Formation of self-assembled fibril aggregates of trypsin-controllably hydrolyzed soy protein and its regulation on stability of high internal phase Pickering emulsions.

The mechanisms of trypsin hydrolysis time on the structure of soy protein hydrolysate fibril aggregates (SPHFAs) and the stability of SPHFAs-high internal phase Pickering emulsions (HIPPEs) were investigated. SPHFAs were prepared using soy protein hydrolysate (SPH) with different trypsin hydrolysis time (0 min-120 min) to stabilize SPHFAs-HIPPEs. The results showed that moderate trypsin hydrolysis (30 min, hydrolysis degree of 2.31 %) induced SPH unfolding and increased the surface hydrophobicity of SPH, thereby promoting the formation of flexible SPHFAs with maximal thioflavin T intensity and ζ-potential. Moreover, moderate trypsin hydrolysis improved the viscoelasticity of SPHFAs-HIPPEs, and SPHFAs-HIPPEs remained stable after storage at 25 °C for 80 d and heating at 100 °C for 1 h. Excessive trypsin hydrolysis (> 30 min) decreased the stability of SPHFAs-HIPPEs. In conclusion, moderate trypsin hydrolysis promoted the formation of flexible SPHFAs with high surface charge by inducing SPH unfolding, thereby promoting the stability of SPHFAs-HIPPEs.

Highly ordered aggregation of soy protein isolate particles for enhanced gel-related properties through konjac glucomannan addition.

This study assessed the effect of konjac glucomannan (KGM) on the aggregation of soy protein isolate (SPI) and its gel-related structure and properties. Raman results showed that KGM promoted the rearrangement of SPI to form more ß-sheets, contributing to the formation of an ordered structure. Atomic force microscopy, confocal laser scanning microscopy, and small-angle X-ray scattering results indicated that KGM reduced the size of SPI particles, narrowed their size distribution, and loosened the large aggregates formed by the stacking of SPI particles, improving the uniformity of gel system. As the hydrogen bonding between the KGM and SPI molecules enhanced, a well-developed network structure was obtained, further reducing the immobilized water's content (T22) and increasing the water-holding capacity (WHC) of SPI gel. Furthermore, this gel structure showed improved gel hardness and resistance to both small and large deformations. These findings facilitate the design and production of SPI-based gels with desired performance.

Plant-based protein emulsions with soy protein isolate and gluten improve freeze-thaw stability and shelf life of pork meatballs.

This study investigated the effects of oil-in-water emulsions used as fat substitutes on the physicochemical properties of meatballs during frozen storage. Different formulations of fat replacers were prepared, including pork fat as the control (C), oil and water (OW), oil-in-water emulsion (E), emulsion with soy protein isolate (SE), emulsion with gluten (GE), and emulsion with soy protein isolate and gluten (SG). These fat substitutes were applied to a meatball paste. The samples were stored at -18 °C for 30 and 60 days, and their physicochemical properties were analyzed after thawing at 4 °C for 12 h. The SE formulation had the highest values for both water content and liquid holding capacity during frozen storage (P < 0.05). SE, GE, and SG showed significantly higher hardness, cohesiveness, springiness, gumminess, and chewiness than those of E during storage (P < 0.05). The vegetable protein addition treatments maintained a compact structure throughout storage. SE, GE, and SG prevented lipid and protein oxidation during frozen storage. These results demonstrated that SE, GE, and SG offer significant advantages in improving the freeze-thaw stability, liquid holding capacity, and oxidation stability of pork meatballs during long-term frozen storage. Therefore, our study suggest that plant-based protein emulsions can effectively replace animal fats while maintaining product quality, offering valuable implications for the meat processing industry.

Fabrication of ultrafine Himalayan walnut oil Pickering emulsions by ultrasonic emulsification: Techno-functional properties of emulsions and microcapsules.

In present scenario, much of the attention has been put on the production and utilization of Pickering emulsions deciphering enhanced stability and applicability over wide environmental conditions. In this context the present study was carried out to elaborate effect of different wall materials and pH systems on the physicochemical, structural and morphological properties of Himalayan walnut oil Pickering emulsions by ultrasonic emulsification. In this study, concentrated Pickering emulsion of Himalayan walnut oil (HWO) was prepared utilizing soy protein isolate (SPI), maltodextrin (MD) stabilized by pectin at varying concentrations and pH systems (4.0, 7.0). With increase in pectin and SPI concentration and lowering MD, stable emulsions were obtained as deciphered by an Emulsion stability index (ESI) of 100 for 7 days at ambient storage. HWO Pickering emulsions were analysed for particle size measurements (2.13-13.64 µm) and depicted negative zeta potential values (-3.70 to -18.58). Lyophilized HWO microcapsules depicted moderate encapsulation efficiency (44.69-57.63 %) whereas the hygroscopicity values of the microcapsule ranged from (0.21-12.10 %). Thermogravimetric analysis (TGA) of the samples depicted the temperature of maximum degradation rate up to 550 °C whereas XRD spectra depicted amorphous nature of oil microcapsules. FTIR spectra revealed a close association between the SPI-MD-Pectin matrix. SEM analysis revealed stable oil globules entrapped in protein-polysaccharide matrix with no visible cracks and fissures.

Preparation and characteristics of soy protein isolate - Sea buckthorn flavone emulsion and their effects of on quality and heterocyclic amines of roasted mutton granules.

A soy protein isolate (SPI) - sea buckthorn flavonoid emulsion was developed to study its effects on roasted lamb quality and heterocyclic amine (HAAs) precursors. The emulsion was stable with uniformly dispersed, well-encapsulated droplets averaging 0.1 to 10 µm. CLSM confirmed its good physical stability, small particle size, and uniform dispersion. FTIR the existence of hydrogen bond, hydrophobic interaction and physical adhesion between SPI and sea-buckthorn flavonoids. The emulsion improved lamb pellet texture by reducing chewiness and hardness, increasing adhesion, and decreasing browning. The emulsion-treated roasted mutton showed a 47.95-53.56 % increase in DPPH scavenging activity and MDA content reduction from 60.78 to 17.80 nmol/mg, indicating strong antioxidant activity and lipid oxidation inhibition. For both precursors and HAAs, there was a significant intensity of inhibition, where creatine decreased by about 44.91-68.34 %, glucose by 84.47 %-97.74 %, and the seven HAAs, Norharman, Harman, IQ, MeIQ, MeIQx, AαC, and PhIP, were inhibited by 79.64 %, respectively, 88.76 %, 65.07 %, 87.27 %, 96.16 %, 89.30 % and 49.44 %, respectively. This study aimed to develop a novel soy protein isolate-sea buckthorn flavonoid emulsion and evaluate its potential to improve roasted lamb quality while inhibiting the formation of harmful HAAs.

Effects of Soy Protein Isolate and Inulin Conjugate on Gel Properties and Molecular Conformation of Spanish Mackerel Myofibrillar Protein.

The gel properties and molecular conformation of Spanish mackerel myofibrillar protein (MP) induced by soy protein isolate-inulin conjugates (SPI-inulin conjugates) were investigated. The addition of SPI-inulin conjugates significantly enhanced the quality of the protein gel. An analysis of different additives was conducted to assess their impact on the gel strength, texture, water-holding capacity (WHC), water distribution, intermolecular force, dynamic rheology, Raman spectrum, fluorescence spectrum, and microstructure of MP. The results demonstrated a substantial improvement in the strength and water retention of the MP gel with the addition of the conjugate. Compared with the control group (MP), the gel strength increased from 35.18 g·cm to 41.90 g·cm, and WHC increased from 36.80% to 52.67% with the inclusion of SPI-inulin conjugates. The hydrogen bond content was notably higher than that of other groups, and hydrophobic interaction increased from 29.30% to 36.85% with the addition of SPI-inulin conjugates. Furthermore, the addition of the conjugate altered the secondary structure of the myofibrillar gel, with a decrease in α-helix content from 62.91% to 48.42% and an increase in ß-sheet content from 13.40% to 24.65%. Additionally, the SPI-inulin conjugates led to a significant reduction in the endogenous fluorescence intensity of MP. Atomic force microscopy (AFM) results revealed a substantial increase in the Rq value from 8.21 nm to 20.21 nm. Adding SPI and inulin in the form of conjugates is an effective method to improve the gel properties of proteins, which provides important guidance for the study of adding conjugates to surimi products. It has potential application prospects in commercial surimi products.

Rapidly molded sodium alginate/soy protein adhesive hydrogel with 808-nm laser inhibition of infected wounds.

Infected wounds produce pus and heal slowly. To address this issue, we developed a rapid-setting SP/SA@BP-C hydrogel by combining sodium alginate (SA) and soy protein (SP) with black phosphorus (BP) grafted with clarithromycin (Cla) and incorporating Ca2+ for chelation. This hydrogel dressing exhibits excellent photothermal (PT) and photodynamic (PD) bacteriostatic effects without biotoxicity, making it suitable for treating infected wounds. Characterization confirmed its successful fabrication, and the bacteriostatic effect demonstrated over 99 % efficacy through the synergistic effects of PT, PD, and Cla. Cellular studies indicated nontoxicity and a promoting effect on cell proliferation (121.6 %). In the mouse-infected wound model, the hydrogel led to complete healing in 12 days, with good recovery of the skin's superficial dermal layer and appendages. Consequently, SP/SA@BP-C is a natural hydrogel dressing with promising properties.

The Effect of High Hydrostatic Pressure (HHP) Induction Parameters on the Formation and Properties of Inulin-Soy Protein Hydrogels.

The aim of this study was to determine the effect of high hydrostatic pressure (HHP) induction parameters on the formation and properties of inulin-soy protein hydrogels. Solutions containing 20 g/100 g of inulin and 3 or 6 g/100 g of soy protein isolate (3 SPI; 6 SPI) were subjected to HHPs of 150, 300, or 500 MPa for 5, 10, or 20 min. The HHP parameters had no significant impact on the effectiveness of hydrogel formation. In most cases, the time of solution pressurization had no significant effect on the characteristics of hydrogels. However, increasing the induction pressure from 150 to 300 MPa resulted in hydrogels with different characteristics being obtained, e.g., more flattened microstructure; higher stability (only 3 SPI); higher yield stress, firmness, and adhesiveness; and lower spreadability. These changes were more noticeable in the hydrogels with lower protein content. An increase in the induction pressure (to 500 MPa) did not result in a significant strengthening of the hydrogel structure. However, in the case of 6 SPI hydrogels, induction with a pressure of 500 MPa had an unfavorable effect on their stability. The results indicate that HHP (300 MPa) can be used as an effective method for strengthening the structure of inulin-protein hydrogels.

Formation of thermal-induced microgels from soy protein hydrolysates: Effects of selective proteolysis on glycinin/ß-conglycinin.

This study explored the impact of selective proteolysis on the formation of thermally induced soy protein microgels. Glycinin hydrolysate (GH) and ß-conglycinin hydrolysate (CH) were obtained by subjecting soy protein isolate to selective proteolysis for different hydrolysis time (10-90 min), as confirmed by SDS-PAGE. In the early stages of hydrolysis, free sulfhydryl, surface hydrophobicity, storage modulus (G') and loss modulus (G″) of GH and CH increased, which enhanced their gelling potential. However, as hydrolysis time increased, the gel properties of the hydrolysates progressively weakened. Structural characterization of microgels revealed that GH yielded microgels with smaller particle sizes and coarser and relatively dispersed granular structures, while CH resulted in microgels with lower potential values, smoother surfaces, and lumps resembling strand-like formations. Analysis of the structure and intermolecular force of microgels showed that the microgel formed by the GH gradually tended to be disordered, whereas the secondary structure of microgels formed by CH showed lower random coil content, resulting in a dense gel network aggregated through disulfide bonding, hydrophobic interactions and hydrogen bonding as demonstrated by frequency-dependent storage moduli measurements. Overall, this study presents a thorough characterization of microgels and shows that they can be tailored by selective proteolysis, which enables controlling the ß-conglycinin/glycinin ratio of soy protein.

Pomegranate peel extract incorporated soy protein isolate/Artemisia sphaerocephala Krasch. gum composite films for fresh-cut apples preservation.

The objective of this study was to prepare an active packaging film using phosphorylated soy protein isolate (PPS) and Artemisia sphaerocephala Krasch. gum (ASKG) as film matrices, with the incorporation of pomegranate peel extract (PPE) to preserve fresh-cut apples. The results showed that PA-PPE (PPS/ASKG-PPE) films significantly increased thickness by 24.47 %, tensile strength by 58.76 %, and elongation at break by 30.48 %. Additionally, water vapor permeability and oxygen permeability decreased significantly to 6.17 × 10-13 and 0.62 × 10-13 Kg•m•m-2•s-1•Pa-1, respectively. FTIR, XRD, and SEM analyses confirmed the formation of intermolecular hydrogen bonds between PPS, ASKG, and polyphenols extracted from pomegranate peel, indicating excellent compatibility. Furthermore, radical scavenging activity experiments demonstrated that these films exhibited a remarkable ability to scavenge DPPH and ABTS+ radicals up to 70.44 % and 74.28 %, respectively, when the PPE content was at 3 wt%. Moreover, PPS could achieve a sustained release effect on polyphenols with a relatively low release rate (63.83 %) even after seven days' time elapsed. Finally, the PA-PPE film displayed superior performance in reducing the weight loss and browning index of fresh-cut apples within 24 h of storage. The development of PA-PPE film could promote sustainable resource protection and demonstrate promising prospects in the field of fresh-cut fruit packaging.

Effects of soy protein isolate interaction with brown rice starch on the multiscale structure of brown rice bread.

BACKGROUND: Gluten-free bread (GFB) has technical bottlenecks such as hard texture, rough taste and low nutrition in practical production. In order to solve these problems, this study used germinated brown rice starch as the main raw material, and investigated the effects of soybean isolate protein (SPI) on the multiscale structure of germinated brown rice starch and bread quality. RESULTS: A gluten-free rice bread process simulation system was established, and the interaction between SPI and starch in the simulation system was characterized. The result shows that the interaction forces between SPI and germinated brown rice starch were mainly represented by hydrogen bonds, and with the addition of SPI, the crystallinity of starch showed a downward trend. At the same time, when the amount of SPI was 3%, the appearance quality was the best and the specific volume of bread was 1.08 mL g-1. When the amount of SPI was 6%, the texture quality was the best. Compared with the bread without SPI, the hardness of the bread with 6% SPI was reduced by 0.13 times, the springiness was increased by 0.03 times, the color was the most vibrant, the L* value being 1.02 times the original, and the baking loss was reduced to 0.98 times the original. CONCLUSIONS: The interaction force between SPI and germinated brown rice starch and its effect on bread quality were clarified, and these results inform choices about providing a theoretical basis for the subsequent development of higher-quality GFB. © 2024 Society of Chemical Industry.

Improved encapsulation efficiency and storage stability of lutein by soy protein isolate nanocarriers with thermal and trypsin treatments.

BACKGROUND: Encapsulation of bioactive compounds within protein-based nanoparticles has garnered considerable attention in the food and pharmaceutical industries because of its potential to enhance stability and delivery. Soy protein isolate (SPI) has emerged as a promising candidate, prompting the present study aiming to modify its properties through controlled thermal and trypsin treatments for improved encapsulation efficiency (EE) of lutein and its storage stability. RESULTS: The EE of lutein nanoparticles encapsulated using SPI trypsin hydrolysates (SPIT) with three varying degrees of hydrolysis (4.11%, 6.91% and 10.61% for SPIT1, SPIT2 and SPIT3, respectively) increased by 12.00%, 15.78% and 18.59%, respectively, compared to SPI. Additionally, the photostability of SPIT2 showed a remarkable increase of 38.21% compared to SPI. The superior encapsulation efficiency and photostability of SPIT2 was attributed to increased exposure of hydrophobic groups, excellent antioxidant activity and uniform particle stability, despite exhibiting lower binding affinity to lutein compared to SPI. Furthermore, in SPIT2, the protein structure unfolded, with minimal impact on overall secondary structure upon lutein addition. CONCLUSION: The precise application of controlled thermal and trypsin treatments to SPI has been shown to effectively produce protein nanoparticles with substantially improved encapsulation efficiency for lutein and enhanced storage stability of the encapsulated lutein. These findings underscore the potential of controlled thermal and trypsin treatments to modify protein properties effectively and offer significant opportunities for expanding the applications of protein-based formulations across diverse fields. © 2024 Society of Chemical Industry.

Characterization of Plant-Based Meat Treated with Hot Air and Microwave Heating.

Plant-based meat is growing globally due to health, environmental, and animal welfare concerns, though there is a need for quality improvements. This study assessed how different ratios of wheat gluten (WG) to soy protein isolate (SPI) and various baking methods-hot air (HA), microwave (MW), and a combination of both (HA-MW)-affect the physicochemical properties of plant-based meat. Increasing the SPI from 0% to 40% significantly enhanced lightness, hardness, chewiness, water-holding capacity, moisture content, and lysine (an essential amino acid) (p ≤ 0.05). Hardness and chewiness ranged from 4.23 ± 1.19 N to 25.90 ± 2.90 N and 3.44 ± 0.94 N to 18.71 ± 1.85 N, respectively. Baking methods did not affect amino acid profiles. Compared to HA baking, MW and HA-MW baking increased lysine content (561.58-1132.50 mg/100 g and 544.85-1088.50 mg/100 g, respectively) while reducing fat and carbohydrates. These findings suggest that a 40% SPI and 60% WG ratio with microwave baking (360 W for 1 min) optimizes plant-based meat, offering benefits to both consumers and the food industry in terms of health and sustainability.

The Preparation of W/O/W High-Internal-Phase Emulsions as Coagulants for Tofu: The Effect of the Addition of Soy Protein Isolate in the Internal Water Phase.

Tofu quality is determined by a controlled coagulation process using a W/O/W emulsion coagulant. The impact of adding soy protein isolate (SPI) to the inner water phase on the stability of W/O/W high-internal-phase emulsions (HIPEs) and its application as a coagulant for tofu was assessed. No creaming occurred during 7-day storage with SPI concentrations up to 0.3%, while the emulsion droplets aggregated with 0.5% and 0.7% SPI. Emulsions containing 0.3% SPI maintained a constant mean droplet size after 21 days of storage and exhibited the lowest TURBISCAN stability index value. HIPE stability against freeze-thaw cycles improved after heating. HIPEs with SPI concentrations above 0.3% demonstrated an elastic gel-like behavior. The increased viscosity and aggregation of the protein around droplets indicated that the interaction among emulsion droplets could enhance stability. W/O/W HIPE coagulants significantly increased tofu yield, reduced hardness, and produced a more homogenous tofu gel compared to a MgCl2 solution. The HIPE with 0.3% SPI was found to be optimal for use as a coagulant for tofu.

Effect of Mono- and Polysaccharide on the Structure and Property of Soy Protein Isolate during Maillard Reaction.

As a protein extracted from soybeans, soy protein isolate (SPI) may undergo the Maillard reaction (MR) with co-existing saccharides during the processing of soy-containing foods, potentially altering its structural and functional properties. This work aimed to investigate the effect of mono- and polysaccharides on the structure and functional properties of SPI during MR. The study found that compared to oat ß-glucan, the reaction rate between SPI and D-galactose was faster, leading to a higher degree of glycosylation in the SPI-galactose conjugate. D-galactose and oat ß-glucan showed different influences on the secondary structure of SPI and the microenvironment of its hydrophobic amino acids. These structural variations subsequently impact a variety of the properties of the SPI conjugates. The SPI-galactose conjugate exhibited superior solubility, surface hydrophobicity, and viscosity. Meanwhile, the SPI-galactose conjugate possessed better emulsifying stability, capability to produce foam, and stability of foam than the SPI-ß-glucan conjugate. Interestingly, the SPI-ß-glucan conjugate, despite its lower viscosity, showed stronger hypoglycemic activity, potentially due to the inherent activity of oat ß-glucan. The SPI-galactose conjugate exhibited superior antioxidant properties due to its higher content of hydroxyl groups on its molecules. These results showed that the type of saccharides had significant influences on the SPI during MR.

Soy protein hydrolysates induce menaquinone-7 biosynthesis by enhancing the biofilm formation of Bacillus subtilis natto.

Menaquinone-7 (MK-7) is a form of vitamin K2 with health-beneficial effects. A novel fermentation strategy based on combining soy protein hydrolysates (SPHs) with biofilm-based fermentation was investigated to enhance menaquinone-7 (MK-7) biosynthesis by Bacillus subtilis natto. Results showed the SPHs increased MK-7 yield by 199.4% in two-stage aeration fermentation as compared to the SP-based medium in submerged fermentation, which was related to the formation of robust biofilm with wrinkles and the enhancement of cell viability. Moreover, there was a significant correlation between key genes related to MK-7 and biofilm synthesis, and the quorum sensing (QS) related genes, Spo0A and SinR, were downregulated by 0.64-fold and 0.39-fold respectively, which promoted biofilm matrix synthesis. Meanwhile, SPHs also enhanced the MK-7 precursor, isoprene side chain, supply, and MK-7 assembly efficiency. Improved fermentation performances of bacterial cells during fermentation were attributed to abundant oligopeptides (Mw < 1 kDa) and moderate amino acids, particularly Arg, Asp, and Phe in SPHs. All these results revealed that SPHs were a potential and superior nitrogen source for MK-7 production by Bacillus subtilis natto.

Comparison of Soy and Pea Protein for Cultured Meat Scaffolds: Evaluating Gelation, Physical Properties, and Cell Adhesion.

Cultured meat is under investigation as an environmentally sustainable substitute for conventional animal-derived meat. Employing a scaffolding technique is one approach to developing cultured meat products. The objective of this research was to compare soy and pea protein in the production of hydrogel scaffolds intended for cultured meat. We examined the gelation process, physical characteristics, and the ability of scaffolds to facilitate cell adhesion using mesenchymal stem cells derived from porcine adipose tissue (ADSCs). The combination of soy and pea proteins with agarose and agar powders was found to generate solid hydrogels with a porous structure. Soy protein-based scaffolds exhibited a higher water absorption rate, whereas scaffolds containing agarose had a higher compressive strength. Based on Fourier transform infrared spectroscopy analysis, the number of hydrophobic interactions increased between proteins and polysaccharides in the scaffolds containing pea proteins. All scaffolds were nontoxic toward ADSCs, and soy protein-based scaffolds displayed higher cell adhesion and proliferation properties. Overall, the soy protein-agarose scaffold was found to be optimal for cultured meat production.

Shear, extensional rheology, and tribology of polysaccharide-thickened soy protein-based liquid systems for dysphagia management.

Modifying food texture is a valuable approach to enhancing the quality of life for patients with dysphagia. Incorporating thickened soy protein-based liquid systems (SPLS) into their diet not only improves protein intake but also promotes safer swallowing. However, the properties of thickened SPLS are crucial for safe swallowing, may vary depending on the conformation of the thickened polysaccharides used. In this study, SPLS with different levels of thickening were prepared using xanthan gum, pectin and guar gum. The influence of polysaccharide conformation on the rheological (shear and extensional) and tribological properties of thickened SPLS was investigated. The results revealed that xanthan gum-thickened SPLS exhibiting the highest shear viscosity (110.073 Pa.s) and extensional viscosity (7.405 Pa.s), which increased with polysaccharide concentration. Meanwhile, xanthan gum possessed the strongest lubricating properties. These results shed light on the development of plant protein-based solutions for dysphagia management.

Soy protein isolate ameliorate gel properties by regulating the non-covalent interaction between epigallocatechin-3-gallate and myofibrillar protein.

This study primarily investigated the improvement of high-dose Epigallocatechin-3-Gallate (EGCG)-induced deterioration of MP gel by soy protein isolate (SPI) addition. The results showed that EGCG could interact with MP, SPI, and HSPI (heated), indicating the competitive ability of SPI/HSPI against EGCG with MP. EGCG was encapsulated by SPI/HSPI with high encapsulation efficiency and antioxidation, with antioxidant activities of 78.5% âˆ¼ 79.2%. FTIR and molecular docking results revealed that MP, SPI, and HSPI interacted with EGCG through hydrogen bonding and hydrophobic interactions. SPI/HSPI competed with MP for EGCG, leading to the restoration of MHC and Actin bands, alleviating the aggregation caused by EGCG and oxidation. Additionally, SPI/HSPI-E significantly reduced the high cooking loss (23.71 and 26.65%) and gel strength (13.60 and 17.02%) induced by EGCG. Hence, SPI competed with MP for EGCG binding site to ameliorate MP gel properties, thereby alleviating the detrimental changes in MP caused by high-dose EGCG and oxidation.

Protein blend extrusion: Crafting meat analogues with varied textural structures and characteristics.

With an increasing emphasis on health and environmental consciousness, there is a growing inclination toward plant protein-based meat substitutes as viable alternatives to animal meat. In the pursuit of creating diverse and functional plant protein-based substitutes, innovative plant proteins have been introduced in conjunction with soy protein isolate (SPI), encompassing pea protein isolate (PPI), rice bran protein (RBP), fava bean protein isolate (FPI), and spirulina protein isolate (SPPI). Notably, SPI-WG extrudates and SPI-PPI extrudates exhibited superior fiber structures (fiber degrees were 1.72 and 1.88, respectively), with coarse fibers in SPI-WG extrudates and fine, dense fibers in SPI-PPI extrudates. The addition of RBP, FPI and SPPI had minimal effect on fiber structure. Fresh SPI-FPI displayed the slowest rate of water loss, losing about 7.11% of their total weight in 5 h. Different plant proteins can be selected for the preparation of plant protein-based meat substitutes according to practical needs.