Effect of chickpea (Cicer arietinum L.) protein isolate on the heat-induced gelation properties of pork myofibrillar protein.

BACKGROUND: Heat-induced composite gels were prepared with 30 mg mL-1 pork myofibrillar protein (MP) and chickpea protein isolate (CPI) (0, 3, 6, 9, 12, and 15 g kg-1 ) in 0.6 mol L-1 NaCl, at pH 7.0. The gel strength, water-holding capacity, rheological properties, and microstructure of MP-CPI composite gels were investigated. RESULTS: Chickpea protein isolate improved (P < 0.05) gel strength and water-holding capacity of the MP composite gels. The rheological properties of MP-CPI composite gels were improved significantly by the addition of CPI. Meanwhile, the effects of CPI on the storage modulus of composite gels were positively correlated with the increased addition of CPI. Furthermore, according to low-field nuclear magnetic resonance (LF-NMR) results, the addition of CPI reduced the relaxation time of the composite gels and the relaxation peak area of free water, indicating that CPI could improve the water-holding capacity of MP-CPI composite gels. The microstructure of MP-CPI composite gels presented smaller and more uniform pores, which means that more water could be retained. CONCLUSION: The addition of chickpea protein isolate improved the gel strength, water-holding capacity, rheological properties, and microstructure of MP gels, indicating that CPI could be a potential protein additive to improve the microstructure, texture, and functional quality of meat products. © 2020 Society of Chemical Industry.

Gelation and microstructural properties of fish myofibrillar protein gels with the incorporation of l-lysine and l-arginine at low ionic strength.

BACKGROUND: The solubility limitation and poor gelation properties of myofibrillar proteins at low ionic strength are the most challenging obstacle to limit salt reduction in meat products. In the present study, five amino acids with different concentrations of 5, 10 15, and 20 mmol L-1 , l-lysine (Lys), l-arginine (Arg), l-histidine (His), l-proline (Pro) and l-glycine (Gly), were introduced into myofibrillar protein (MP) suspensions at low ionic strength to improve solubility and gelation properties. RESULTS: The dynamic rheological analysis showed that the MPs at 100 mmol L-1 NaCl containing 15/20 mmol L-1 Lys/Arg exhibited similar gelling behaviors to MPs at 600 mmol L-1 NaCl. Similarly, 15/20 mmol L-1 Lys/Arg significantly increased the solubility of MPs and the water holding capacity (WHC) and gel strength of MP gels, which was comparable to those of MPs at 600 mmol L-1 NaCl. Furthermore, Lys and Arg promoted the formation of aggregation-type gel with a dense and compact structure observed by scanning electron microscopy. The gels containing 15/20 mmol L-1 Lys/Arg exhibited a significant increase in the proportion of immobilized water (P21 ). CONCLUSION: The enhancement of WHC, gel strength, and P21 was closely associated with the increased solubility and the dense microstructure induced by Lys and Arg with high concentrations of 15 and 20 mmol L-1 . The knowledge obtained from this study may be useful for the improvement of gelation properties of MPs at low ionic strength using l-lysine and l-arginine. © 2021 Society of Chemical Industry.

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review.

To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic-protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat-induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose-dependent and dual-role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross-linked three-dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.

Improvement of gelation properties of Penaeus vannamei surimi by magnetic field-assisted freezing in combination with curdlan.

Traditional methods of freezing and thawing may harm the quality of meat products. In order to reduce the negative impact of freezing on surimi products, the magnetic field-assisted freezing method is combined with various curdlan ratios to enhance the gelation characteristics of Penaeus vannamei surimi in this study. The results showed that the magnetic field-assisted freezing technique significantly improved the quality of thawed surimi compared with soaking freezing (SF), whereas the addition of curdlan further improved the gelation properties, and the gel strength, water-holding capacity, textural properties, whiteness, and G' value were significantly improved when its content was increased to 0.6 %. However, excessive amounts of curdlan interfered with protein covalent cross-linking, leading to a decrease in gel quality. Additionally, the addition of magnetic field and curdlan encouraged the shift of the α-helix to the random coil and ß-sheet transition, which stimulated the growth of myofibril molecules, exposed the hydrophobic groups and thiols, improved protein-molecule interactions, and promoted systematic gathering of proteins, leading to the formation of the microstructure of dense and small pores. It also resulted in a drop in water release, an increase in the proton density and a shift in the water condition from free water to more immobile water, which had higher sensory qualities. These effects together resulted in a reduction in thawing and cooking loss to 11.41 % and 13.83 %, respectively. These results also help to clarify the gelation process of shrimp surimi and help to regulate the gelation characteristics of shrimp surimi products.

Gelation of crocodile myofibrillar protein - κ-carrageenan mixtures in two low-NaCl solution.

Crocodile meat is a novel reptile meat source, but its processing method is rare. This study investigated the effect of κ-carrageenan addition and partial substitution of NaCl on the gel properties of crocodile myofibrillar protein (CMP). Result showed that CMP formed gel when temperature above 60 ℃. The water-holding capacity, gel strength, denaturation degree, sulfhydryl content covalent bond and hydrophobic bond of gel in KCl solution were significantly higher than those in CaCl2 solution (P < 0.05). K+ induced CMP to form a tight network structure with uniform small pores though covalent and hydrophobic bonds, but the gel properties were reduced by κ-carrageenan. In CaCl2 solution, κ-carrageenan improved the gel structure by filling the protein network through hydrogen bonding. Therefore, it can be concluded that KCl is better than CaCl2 in the manufacturing of low-sodium crocodile foods. Moreover, κ-carrageenan was only beneficial to gel quality in CaCl2 solution.

Characterization of bamboo shoots dietary fiber modified by ball milling and its role in altering the physicochemical properties of shrimp surimi.

A simple but robust strategy of ball milling (20 Hz, 30 Hz for 30 s, 60 s, 120 s, 180 s) was utilized to modify bamboo shoots fiber (BSDF) in shrimp surimi. The water holding capacity, swelling capacity, and oil binding capacity of 30 Hz-60 s milled BSDF exhibited the highest values of 5.61 g/g, 3.13 mL/g, and 6.93 g/g, significantly higher (P < 0.05) than untreated one (3.65 g/g, 2.03 mL/g, 4.57 g/g). Ball-milled BSDF exhibited a small-sized structure with the relative crystallinity decreased from 40.44 % (control) to 11.12 % (30 Hz-180 s). The myosin thermal stability, gelation properties of surimi were significantly enhanced by incorporating 20 Hz-120 s and 30 Hz-60 s BSDF via promoting protein unfolding, covalent hydrophobic interactions, and hydrogen bonding. A matrix-reinforcing and water entrapping effect was observed, exhibiting reinforced networks with down-sized water tunnels. However, BSDF modified at 180 s contributed to over-aggregated networks with fractures and enlarged gaps. Appropriate ball-milled BSDF (20 Hz-120 s, and 30 Hz-60 s) resulted in a significant decrease in α-helix (P < 0.05), accompanied by an increase of ß-sheets and ß-turn. This work could bring some insights into the applications of modified BSDF and its roles in the gelation of surimi-based food.

Modulation of the conformation, water distribution, and rheological properties of low-salt porcine myofibrillar protein gel influenced by modified quinoa protein.

High-pressure homogenization modified quinoa protein (HQP) was added to porcine myofibrillar proteins (MP) to study its the influence on protein conformation, water distribution and dynamical rheological characteristics of low-salt porcine MP (0.3 M NaCl). Based on these results, the WHC, gel strength, and G' value of the low-salt MP gel were significantly improved with an increase in the added amount of HQP. A moderate amount of HQP (6%) increased the surface hydrophobicity and active sulfhydryl content of MP (P < 0.05). Moreover, the addition of HQP decreased particle size and endogenous fluorescence intensity. FT-IR results indicated that the conformation of α-helix gradually converted to ß-sheet by HQP addition. The incorporation of HQP also shortened the T2 relaxation time and enhanced the proportion of immobile water, contributing to the formation of a compact and homogeneous gel structure. In conclusion, the moderate addition of HQP can effectively enhance the structural stability and functionality of low-salt MP.

Exploring gelation properties and structural features on 3D printability of compound proteins emulsion gels: Emphasizing pH-regulated non-covalent interactions with xanthan gum.

Rational regulation of pH and xanthan gum (XG) concentration has the potential to modulate interactions among macromolecules and enhance 3D printability. This study investigated non-covalent interactions between XG and other components within compound proteins emulsion gel systems across varying pH values (4.0-8.0) and XG concentrations (0-1 wt%) and systematically explored impacts of gelation properties and structural features on 3D printability. The results of rheological and structural features indicated that pH-regulated non-covalent interactions were crucial for maintaining structural stability of emulsion gels with the addition of XG. The 3D printability of emulsion gels would be significantly improved through moderate depletion flocculation produced when XG concentration was 0.75 wt% at the pH 6.0. Mechanical properties like viscosity exhibited a strongly negative correlation with 3D printability, whereas structural stability showed a significantly positive correlation. Overall, this study provided theoretical insights for the development of emulsion gels for 3D printing by regulating non-covalent interactions.

Effect of exogenous selenium on physicochemical, structural, functional, thermal, and gel rheological properties of mung bean (Vigna radiate L.) protein.

Selenium (Se) biofortification during the growth process of mung bean is an effective method to improve the Se content and quality. However, the effect of Se biofortification on the physicochemical properties of mung bean protein is unclear. The objective of this study was to clarify the changes in the composition, Se forms, particle structure, functional properties, thermal stability, and gel properties of mung bean protein at four Se application levels. The results showed that the Se content of mung bean protein increased in a dose-dependent manner, with 7.96-fold (P1) and 8.52-fold (P2) enhancement at the highest concentration. Exogenous Se application promotes the conversion of inorganic Se to organic Se. Among them, selenomethionine (SeMet) and methyl selenocysteine (MeSeCys) replaced Met and Cys through the S metabolic pathway and became the dominant organic Se forms in Se-enriched mung bean protein, accounting for more than 80 % of the total Se content. Exogenous Se at 30 g/hm2 significantly up-regulated protein content and promoted the synthesis of sulfur-containing protein components and hydrophobic amino acids in the presence of increased levels of SeMet and MeSeCys. Meanwhile, Cys and Met substitution altered the sulfhydryl groups (SH), ß-sheets, and ß-turns of protein. The particle size and microstructural characteristics depend on the protein itself and were not affected by exogenous Se. The Se-induced increase in the content of hydrophobic amino acids and ß-sheets synergistically increases the thermal stability of the protein. Moderate Se application altered the functional properties of mung bean protein, which was mainly reflected in the significant increase in oil holding capacity (OHC) and foaming capacity (FC). In addition, the increase in SH and ß-sheets induced by exogenous Se could alter the protein intermolecular network, contributing to the increase in storage modulus (G') and loss modulus (G″), which resulted in the formation of more highly elastic gels. This study further promotes the application of mung bean protein in the field of food processing and provides a theoretical basis for the extensive development of Se-enriched mung bean protein.

Hawthorn (Crataegus pinnatifida) berries ripeness induced pectin diversity: A comparative study in physicochemical properties, structure, function and fresh-keeping potential.

The effect of hawthorn berries ripeness on the physicochemical, structural and functional properties of hawthorn pectin (HP) and its potential in sweet cherry preservation were investigated. With the advanced ripeness of hawthorn berries, the galacturonic acid (GalA) content decreased from 59.70 mol% to 52.16 mol%, the molecular weight (Mw) reduced from 368.6 kDa to 284.3 kDa, the microstructure exhibited variable appearance from thick lamella towards porous cross-linked fragment, emulsifying activity and emulsions stability, antioxidant activities, α-amylase and pancreatic lipid inhibitory capacities significantly increased. The heated emulsion stored for 30 d presented higher creaming index and more ordered oil droplets compared to the unheated emulsion. With the extended berries ripeness, the firmness of HP gels remarkably decreased from 225.69 g to 73.39 g, while the springiness increased from 0.78 to 1.16, HP exhibited a superior inhibitory effect in water loss, browning, softening, and bacterial infection in sweet cherries preservation.

Comprehensive investigation into the effects of yeast dietary fiber and temperature on konjac glucomannan/kappa-carrageenan for the development of fat analogs.

In this study, yeast dietary fiber (YDF) was incorporated into konjac glucomannan/kappa-carrageenan (KGM/κ-KC) for the development of fat analogs, and the impact of YDF on the gelation properties and behavior of KGM/κ-KC composite gels was assessed. YDF improved the composite gel whiteness value, and affected the mechanical properties of the composite gel, especially enhancing its hardness, and decreasing its chewiness, elasticity, and gel strength, making it more similar to porcine back fat. When the yeast dietary fiber content was 0.033 g/mL and the heating temperature was 80 °C (T80-2), the textural properties of the composite gel were closest to porcine back fat. The frequency sweep results suggested that YDF incorporation led to enhancement of the intermolecular interaction and intermixing and interaction among more easily at higher processing temperatures (80 °C and 90 °C). By scanning electron microscopy, the fatty surface of porcine back fat was flat and covered with a large amount of oil, while KGM/κ-KC/YDF composite gels developed a dense, stacked network structure. YDF caused more fragmented, folded, and uneven structures to emerge. Overall, YDF could influence the gel behavior of KGM/κ-KC composite gels, and change their colors and mechanical properties. This work could serve as a guide for preparing fat analogs with KGM/κ-KC composite gels.

Effect of Thermal Treatment on Gelling and Emulsifying Properties of Soy ß-Conglycinin and Glycinin.

This study investigated the impact of different preheat treatments on the emulsifying and gel textural properties of soy protein with varying 11S/7S ratios. A mixture of 7S and 11S globulins, obtained from defatted soybean meal, was prepared at different ratios. The mixed proteins were subjected to preheating (75 °C, 85 °C, and 95 °C for 5 min) or non-preheating, followed by spray drying or non-spray drying. The solubility of protein mixtures rich in the 7S fraction tended to decrease significantly after heating at 85 °C, while protein mixtures rich in the 11S fraction showed a significant decrease after heating at 95 °C. Surprisingly, the emulsion stability index (ESI) of protein mixtures rich in the 7S fraction significantly improved twofold during processing at 75 °C. This study revealed a negative correlation between the emulsifying ability of soy protein and the 11S/7S ratio. For protein mixtures rich in either the 7S or the 11S fractions, gelling proprieties as well as emulsion activity index (EAI) and ESI showed no significant changes after spray drying; however, surface hydrophobicity was significantly enhanced following heating at 85 °C post-spray drying treatment. These findings provide insights into the alterations in gelling and emulsifying properties during various heating processes, offering great potential for producing soy protein ingredients with enhanced emulsifying ability and gelling property. They also contribute to establishing a theoretical basis for the standardized production of soy protein isolate with specific functional characteristics.

Insight into the effects of ultrasound-assisted intermittent tumbling on the gelation properties of myofibrillar proteins: Conformational modifications, intermolecular interactions, rheological properties and microstructure.

The aim of the present study was to evaluate the effects of ultrasound-assisted intermittent tumbling (UT) at 300 W, 20 kHz and 40 min on the conformation, intermolecular interactions and aggregation of myofibrillar proteins (MPs) and its induced gelation properties at various tumbling times (4 and 6 h). Raman results showed that all tumbling treatments led the helical structure of MPs to unfold. In comparison to the single intermittent tumbling treatment (ST), UT treatment exerted more pronounced effects on strengthening the intermolecular hydrogen bonds and facilitating the formation of an ordered ß-sheet structure. When the tumbling time was the same, UT treatment caused higher surface hydrophobicity, fluorescence intensity and disulfide bond content in the MPs, inducing the occurrence of hydrophobic interaction and disulfide cross-linking between MPs molecules, thus forming the MPs aggregates. Additionally, results from the solubility, particle size, atomic force microscopy and SDS-PAGE further indicated that, relative to the ST treatment, UT treatment was more potent in promoting the polymerization of myosin heavy chain. The MPs aggregates in the UT group were more uniform than those in the ST group. During the gelation process, the pre-formed MPs aggregates in the UT treatment increased the thermal stability of myosin, rendering it more resistant to heat-induced unfolding of the myosin rod region. Furthermore, they improved the protein tail-tail interaction, resulting in the formation of a well-structured gel network with higher gel strength and cooking yield compared to the ST treatment.

Effect of pH-shifting on the water holding capacity and gelation properties of mung bean protein isolate.

In this study, alkaline pH-shifting modified the globular structure of mung bean protein isolate (MBPI) to form flexible and stretched structures. In contrast, acidic pH-shifting increased the rigidity of MBPI. The increased flexibility (at the level of the secondary structure) and newly exposed intermolecular amino acid groups induced by alkaline pH-shifting improved the water holding capacity and gelation properties of proteins. Specifically, MBPI treated at pH 12 (MP12) showed the most flexible structure and highest water holding capacity and gel formation properties (least gelation concentration). The water-holding capacity of native MBPI increased from 1.56 g/g to 4.81 g/g, and its least gelation concentration decreased from 22 % to 15 % by pH-shifting at pH 12. Furthermore, MP12 formed stronger and more elastic heat-induced gels than native MBPI. We identified significant differences in the structural properties and water holding capacity, and gelation properties of acidic and alkaline pH-shifted MBPI and investigated the gelation properties of MP12 including rheological and morphological analyses. Our findings can facilitate the use of mung beans as a protein source in a wide range of food applications, including plant-based and processed meats.

Quality Control Assessment of Human Adipose-Derived Hydrogels.

Decellularized human-adipose tissue (hDAT) can serve as an alternative to two-dimensional monolayer culture and current ECM hydrogels due to its unlimited availability and cytocompatibility. A major hurdle in the clinical translation and integration of hDAT and other hydrogels into current in vitro culture processes is adherence to current good manufacturing practices (cGMP). Transferring of innovative technologies, including hydrogels, requires the establishing standardized protocols for quality assurance and quality control (QA/QC) of the material.Integration of basic characterization techniques, including physiochemical characterization, structural/morphological characterization, thermal and mechanical characterization, and biological characterization, in addition to the reduction of batch-to-batch variability and establishment of proper sterilization, storage, and fabrication processes verifies the integrity of the hydrogel. Obatala Sciences has established a characterization protocol that involves a series of assays including the evaluation of gelation properties, protein content, glycosaminoglycan content, soluble collagen content, and DNA content of hDAT.

Ultrasonic treatment combined with curdlan improves the gelation properties of low-salt Nemipterus virgatus surimi.

In this study, the gel properties of ultrasonic alone, curdlan treatment alone, and the combination of both at low-salt surimi levels were investigated, mainly in terms of textural properties, water holding capacity, water distribution, dynamic rheology, protein secondary structure, microstructure and correlation analysis. The results showed that the springiness, gel strength, water holding capacity and energy storage modulus (G') of the low-salt surimi gels without ultrasonic or curdlan treatment were lower than those of the high-salt concentration surimi gels. Compared with the 1 % low-salt group, the ultrasonic treatment combination with curdlan resulted in a significant improvement (p < 0.05) in the texture, water holding capacity and energy storage modulus (G') of the low-salt surimi at the same salt concentration. The gel strength increased significantly from 3386.360 g·mm to 5457.203 g·mm, but there was no significant improvement in whiteness (p > 0.05). In addition, ultrasonic treatment combined with curdlan promoted the shift of the α-helix to the random coil and the ß-turn angle shift, thus exposing the internal groups, enhancing protein intermolecular interactions, and promoting the orderly aggregation of proteins, resulting in a microstructure of dense, and obtained the lowest porosity of 14.534 %. The present study might be necessary for promoting the high-value use of aquatic surimi products and the development of low-salt foods.

Synergistic effects of oat ß-glucan combined with ultrasound treatment on gel properties of silver carp surimi.

The effect of oat ß-glucan (OG) combined with ultrasound treatment on the gelation properties of silver carp surimi with different salt contents was investigated. The results demonstrated that the gelation properties of surimi gels at high salt concentration were superior than those at low salt level. The addition of OG or ultrasound treatment could significantly enhance the texture properties, gel strength and water holding capacity (WHC) of gel samples, regardless of salt contents. The ultrasound treatment improved the whiteness of surimi gels, whereas the OG addition slightly declined the whiteness. Both OG addition and ultrasound treatment markedly reduced the total sulfhydryl content (total SH) and strengthened the hydrophobic interactions, forming the more uniform and denser gel network structures, hence more water was captured in network structures and became immobilized. Moreover, the combined treatment of OG and ultrasound showed synergic action on the gelation properties of surimi, and the gel strength and WHC of low-salt surimi gel treated by the combination of OG and ultrasound were even superior than that of high-salt gel without OG by traditional heating.

Terminal temperature dominates the gel quality of chicken meat paste: An emphasis on multiple heating-cooling regimes.

A survey of various heating strategies, including terminal temperature (70 and 90 °C), step heating (with or without holding at 50 °C for 10 min) and step cooling (with or without holding at 50 °C for 10 min), on the gelation properties of chicken meat paste was conducted. Compared to 70 °C, 90 °C heating drastically increased (p < 0.05) cooking loss (CL) from 5% to > 15% since more immobilized water was pushed out as free water. Step cooling could mitigate the high-temperature-induced CL. The impact of heating strategies on the textural properties of chicken meat is much lower than that on CL. For both 70 °C and 90 °C cooked samples, step heating reduced (p < 0.05) their whiteness by increasing the yellowness. The storage modulus (G') increase during cooling is mainly driven by cooling leaded lower mobility. Overall, low-temperature ramping heating produced excellent meat gel with low energy consumption.

Mechanism on the Synergistic Gelation of the Myofibrillar Protein Composite Gel Enhanced by "Clean-Label" Skin Functional Protein Powders.

The concept of healthiness and sustainability has promoted the innovation and development of "clean-label" products. Herein, this study aims to explore the influence mechanism of "clean label" skin protein powder (FPP) on the gelation properties of myofibrillar proteins (MPs). Specifically, the addition of FPP (0.2-4.0%) can improve the water holding capability and texture properties of MP composite gels. When the FPP concentration is over 1.0%, the composite gels exhibit no significant water loss during centrifugation. Dynamic rheology and sodium-dodecyl sulfate-polyacrylamide gel electrophoresis results revealed that FPP can slow the aggregation and denaturation of myosin and promote the formation of disulfide bonds between myofibril proteins, thus forming a stable network structure. Structural observation revealed that FPP can fill into the MP gel and lead to the formation of compact gel structures. Besides, with the increase of FPP concentration, the chemical forces involved in structural stabilization change significantly. Specifically, hydrophobic interaction and hydrogen bonding are the dominant forces at a lower FPP concentration (0.2 and 0.4%), while the ionic bond and disulfide bond are the dominant forces at a higher concentration. Overall, this work demonstrated that FPP can significantly improve the gel functionality of MP by altering the gel structure and strengthening the molecular forces.

Comparative investigation of various modification methods on Trachypenaeus Curvirostris surimi gel: Gelling properties, rheological behaviors and structure characteristics.

The aim of this study was to compare the investigations of various contents of egg white protein (2.0%-8.0%, EWP), microbial transglutaminase (0.1%-0.4%, MTGase), and konjac glucomannan (0.5%-2.0%, KGM) on the gelling properties and rheological behavior of Trachypenaeus Curvirostris shrimp surimi gel (SSG), and assessed the modification mechanisms through the analysis of structure characteristics. The findings suggested that all modified SSG samples (expect SSG-KGM2.0% ) had the higher gelling properties and the denser network structure than those of unmodified SSG. Meanwhile, EWP could give SSG a better appearance than MTGase and KGM. Rheological results showed that SSG-EWP6% and SSG-KGM1.0% had the highest G' and G″, demonstrating that the formation of higher levels of elasticity and hardness. All modifications could increase gelation rates of SSG along with the reduction of G″ during the degeneration of protein. According to the FTIR results, three modification methods changed SSG protein conformation with the increasing α-helix and ß-sheet contents and the decreasing of random coil content. LF-NMR results indicated that more free water could be transformed into immobilized water in the modified SSG gels, which contributed to improve the gelling properties. Furthermore, molecular forces showed that EWP and KGM could further increase the hydrogen bonds and hydrophobic interaction in SSG gels, while MTGase could induce the formation of more disulfide bonds. Thus, compared with another two modifications, EWP modified SSG gels showed the highest gelling properties.