Total Sulfhydryl Content Research Articles

Enzymatic production and physicochemical and functional properties of sorghum protein isolates.

Grain sorghum has emerged as a promising source for producing alternative proteins, yet current extraction methods lack efficiency. In this study, a novel enzymatic approach using α-amylase and cellulase on sorghum materials was developed to address this challenge. Comparisons were made among the proteins isolated from dry-milled sorghum flours, wet-milled sorghum gluten meals, and sorghum dried distiller's grains (DDG). Remarkably, proteins obtained from sorghum gluten meals demonstrated the highest protein purity (83-85 %) and recovery rate (92-93 %), followed by those from sorghum flour (purity 75-76 %) and DDG (purity 45-50 %). Physicochemical properties and functionalities of the isolated sorghum proteins were analyzed and compared with common commercial plant proteins (e.g., soy protein isolate, pea protein isolate, and wheat gluten). Sorghum proteins exhibited higher levels of crude fat content, α-helix, and random coil structures, along with higher surface hydrophobicity and oil holding capacity (OHC) compared to the commercial plant protein isolates. Notably, proteins extracted from sorghum flours displayed slightly higher α-helix and random coil structures, total sulfhydryl content, water holding capacity (WHC), OHC, and protein digestibility compared to proteins isolated from sorghum gluten meals. Overall, this study demonstrates that enzymatic processing is feasible in producing sorghum proteins and provides insights into their basic properties and functionalities.

Effects of freeze-thaw cycles and heat treatment on the odor-binding properties of myofibrillar protein to key fishy compounds

This study investigated the effects of different freeze-thaw (F-T) cycles and subsequent heat treatment on the odor-binding properties of myofibrillar protein (MP) in grass carp to four key fishy substances. The odor-binding ability of MP significantly decreased as freeze-thaw (F-T) cycles increased (p < 0.05). After heating, the odor-binding ability of MP further decreased. Freeze-thaw treatment induced the oxidative denaturation, decreased total sulfhydryl content and unfolded the α-helix in MP, which modified and re-buried the exposed odor-binding sites, reducing odor-binding ability. After heating, the oxidative damage and aggregation of MP induced by freeze-thaw cycles, along with thermal effects, synergistically accelerated the oxidative denaturation and formation of disordered structures of heated MP. Enhanced hydrophobic interactions led to a dominant aggregation effect, which reduced the binding sites and further decreased the odor-binding ability of heated MP, resulting in more release of odors.

Fucoidan-Vegetable Oil Emulsion Applied to Myosin of Silver Carp: Effect on Protein Conformation and Heat-Induced Gel Properties.

How to improve the gel properties of protein has become a research focus in the field of seafood processing. In this paper, a fucoidan (FU)-vegetable oil emulsion was prepared, and the mechanism behind the effect of emulsion on protein conformation and the heat-induced gel properties was studied. The results revealed that the FU-vegetable oil complex caused the aggregation and cross-linking of myosin, as well as increased the surface hydrophobicity and total sulfhydryl content of myosin. In addition, the addition of the compound (0.3% FU and 1% vegetable oil) significantly improved the gel strength, hardness, chewiness, and water-holding capacity of the myosin gel (p < 0.05). In particular, when the addition of camellia oil was 1%, the gel strength, hardness, chewiness, and water-holding capacity had the highest values of 612.47 g.mm, 406.80 g, 252.75 g, and 53.56%, respectively. Simultaneously, the emulsion (0.3% FU-1% vegetable oil) enhanced the hydrogen bonds and hydrophobic interaction of the myosin gels. The image of the microstructure showed that the emulsion with 0.3% FU-1% vegetable oil improved the formation of the stable three-dimensional network structure. In summary, the FU-vegetable oil complex can promote unfolding of the protein structure and improve the gel properties of myosin, thus providing a theoretical basis for the development of functional surimi products.

Enhanced oxidative stability and quality of chilled mirror carp fillet using an antioxidant film of chitosan/clove essential oil nanoemulsion

This study evaluates the effects of chitosan/clove essential oil nanoemulsion antioxidant films (CH-CEON) on the oxidative stability and quality of chilled mirror carp fillets. During storage, increased lipid and protein oxidation of all samples was observed, which resulted in a darker color, a softer texture, and increased water loss. Compared to the control, the oxidation and quality deterioration were inhibited in other samples, with the best effect was observed in those treated with CH-CEON. The peroxide value, thiobarbituric acid reactive substances (TBARS), total viable count, pH, total volatile basic nitrogen (TVB-N), b*, centrifugal, and cooking loss of samples treated with CH-CEON were 20.8%, 37.4%, 20.6%, 4.5%, 58.8%, 13.5%, 23.4%, and 11.1% lower than the control at 12 days, respectively. Conversely, the active and total sulfhydryl content, L*, a*, and whiteness (W) increased by 64.4%, 31.9%, 13.4%, 186%, and 15.3%, respectively. The texture of the treated samples was improved, and the shelf life was extended by 5 days. These changes were attributed to the slow release of phenolics in the films, which inhibited oxidation and quality deterioration of fish by scavenging free radicals. Moreover, the nanoemulsion increased the contact between clove essential oil (CEO) and samples, adsorbing free radicals more efficiently. This highlights the significant potential of CH-CEON for application in fish preservation.

L-lysine enhances pork color through antioxidant activity and myoglobin conformational changes

This study aimed to investigate the effect of L-lysine (Lys) on the color of pork and reveal the possible mechanism. The results showed that the L* and a* values increased from 53.69 to 56.32, 56.39, and 56.47, and from 12.93 to 13.21, 13.24, and 13.52 with the addition of 0.1 %, 0.15 % and 0.2 % Lys, respectively. Meanwhile, the oxymyoglobin (Fe2+) levels increased from 21.14 % to 22.63 %, 23.83 %, and 23.53 %, while the metmyoglobin (Fe3+) levels decreased from 44.69 % to 40.28 %, 41.21 %, and 41.63 % with the addition of 0.1 %, 0.15 % and 0.2 % Lys, respectively. Additionally, the addition of Lys increased total sulfhydryl and active sulfhydryl contents, and decreased the levels of reactive oxygen species (ROS) (P<0.05). The particle size and the absolute value of the ζ-potential increased with the addition of Lys, reaching maximum values of 534.39 nm and −13.73 mV, respectively. The molecular dynamics results suggested that Lys can bind to myoglobin (Mb) through hydrophobic interactions and hydrogen bonds, forming a stable Lys-Mb complex, acting as a protective shield to prevent the entry of ROS and other oxidizing agents. Finally, the addition of 0.15 % Lys resulted in the highest surface hydrophobicity, which was 5.79 μg. The multispectral results indicated that Lys primarily induces changes in the secondary and tertiary structures of Mb through interactions with tyrosine residues. These changes stabilized the free-moving rings within the amino acid residues of Mb, thereby improving the structural stability of Mb and ultimately enhancing the color stability of pork. In summary, Lys improved meat color stability through a dual mechanism of antioxidation and interaction with Mb to alter its conformational stability.

Effects of sodium carboxymethyl cellulose-tea polyphenols ice coating on the quality degradation of frozen-thawed beef due to changes in protein structure and fat and protein oxidation

During freeze-thaw (FT) cycles, protein structural degradation, lipid and protein oxidation can lead to quality deterioration of beef samples. To address this issue, we developed a cost-effective and easy-to-operate carboxymethyl cellulose sodium-tea polyphenol (CMC-TP) ice coating to inhibit quality deterioration caused by these factors. The beef samples were characterized for various quality attributes, lipid and protein oxidation, and protein structure. The results demonstrated that the CMC-TP ice coating significantly inhibited the deterioration in water-holding capacity (WHC) and tenderness of the beef samples (P < 0.05). Analysis of peroxide value (POV), thiobarbituric acid (TBARS), total volatile basic nitrogen (TVB-N), and carbonyl content revealed that the CMC-TP ice coating significantly suppressed lipid and protein oxidation during FT cycles (P < 0.05). Additionally, assessments of total sulfhydryl content, fluorescence intensity, and surface hydrophobicity indicated that the CMC-TP ice coating effectively mitigated protein structural degradation through antioxidant and cryoprotective effects (P < 0.05). Therefore, the CMC-TP ice coating can enhance the FT stability of beef.

Identification of Key Volatile Compounds in Tilapia during Air Frying Process by Quantitative Gas Chromatography-Ion Mobility Spectrometry.

Air frying as a new roasting technology has potential for roasted fish production. In this study, the changes in volatile compounds (VCs) during air frying of tilapia were studied by quantitative gas chromatography-ion mobility spectrometry, followed by the identification of key VCs based on their odor activity value (OAV). There were 34 verified VCs, of which 16 VCs were identified as the key VCs with OAV ≥ 1. Most of the VCs were improved by air frying and peaked at 20 min. During the air frying, the total sulfhydryl content markedly decreased, while the protein carbonyl and MDA content significantly increased, suggesting the enhancement in the oxidation of lipids and proteins. The correlation network among the chemical properties and key VCs was constructed. The change in total sulfhydryl, protein carbonyl, and MDA showed significant correlation with most of the key VCs, especially 2-methyl butanal, ethyl acetate, and propanal. The results indicated that the oxidation of lipids and proteins contributed the most to the flavor improvement in air-fried tilapia. This study provides a crucial reference for the volatile flavor improvement and pre-cooked product development of roasted tilapia.

Covalent interaction of ovalbumin with proanthocyanidins improves its thermal stability and antioxidant and emulsifying activity.

The structure of proanthocyanidins (PC) contains a large number of active phenolic hydroxyl groups, which makes it have strong antioxidant capacity. This study investigated the structural and functional properties of ovalbumin (OVA) modified by its interaction with PC. It was found that on increasing the concentration ratio of PC to OVA from 10:1 to 40:1, the free amino and total sulfhydryl contents of OVA decreased from 470.59 ± 38.77 and 29.81 ± 0.31 nmol mg-1 to 96.61 ± 4.55 and 21.22 ± 0.78 nmol mg-1, respectively, and the free sulfhydryl content increased from 7.65 ± 0.41 to 9.48 ± 0.58 nmol mg-1. These results indicated that CN and CS bonds were formed and PC was covalently linked with OVA. The PC content in the OVA-PC conjugates increased from 281.93 ± 12.92 to 828.81 ± 46.09 nmol mg-1 on increasing the concentration ratio of PC to OVA from 10:1 to 40:1. The contents of α-helix and β-turn of OVA decreased, and the contents of β-sheet and random coil increased, confirmed by circular dichroism. The tertiary structure of OVA was also altered according to the results of fluorescence and ultraviolet absorption spectra. The surface hydrophobicity of OVA-PC conjugates decreased with increasing bound polyphenol content. The conjugation of OVA to PC significantly improved its emulsification and antioxidant activity and denaturation temperature. This study may provide valuable information for improving OVA's functional properties and its PC conjugates for applications in the food industry. © 2024 Society of Chemical Industry.

Acute effect of gold nanoparticles on neuropathic pain in a model of regional complex pain syndrome

We evaluated the effects of gold nanoparticles (AuNPs) administered in the acute phase of an animal model of Complex Regional Pain Syndrome Type I (CRPS-I). Oxidative stress parameters [substances reactive to thiobarbituric acid (TBA-RS), total sulfhydryl content (SH), protein carbonyl content and the activities of catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px)] and pain, through mechanical and thermal allodynia, were evaluated in the blood and sciatic nerves of mice. Animals were anesthetized and an elastic tourniquet was used around the left hind paw for 120 minutes, followed by measurements of the mechanical threshold and thermal. Animals received intraperitoneal administrations of AuNPs at concentrations of 2.5 mg/L, 7.0 mg/L and 22.0 mg/L, Ankyrin Transient Potential Receptor 1 (TRPA1) antagonist (HC030031) or saline vehicle after induction of CRPS-I. AuNPs showed significant results in thermal and mechanical anti-allodynic effects on day 1 (2.5 mg/L), days 2 and 3 (7.0 and 22.0 mg/L). The TRPA1 reduced mechanical allodynia (days 1 and 2) and thermal allodynia (days 1, 2 and 3), in addition to reversing the changes caused by CRPS-I in oxidative stress. The CRPS-I model increased TBA-RS, reduced the total sulfhydryl content and increased CAT activity. The results showed that, at all concentrations, AuNPs reversed the increase in CAT. At 7.0 mg/L partially reversed and at 22.0 mg/L completely reversed the increase in TBA-RS levels and at 22.0 mg/L reversed the reduction in sulfhydryl content.

Effect of Dry Processing of Coconut Oil on the Structure and Physicochemical Properties of Coconut Isolate Proteins.

The effects of the dry processing of coconut oil on the amino acid composition, molecular weight, secondary structure, solubility, surface hydrophobicity, microstructure, total sulfhydryl and free sulfhydryl content, free amino acid content, thermal properties, and water-holding, oil-holding, foaming, and emulsifying properties of coconut isolate protein were investigated. The results showed that the dry processing altered the amino acid composition of coconut isolate proteins as well as resulted in fewer irregular structural regions and more homogeneous particle sizes, leading to an improvement in the thermal stability of the proteins. SDS-PAGE analysis showed that globular proteins located at ~34 kDa in coconut isolate proteins underwent slight degradation during the dry processing of coconut oil. The dry processing reduced the surface hydrophobicity, total and free sulfhydryl groups, solubility, and free amino acid content of coconut isolate proteins. In addition, the water-holding capacity, oil-holding capacity, and foam stability of coconut isolate proteins were improved to different degrees after the dry processing. Therefore, the development and utilization of copra meal protein is of great significance to increase its added value.

Characteristics of Films Prepared from Wheat Gluten and Phenolic Extracts from Porphyra haitanensis and Its Application for Salmon Preservation.

The effect of wheat gluten (WG)/phenolic extracts (PE) coating on the storage qualities of salmon fillets was studied. Porphyra haitanensis, belonging to red algae, possesses abundant phenolic compounds. Films were prepared by incorporating phenolic extracts (0, 0.5%, 0.75%, and 1.0%, w/v) from Porphyra haitanensis to WG. The PE showed strong antioxidant activities by scavenging DPPH and ABTS radicals. The increased addition of PE to WG film significantly increased tensile strength compared to that of WG film, but reduced water vapor permeability. The quality of salmon fillet stored at 4 °C from 0 to 9 days was decreased due to the oxidation of lipid and protein. However, the increased addition of PE to WG significantly reduced pH, TVB-N, TBA, peroxide value, total sulfhydryl content, and carbonyl content of salmon fillet compared to control salmon fillet. In addition, the increased addition of PE to WG also significantly improved water holding capacity, hardness, chewiness, and springiness of salmon fillet during storage compared to those of control salmon fillet. Taken together, this study showed phenolic extracts from Porphyra haitanensis improved wheat gluten-based film properties and further enhanced the qualities of coated salmon fillet during storage.

Effect of freezing on physicochemical properties and microstructure of soy protein gels

This study aimed to analyze the dynamic evolution of physicochemical properties and microstructure in soybean protein gels subjected to freezing conditions. SPI, 7S, and 11S were used in experiments. A 12g/100g protein gel was formulated after 1 and 5 days of freezing. Subsequent determination and analysis encompassed various indices, including texture, subunit composition, sulfhydryl group content, water distribution, and microstructure. The findings revealed a significant increase in the hardness of SPI, 7S, and 11S protein gels with prolonged freezing time. The 11S gel exhibited the most substantial increase, followed by SPI and 7S. And the decreases in the water-holding properties of the protein gels were 10.08%, 1.19%, and 49.34%, with the largest decrease in the water-holding properties of the 11S protein gels. Conversely, the water-holding capacity and total sulfhydryl content of SPI, 7S, and 11S protein gels decreased over time during freezing. Subunit distribution analysis indicated darker bands at the top of concentrated and separation gels. The freezing process induced the formation and growth of ice crystals, altering the spatial network structure of protein gels. Consequently, the proportion of free water in all three soybean protein gels increased, leading to enhanced mobility and a looser network structure.

Uncovering quality changes of shrimp (Penaeus vannamei) during solar drying and its relationship with protein-related properties

This study explored the intrinsic relationship between the quality traits and protein-related property changes during the solar drying of shrimps (Penaeus vannamei). During drying, the shrimp exhibited a gradual decline in L*a*b* values and a notable increase in the hardness and chewiness. Proteins were degraded and oxidized. Especially, the trichloroacetic acid-soluble peptide and carbonyl contents increased, whereas the total sulfhydryl content decreased. The proportions of different types of intramolecular bonds were significantly changed. The ionic and hydrogen bonds greatly decreased to 10.72% and 9.05% and the hydrophobic and disulfide bonds notably increased to 19.38% and 28.19%, indicating the changes in the spatial structure of the protein and its denaturation during the drying process. The Pearson's correlation analysis showed that protein degradation and denaturation greatly affected the textural properties and protein oxidation caused color changes. The result of this work provides a theoretical support for improving the quality of shrimp products.

Cryoprotective effect of low molecular-mass nitrogen compounds on the myofibrillar protein of the jumbo squid (Dosidicus gigas) muscle

The study aimed to evaluate the low molecular-mass nitrogen compounds (LMMNC) arginine (Arg), taurine (Tau), and trimethylamine oxide (TMAO) (individually or their mixtures) cryostabilizing effect over jumbo squid (Dosidicus gigas) myofibrillar protein (JSMP) frozen at -20°C for 0, 30, and 90 days. Washed muscle (three times, 1:3, muscle:water) was lyophilized (sample). Washing water was ultrafiltrated (&lt;1 kDa cut-off) and permeate lyophilized (&lt;1 kDa fraction). LMMNC, Control+ (with &lt;1 kDa fraction)] added at muscle concentration and control (washed-muscle only) were stored at -20 °C. Cryoprotective effect on JSMP was evaluated by differential scanning calorimetry, surface hydrophobicity (SoANS), solubility, and total-sulfhydryl (TS) content. Myosin thermal stability increased (P ≤ 0.05) in Control+ (43.6 ± 0.1), TMAO (44.3 ± 0.3), and Arg + TMAO (44.2 ± 0.9) compared to Con (42.6 ± 0.3) before freezing (day 0). At 90 days of storage, all TMAO-involved treatments and Control+ remained higher (p ≤ 0.05) than Control. Solubility increased (p ≤ 0.05) in Tau (11.2±0.0-12.8±0.1) and Arg+Tau (10.6±0.1-12.7±0.0) comparing day 0 vs. 90, respectively. LMMNC reduced SoANS (p ≤ 0.05, Arg+Tau+TMAO) throughout storage. LMMNC reduced (p &gt; 0.05) TS in most treatments. LMMNC, especially Taurine and TMAO, protects JSMP from freezing denaturation, stabilizing its structure.

Effect of water migration on changes of quality and volatile compounds in frozen Penaeus monodon

The purpose of this study was to clarify effects of water changes on the quality and volatile compounds of Penaeus monodon during frozen storage. The content of immobilized water decreased significantly while the bound water and free water increased significantly. Total sulfhydryl content, and Ca2+-ATPase activity decreased significantly to 68.31 μmol/g and 0.127 U/mg, meantime, carbonyl content and MFI value increased significantly to 2.04 μmol/g prot and 55.10. Total of 50 volatile compounds were identified. Nonanal (M & D), 2-nonanone and octanal were only detected in fresh samples, while 3-hydroxy-2-butanone and 1-hydroxy-2-propanone were only found in the samples after 20 days of storage. Correlation analysis revealed that 6 of the volatile compounds were associated with the change of free water. Total of 28 and 17 volatile compounds showed significant correlations with the immobilized water and bound water, respectively. Four volatile compounds have the potential to be used as the flavor marker.

Analysis of quality-related proteins in golden pompano (Trachinotus ovatus) fillets with modified atmosphere packaging under superchilling storage

Here, we aimed to study the changes in proteome of golden pompano fillets during post-mortem storage. Tandem mass tags (TMT)-labeled quantitative proteomic strategy was applied to investigate the relationships between protein changes and quality characteristics of modified atmosphere packaging (MAP) fillets during superchilling (-3 ℃) storage. Scanning electron microscopy was used to show that the muscle histology microstructure of fillets was damaged to varying degrees, and low-field nuclear magnetic resonance was used to find that the immobile water and free water in the muscle of fillets changed significantly. Total sulfhydryl content, TCA-soluble peptides and Ca2+-ATPase activity also showed that the fillet protein had a deterioration by oxidation and denaturation. The Fresh (FS), MAP, and air packaging (AP) groups were set. Total of 150 proteins were identified as differential abundant proteins (DAPs) in MAP/FS, while 209 DAPs were in AP/FS group. The KEGG pathway analysis indicated that most DAPs were involved in binding proteins and protein turnover. Correlation analysis found that 52 DAPs were correlated with quality traits. Among them, 8 highly correlated DAPs are expected to be used as potential quality markers for protein oxidation and water-holding capacity. These results provide a further understanding of the muscle deterioration mechanism of packaging golden pompano fillets during superchilling.

Colour stability improving of yellowfin tuna slices by compound antioxidant against oxidation of myoglobin

SummaryBrown stain is a major problem for tuna during storage. This study aimed to investigate the impact of antioxidants on myoglobin oxidation and the promotion of metmyoglobin (MetMb) reduction in tuna slices. Response surface methodology (RSM) was used to optimise the formula of the compound antioxidant in yellowfin tuna (YFT) slices, with the percentage of MetMb as the response value. The ratios of ε‐polylysine, sodium lactate and D‐sodium ascorbate were 0.43%, 2.21% and 2.71%, respectively. The interactions between sodium lactate and D‐sodium ascorbate had a greater impact on the percentage of MetMb. Then, verification experiments were conducted, and the results revealed that the samples treated with compound antioxidants had higher a* values, total sulfhydryl content, Ca2+‐ATPase activity, total reducing activity (TRA) and MetMb‐reducing activity (MRA) and lower percentages of MetMb and carbonyl contents than did the control samples. It also helps to maintain the stability of the NADH/NAD+ ratio, which contributes to facilitating MetMb reduction. The results showed that the compound antioxidant significantly inhibited myoglobin oxidation, promoted the reduction of MetMb in tuna slices and significantly enhanced the myoglobin stability of refrigerated YFT slices.

Role of ultrasonic freezing­treated pork dumpling filling during frozen storage: Insights from protein oxidation, aggregation, and functional properties

The effects of air freezing (AF), immersion freezing (IF), and ultrasonic freezing (UF) on the oxidation, aggregation, and functional properties of myofibrillar protein (MP) in pork dumpling filling during frozen storage were investigated. The findings demonstrated that, compared to AF and IF treatments, UF treatment had higher total and reactive sulfhydryl content, solubility, and absolute zeta potential. Conversely, it exhibited lower values in carbonyl content, dityrosine content, turbidity, and particle size within the same storage time (p < 0.05). SDS-PAGE revealed that UF treatment delayed the oxidation and excessive aggregation of MP during frozen storage. Moreover, samples treated with UF at 180 days (d) displayed similar functional and qualitative characteristics to those treated with IF at 90 d or AF at 60 d, as per the hierarchical cluster analysis findings. In conclusion, UF effectively delayed the oxidation, aggregation, and loss of functional properties of MP in pork dumpling filling during frozen storage.

Insight into quality, microstructure, and protein physicochemical properties of Monopterus albus frozen with liquid nitrogen

Monopterus albus is highly susceptible to spoilage due to high protein and moisture contents while frozen storage can effectively prolong the shelf-life. To study the effect of liquid nitrogen freezing (LNF) on quality, microstructure of ice crystal and muscle fiber, and physicochemical properties of proteins, Monopterus albus was frozen at -20 °C by refrigerator (RF, control), -50 °C, -80 °C, and -110 °C by LNF, respectively. The -110 °C LNF exhibited the highest freezing rate among four groups, contributing to the formation of small ice crystals with more uniform distribution and alleviating the damage to muscle fiber. In -110 °C LNF group, protein secondary structure changed relatively subtle, resulting in high protein solubility, Ca2+-ATPase activity, and total sulfhydryl content, as well as low surface hydrophobicity and disulfide bond content. LNF retarded the rise of TVB-N value, prevented the loss of immobilized and free water, and maintained water holding capacity and shear force. In conclusion, -110 °C LNF was recommended a promising freezing process for frozen Monopterus albus due to less alteration of quality and alleviation of protein denaturation.

Effects of moderate electric fields on the structural and gelling properties of soybean protein isolate gel induced by glucono-δ-lactone

To investigate the effects of moderate electric fields (MEF) treatment on the gelling properties of soybean protein isolate (SPI) gels induced by glucono-δ-lactone (GDL), SPI was treated by applying different electric field intensities (EFI) before GDL-induced gelation. The structure of SPI (4% and 6%, w/v) was characterized via particle size distribution, ζ-potential, fluorescence spectra, and total free sulfhydryl content. The effects of MEF treatment on the acidification pH, rheological properties, water-holding capacity (WHC), textural properties, intermolecular forces, and microstructure of GDL-induced SPI gels were investigated. The results revealed that the SPI gels treated with EFI 4 V/cm aggregated faster during acidification, with higher storage modulus, stronger gel texture, and better deformation resistance. The WHC of the gel was enhanced, and the gel network was finer and more uniform. The results suggested that MEF treatment can improve the characteristics of vegetable protein gels.