tremella fuciformis fruiting body polysaccharide: Focus on structural network, interaction and gel properties.

Soybean protein isolate (SPI) and acidic tremella fuciformis fruiting body polysaccharide (AP) were used to prepare phased products "sterilized soft gel (SPI-AP)" and "fermented strong gel (FSPI-AP)" to study the structural network, interaction and gel characteristics. The contents of α-helix (20.43% to 25.36%) and β-sheet (31.24% to 35.12%) of FSPI-AP increased compared with that of SPI. The introduction of AP and microorganisms improved the orderliness of peptide chain through non-covalent and covalent interactions, with hydrophobic (33.33%), electrostatic (26.77%), and disulfide bonds (24.45%) being the dominant forces in the formation of gels. Furthermore, AP could decrease the crystallinity and disrupt the regular rigid structure of protein molecules, so FSPI-AP had stronger cohesion to resist external force. FSPI-AP had the highest proportion of interaction (12.57%) in the interaction network, while SPI-AP was 9.07%. This study will provide a new idea for innovating the application of protein-polysaccharide gel systems.

Dual-protein system composed of soy protein and β-lactoglobulin: effect of transglutaminase-mediated crosslinking on its allergenicity and conformation.

The escalating global prevalence of food allergies has intensified the need for hypoallergenic food products. Transglutaminase (TGase)-mediated crosslinking has garnered significant attention for its potential to reduce the allergenicity of food proteins. This study aimed to investigate the effects of TGase crosslinking on the potential allergenicity and conformational changes in a dual-protein system composed of β-lactoglobulin (β-LG) and soy protein isolate (SPI) at varying mass ratios (10:0, 7:3, 5:5, 3:7 and 0:10 (w/w)). TGase preferentially crosslinked the 7S and 11S subunits of soy protein, rather than β-LG. Crosslinking treatment reduced the allergenic potential of both soy protein and β-LG, with the degree of reduction depending on the protein ratio. The β-LG5:SPI5 and β-LG7:SPI3 mixtures showed the most significant reduction in antibody reactivity towards soy protein and β-LG, respectively. Additionally, TGase-mediated crosslinking significantly reduced the binding capacity of all dual-protein samples to serum immunoglobulin E from allergic patients, compared to the control group (P < 0.05). The allergenicity reduction was accompanied by structural modifications, including a decrease in β-sheet content, an increase in β-turn and random coil structures, enhanced ultraviolet absorption and intrinsic fluorescence, reduced free sulfhydryl levels and altered intermolecular forces. These changes suggest that TGase-induced crosslinking may disrupt or mask allergenic epitopes, thus lowering allergenicity. TGase crosslinking effectively reduced the allergenic potential of the dual-protein system by inducing structural changes. These findings underscore the potential of TGase in developing hypoallergenic dual-protein food products and provide a scientific foundation for future research and application in the food industry. © 2025 Society of Chemical Industry.

Techno-Functionalities of White Bean Protein Concentrate: A Comparative Study with Soy and Pea Proteins

The study of the techno-functional properties of novel plant-based proteins has gained importance due to their as alternatives to conventional proteins in food systems. This work evaluated the techno-functional and structural properties of white bean protein concentrate (WBPC) in comparison with commercial soy and pea proteins. The WBPC exhibited a higher foaming capacity (FC) at neutral pH and excellent foam stability (FS) at both tested pH levels, outperforming the commercial proteins. Although the WBPC’s gelation occurred only at concentrations above 16% and its water-holding capacity (WHC) was lower than that of the soy and pea proteins, the WBPC showed a high binding capacity for nonpolar molecules, excelling in its oil-holding capacity (OHC) and forming stable emulsions, which are relevant for stabilization in food products. Additionally, WBPC can form more rigid gel networks, suitable for systems requiring greater mechanical strength. These techno-functional properties indicate that WBPC is a promising alternative source for the plant-based food industry, helping to meet the demand for innovative, sustainable products and contributing to the diversification of protein sources.

Techno-functionality of jack bean (Canavalia ensiformis) protein concentrate: a comparative study with soy and pea proteins.

With the growing human awareness of the environmental and animal stress caused by the meat industry, the consumption of plant-based products has expanded. Plant proteins have gained market prominence due to their sustainable origin, economic value and health benefits. Well-established plant proteins in the market, such as those of soy and pea, have various applications as ingredients in the food industry. However, given the wide variety of protein sources, it is necessary to conduct studies on the chemical and techno-functional characterization of other raw materials to further diversify their properties. In this context, the present study introduces jack bean protein concentrate (JBPC) as a potential alternative to proteins already established in the market. Techno-functional properties such as surface hydrophobicity, solubility, zeta potential, water- and oil-holding capacity, foam capacity and stability, emulsion stability and gel formation and rheology were analyzed. The protein content obtained from the extraction of the JBPC was 73 g (100 g)-1 on a dry weight basis, with an extraction yield of approximately 10% (w/w). Least gelation concentration for JBPC was 20%. JBPC exhibited a predominantly hydrophobic nature, with good oil retention capacity and emulsion and foam stabilization properties. The structure of JBPC was more linear, stable and rigid, which primarily influenced gel stiffness. Based on the study of techno-functional properties, JBPC proved to be an excellent alternative to soy protein isolate and pea protein concentrate in various applications, with potential for becoming an innovative ingredient in the food industry. © 2025 Society of Chemical Industry.

Continuous high-soy protein soymilk intake affects ordinary walking speed in the Japanese pre-frail and frail elderly: a randomized controlled trial.

To investigate whether continuous intervention using soymilk containing high soy protein improves physical frailty, a randomized controlled trial was conducted among the Japanese pre-frail and frail elderly. Japanese pre-frail and frail elderly participants (n = 73) were randomly assigned to the high-soy protein and control groups, who then ingested soymilk containing 14.5g/200ml and 3.2g/200ml of soy protein, respectively. Before and after the 12-week intervention, walking speed, skeletal muscle mass, grip strength, and the revised Japanese CHS questionnaire regarding fatigue and physical activity were examined to evaluate the impact of each soymilk on physical frailty and compare the variation between the two groups. Physical activity (monitored using a pedometer), dietary intake (determined by questionnaire), and estimated protein intake (determined by casual urine testing) were also recorded before and after the intervention. For the final analysis of the entire cohort (n = 70), there were no significant differences in the endpoints between the two groups. In the subgroup analysis, among participants with a walking speed of at least 1m/s (n = 35, P = 0.012) and at least 5,000 steps/day before intervention (n = 27, P = 0.0083), the variation in walking speed after the 12-week intervention was significantly higher in the high-soy protein group than in the control group. Estimated protein intake was also significantly higher in the high-soy protein group than in the control group after the intervention. Regarding physical activity and dietary intake, no significant differences were observed between the groups before or after the intervention. The continuous 12-week intervention of high soy protein increased the walking speed among the Japanese pre-frail and frail elderly participants who had an ordinarily high walking speed and high step counts. UMIN Clinical Trials Registry, UMIN000044999. Registered July 29, 2021; https://center6.umin.ac.jp/cgi-open-bin/ctr/ctr_view.cgi?recptno=R000051409 .

Effect of Plant Versus Animal Protein on Muscle Mass, Strength, Physical Performance, and Sarcopenia: A Systematic Review and Meta-analysis of Randomized Controlled Trials.

Dietary protein is recommended for sarcopenia-a debilitating condition of age-related loss of muscle mass and strength that affects 27% of older adults. The effects of protein on muscle health may depend on protein quality. The aim was to synthesize randomized controlled trial (RCT) data comparing plant with animal protein for muscle health. Forty-three eligible RCTs were sourced from Medline, Embase, Scopus, Web of Science, and CENTRAL databases. Four reviewers (R.J.R.-M., S.F.B., N.A.W., D.L.) extracted data from RCTs (study setting, population, intervention characteristics, outcomes, summary statistics) and conducted quality assessment using the Cochrane Risk of Bias 2.0. Standardized mean differences (SMDs) (95% CIs) were combined using a random-effects meta-analysis and forest plots were generated. I2 statistics were calculated to test for statistical heterogeneity. Thirty RCTs (70%) were eligible for meta-analysis and all examined muscle mass outcomes. Compared with animal protein, plant protein resulted in lower muscle mass following the intervention (SMD = -0.20; 95% CI: -0.37, -0.03; P = .02), with stronger effects in younger (<60 years; SMD = -0.20; 95% CI: -0.37, -0.03; P = .02) than in older (≥60 years; SMD = -0.05; 95% CI: -0.32, 0.23; P = .74) adults. There was no pooled effect difference between soy and milk protein for muscle mass (SMD = -0.02; 95% CI: -0.20, 0.16; P = .80) (n = 17 RCTs), yet animal protein improved muscle mass compared with non-soy plant proteins (rice, chia, oat, and potato; SMD = -0.58; 95% CI: -1.06, -0.09; P = .02) (n = 5 RCTs) and plant-based diets (SMD = -0.51; 95% CI: -0.91, -0.11; P = .01) (n = 7 RCTs). No significant difference was found between plant or animal protein for muscle strength (n = 14 RCTs) or physical performance (n = 5 RCTs). No trials examined sarcopenia as an outcome. Animal protein may have a small beneficial effect over non-soy plant protein for muscle mass; however, research into a wider range of plant proteins and diets is needed. PROSPERO registration no. CRD42020188658.

Peanut and Soy Protein-Based Emulsion Gels Loaded with Curcumin as a New Fat Substitute in Sausages: A Comparative Study.

The aim of this study was to evaluate the effects of the complete or partial substitution (0, 20, 40, and 100%) of the pork backfat in prepared sausage with protein emulsion gels loaded with curcumin. The effects of three protein emulsion gels (i.e., peanut proteins, ultrasound-modified peanut proteins, and soy proteins) on sausage characteristics (cooking loss, textural properties, microstructure, sensory characteristics, and antioxidant activity) were investigated and compared using a one-way analysis of variance and Duncan's multiple tests. The results revealed that the addition of each emulsion gel reduced cooking loss and improved the textural properties of the sausages in a dose-dependent manner. When 20% of pork backfat was substituted with untreated or ultrasound-modified peanut protein emulsion gel (PPEG), cooking loss decreased to a greater extent than when soy protein emulsion gel (SPEG) was used. However, the latter yielded higher cohesiveness and resilience at the same substitution levels. Compared with untreated PPEG, the sausages containing modified PPEG (at 200 W for 20 min) had significantly greater resilience and a denser microstructure. In addition, when 100% of pork backfat was substituted with modified PPEG, the sausages had desirable sensory characteristics. All sausages enriched with protein emulsion gels loaded with curcumin presented higher DPPH and ABTS radical scavenging capacities than the control sausages. The sausages prepared with the modified PPEG had the highest antioxidant activity (DPPH: 37.43 ± 0.35%; ABTS: 39.48 ± 0.50%; TBARS: 0.65 ± 0.05 mg MDA/Kg), which may be attributed to the increased stability of curcumin in the modified PPEG with a denser network structure. Therefore, ultrasound-modified PPEG loaded with curcumin can be used as a new fat substitute in functional sausages or other healthy meat products.

Stabilization of calcium-fortified soy protein emulsions by calcium chelating agent sodium tripolyphosphate

Stabilization of calcium-fortified soy protein emulsions by calcium chelating agent sodium tripolyphosphate

Effects of grape seed proanthocyanidin on emulsifying capacity of soy protein isolate in extrusion field and its underlying mechanism.

Soy protein isolate (SPI) has poor emulsifying ability because of its low molecular flexibility and compact structure, limiting its application in extruded protein-based foods. Extrusion technology has emerged as a promising way to alter the structural properties of proteins. Therefore, the impacts of grape seed proanthocyanidin (GSP) on structural and emulsifying characteristics of SPI in extrusion field were explored in this study. After extrusion treatment, the molecular chains of SPI were unfolded. In comparison with extruded SPI, the interaction with GSP led to a rightward shift in particle size distribution and an enhancement in zeta potential values of the protein. As GSP concentration increased from 20 to 80 g kg-1, the free sulfhydryl content of SPI was reduced by 4.17%, 25%, 29.24% and 35.85% compared with that of extruded SPI. The addition of GSP altered the secondary structure of SPI and enhanced the microenvironment polarity. Meanwhile, SDS-PAGE results indicated that the protein presented lower molecular weight with the introduction of GSP. Compared with extruded SPI, the supplementation with GSP increased the molecular flexibility while it decreased the surface hydrophobicity of SPI. Correlation analyses demonstrated that these structural changes induced an improvement in emulsifying activity and emulsion stability of SPI. GSP mainly binds to SPI through hydrogen bonds and hydrophobic interactions under the extrusion environment. This study demonstrated that GSP is a potential modifier, which can be applied to improve the emulsifying capacity of extruded SPI-based foods. © 2025 Society of Chemical Industry.

Microencapsulation of Deer Oil in Soy Protein Isolate-Chitosan Complex Coacervate-Preparation, Characterization, and Simulated Digestion.

Deer oil (DO) is a potentially beneficial functional oil; however, its sensitivity to environmental factors (e.g., oxygen and heat), difficulty in transport, and unfavorable taste hinder practical use. In this study, DO was encapsulated through the cohesive action of soy protein isolate (SPI) and chitosan (CS). The optimal preparation conditions yielded microcapsules with DO's highest encapsulation efficiency (EE) (85.28 ± 1.308%) at an SPI/CS mixing ratio of 6:1 and a core-to-wall ratio of 1:2 at pH 6. Fluorescence and scanning electron microscopy were utilized to examine the microcapsules' structure, showing intact surfaces and effective encapsulation of oil droplets through SPI/CS composite coalescence. Through Fourier transform infrared spectroscopy (FTIR), the electrostatic interplay between SPI and CS was verified during the merging process. At room temperature, the microcapsules resisted core oxidation by reducing gas permeation. In vitro simulated digestion results indicated the microcapsules achieved a slow and sustained release of DO in the intestinal tract. This study further expands the application scope of deer oil and promotes the development of deer oil preparations and functional foods.

Comparing Hydrolysable and Condensed Tannins for Tannin Protein-Based Foams.

Tannin-based foams have gained attention as a potential bio-based alternative to conventional synthetic foams. Traditionally, namely condensed tannins (CT) have been used, leaving the potential of hydrolysable tannins (HT) largely unexplored. This study compared the performance of chestnut (HT) and quebracho (CT) in tannin-protein-based foams at different tannin ratios. Using soy protein isolate (SPI) and hexamine under acidic conditions, a series of tannin foams were produced through a mechanical foaming method and analyzed for cell structure, compression strength, thermal conductivity, and chemical stability. Results show that chestnut tannin is viable in hexamine SPI formulations but is harder to process due to lower reactivity, further resulting in higher material densities compared to quebracho. Foams with higher quebracho content featured smaller, more interconnected cells, while increasing chestnut content led to larger, less interconnected cells. Compression strength decreased with higher chestnut content, while fire resistance and thermal conductivity were influenced by material density rather than tannin type. The 13C-NMR analysis revealed covalent bonding of hexamine with both tannins, but potential covalent bonds with SPI were undetectable. Overall, chestnut tannin can substitute quebracho tannin in hexamine-SPI foams, though with compromises in terms of specific material properties and processability.

Unveiling the potential of bean proteins: Extraction methods, functional and structural properties, modification techniques, physiological benefits, and diverse food applications.

Bean proteins, known for their sustainability, versatility, and high nutritional value, represent a valuable yet underutilized resource, receiving less industrial attention compared to soy and pea proteins. This review examines the structural and molecular characteristics, functional properties, amino acid composition, nutritional value, antinutritional factors, and digestibility of bean proteins. Their applications in various food systems, including baked goods, juice and milk substitutes, meat alternatives, edible coatings, and 3D printing inks, are discussed. The physiological benefits of bean proteins, such as antidiabetic, cardioprotective, antioxidant, and neuroprotective effects, are also presented, highlighting their potential for promoting well-being. Our review emphasizes the diversity of bean proteins and highlights ultrasound as the most effective extraction method among available techniques. Beyond their physiological benefits, bean proteins significantly enhance the structural, technological, and nutritional properties of food systems. The functionality can be further improved through various modification techniques, thereby expanding their applicability in the food industry. While studies have explored the impact of bean protein structure on their nutritional and functional properties, further research is needed to investigate advanced modification techniques and the structure-function relationship. This will enhance the utilization of bean proteins in innovative and sustainable food applications.

Techno-functional properties of soy, rice and carioca bean protein blends

Techno-functional properties of soy, rice and carioca bean protein blends

Metagenomic analysis of microbial dynamics in water kefir grains: influence of soy protein on biomass growth and development of alternative beverage

Metagenomic analysis of microbial dynamics in water kefir grains: influence of soy protein on biomass growth and development of alternative beverage

Improving the tensile strength of yuba films via disulfide bond breaking-mediated aggregation of soy proteins

Improving the tensile strength of yuba films via disulfide bond breaking-mediated aggregation of soy proteins

Recombinant Fungal Aspartic Endopeptidases: Insights into Protein Hydrolysis and Combined Effect with Pepsin for Animal Feed Application.

Protein hydrolysis under acidic conditions can improve the product quality, nutrient availability, and cost efficiency, particularly when neutral or alkaline enzymes are ineffective. Six fungal aspartic endopeptidases (FAPs) were recombinantly expressed as active enzymes in Komagataella phaffi, with peak activity between 30-50 °C and pH 3.0-4.0. Despite FAP1 yielding a higher degree of hydrolysis for soy protein isolate (SPI) than FAP4, mass spectrometry analysis revealed similar cleavage preferences for the two peptidases. FAP1 and FAP4 experienced competitive product inhibition (Ki: 2.8 mg mL-1, Km: 3.2 mg mL-1 for FAP1 and Ki: 9.67 mg mL-1, Km: 6.58 mg mL-1 for FAP4). These findings suggest that Ki and Km values, when studied in isolation, do not always predict a peptidase's hydrolytic efficacy. Among the FAPs, FAP6 notably increased soluble protein content in animal feed by ∼3-fold. FAP1, when combined with pepsin, had a positive effect on the hydrolysis of SPI. These results underscore the potential of FAPs to hydrolyze proteins─specifically, animal feed proteins─in acidic environments.