Soybean 11S Globulin Research Articles

Soybean 11S globulin spray boosts chilled shrimp shelf-life, physicochemical, and sensory attributes beyond twelve days

Soybean 11S globulin spray boosts chilled shrimp shelf-life, physicochemical, and sensory attributes beyond twelve days

Interaction between rice protein and soybean 11S globulin: Effect on the characteristics of rice dough

Exogenous soy protein serves as an enhancer for gluten-free (GF) dough. However, the role of its primary component, soy 11S globulin (11S), and the impact of interactions between exogenous and endogenous proteins on dough remain ambiguous. In this study, the interaction between 11S and rice protein in rice dough was confirmed through the detection of interaction forces and other analytical techniques. Furthermore, the influence on enhancing the quality of rice dough was assessed using additional methodologies. When the content of 11S was 12%, the hydrophobic interaction, hydrogen bond and disulfide bond between 11S and rice protein were increased by 4.85, 3.58 and 6.36 fold, compared with the control group, respectively. Consequently, there was a 55% increase in α-helix content, indicating enhanced stability of the secondary structure. The microscope images showed that the interaction facilitated the development of a network structure within the mixed dough, resulting in increased resistance to kneading, decreased hardness, and heightened springiness. These effects were further reflected in the Mixolab results, the prolonged dough formation time, stable time, and tendency for the C2 value to rise, alongside a diminishing trend in tan δ value. This study confirmed this interaction, which provides the theoretical basis for its future application in GF Foods.

MiRNA Expression Analysis of IPEC-J2 Cells Damaged by Soybean 7S Globulin Reveals ssc-miR-221-5p as the Factor Alleviating Cell Damage.

The most significant and sensitive antigen protein that causes diarrhea in weaned pigs is soybean 7S globulin. Therefore, identifying the primary target for minimizing intestinal damage brought on by soybean 7S globulin is crucial. MicroRNA (miRNA) is closely related to intestinal epithelium's homeostasis and integrity. However, the change of miRNAs' expression and the function of miRNAs in Soybean 7S globulin injured-IPEC-J2 cells are still unclear. In this study, the miRNAs' expression profile in soybean 7S globulin-treated IPEC-J2 cells was investigated. Fifteen miRNAs were expressed differently. The differentially expressed miRNA target genes are mainly concentrated in signal release, cell connectivity, transcriptional inhibition, and Hedgehog signaling pathway. Notably, we noticed that the most significantly decreased miRNA was ssc-miR-221-5p after soybean 7S globulin treatment. Therefore, we conducted a preliminary study on the mechanisms of ssc-miR-221-5p in soybean 7S globulin-injured IPEC-J2 cells. Our research indicated that ssc-miR-221-5p may inhibit ROS production to alleviate soybean 7S globulin-induced apoptosis and inflammation in IPEC-J2 cells, thus protecting the cellular mechanical barrier, increasing cell proliferation, and improving cell viability. This study provides a theoretical basis for the prevention and control of diarrhea of weaned piglets.

Characterization of structural and functional properties of soybean 11S globulin during renaturation after denaturation induced by changes in pH.

This study explored the denaturation of 11S globulin, a protein known for its diverse functional properties in soy protein applications, at pH 3.0 and pH 10.0, followed by a gradual return to pH 7.0 to facilitate renaturation. It investigated the structural and functional changes during renaturation induced by a change in pH, revealing the stabilization mechanism of 11S globulin. The findings revealed that during pH adjustment to neutral, the denatured soybean 11S globulin - resulting from alkaline (pH 10.0) or acidic (pH 3.0) treatments - experienced a refolding of its extended tertiary structure to varying extents. The particle size and the proportions of α-helix and β-sheet in the secondary structure aligned progressively with those of the natural-state protein. However, for the alkali-denatured 11S, the β-sheet content decreased upon adjustment to neutral, whereas an increase was observed for the acid-denatured 11S. In terms of functional properties, after alkaline denaturation, the foaming capacity (FC) and emulsifying activity index (EAI) of 11S increased by 1.4 and 1.2 times, respectively, in comparison with its native state. The solubility, foamability, and emulsifiability of the alkali-denatured 11S gradually diminished during renaturation but remained superior to those of the native state. Conversely, these properties showed an initial decline, followed by an increase during renaturation triggered by pH neutralization. This research contributes to the enhancement of protein functionality, offering a theoretical foundation for the development of functional soy protein products and expanding their potential applications. © 2024 Society of Chemical Industry.

IAVPGEVA: Orally Available DPP4-Targeting Soy Glycinin Derived Octapeptide with Therapeutic Potential in Nonalcoholic Steatohepatitis.

IAVPGEVA, an octapeptide derived from soybean 11S globulin hydrolysis, also known as SGP8, has exhibited regulatory effects on lipid metabolism, inflammation, and fibrosis in vitro. Studies using MCD and HFD-induced nonalcoholic steatohepatitis (NASH) models in mice show that SGP8 attenuates hepatic injury and metabolic disorders. Mechanistic studies suggest that SGP8 inhibits the JNK-c-Jun pathway in L02 cells and liver tissue under metabolic stress and targets DPP4 with DPP4 inhibitory activity. In conclusion, the results suggest that SGP8 is an orally available DPP4-targeting peptide with therapeutic potential in NASH.

Electron beam irradiation induced aggregation, structural and functional changes of soybean 11S globulin

This study investigated the effects of different irradiation doses of an electron beam (e-beam) (0, 2, 4, 6, 8, and 10 kGy) on the structure, emulsification, foaming, and rheological and gel properties of soybean 11S globulin. The irradiation treatment at 4 and 6 kGy significantly increased the solubility, surface hydrophobicity, disulfide bonding, and ζ-potential of 11S globulin, decreased the particle size of the protein solution, and effectively improved the emulsifying activity and foaming stability of the protein solution. Moreover, irradiation induced moderate cross-linking and aggregation of the proteins, thereby increasing the apparent viscosity and shear stress of the protein solution. In addition, the low-field NMR and microstructure analysis results revealed that protein gels formed a dense and homogeneous three-dimensional mesh structure after irradiation (6 kGy), along with increased content of bound water (T2b) and water not readily flowable (T21) and a decrease content of free water (T22). Overall, our results confirmed that e-beam irradiation could significantly improve the physicochemical properties of soybean 11S globulin. Our study thus provides a new technical means for the application of electron beam irradiation technology toward protein modification and broadens the high-value utilization of soybean 11S globulin in the food processing industry.

Revealing the mechanism of the lutein protective function of epicatechin-fructan glycosylated soybean protein isolate

Lutein possesses various physiological activities but is susceptible to light degradation, thermal degradation, and oxidative degradation. As such, protecting the activity of lutein-based products using natural extracts has become a current research. In this study, lutein was protected by complexing inulin-type fructan (ITF), soybean protein isolate (SPI), and epicatechin (EC), and the protection mechanism of epicatechin-fructan glycosylated soybean protein isolate (EC-GSPI) toward lutein was elucidated comprehensively. The results showed that the addition of EC delayed the degradation of lutein. The results of light stability experiments showed that increased EC significantly enhanced the storage time of the GSPI-Lutein system from 4 to 13 days. Additionally, the effect of EC on glycosylated soybean 7S globulin (G7S) and glycosylated soybean 11S globulin (G11S) was assessed. The light stability of G11S-Lutein and G7S-Lutein after the addition of EC was from G11S > G7S → G7S > G11S. Furthermore, the proteins purified from SPI interacted differently with EC and ITF, with soybean 7S globulin (7S) mainly interacting with EC and soybean 11S globulin (11S) mainly interacting with ITF. EC-GSPI-Lutein exhibited a good protective effect, probably due to the occurrence of hygrothermal Maillard between ITF and 11S, providing a porous structure for lutein storage. At the same time, the binding of EC to 7S significantly enhanced the antioxidant property of the solution and the stability of the protein secondary structure, thereby prolonging the storage time of lutein.

Exploring the Interactions of Soybean 7S Globulin with Gallic Acid, Chlorogenic Acid and (-)-Epigallocatechin Gallate.

In this study, the noncovalent interaction mechanisms between soybean 7S globulin and three polyphenols (gallic acid (GA), chlorogenic acid (CA) and (-)-epigallocatechin gallate (EGCG)) were explored and compared using various techniques. Fluorescence experiments showed that GA and EGCG had strong static quenching effects on 7S fluorescence, and that of CA was the result of multiple mechanisms. The interactions caused changes to the secondary and tertiary structure of 7S, and the surface hydrophobicity was decreased. Thermodynamic experiments showed that the combinations of polyphenols with 7S were exothermic processes. Hydrogen bonds and van der Waals forces were the primary driving forces promoting the binding of EGCG and CA to 7S. The combination of GA was mainly affected by electrostatic interaction. The results showed that the structure and molecular weight of polyphenols play an important role in their interactions. This work is helpful for developing products containing polyphenols and soybean protein.

Effects of electric field intensity regulation on protein aggregation behaviour and foaming property of soybean 7S globulin

In this study, the aggregation behaviour of soybean 7S globulin after moderate electric field (MEF) treatment was investigated, and the influence of the electric field and temperature field on the structure and foaming property of the aggregates were analysed and compared with conventional water bath (COV). The results showed that MEF treatment enhanced the properties of the aggregates. The properties of the treated aggregates were significantly better than those of native 7S globulin. At an electric field strength of 8 V/cm, the solubility, turbidity, and particle size increased from 95.81 % to 99.37 %, 0.097 to 0.189 and 61.97 nm to 113.21 nm, respectively, and the absolute value of potential decreased from 23.56 mV to 22.12 mV. The SDS-PAGE and size exclusion chromatography (SEC) results showed that the electric field had a positive effect on the aggregate formation of the Fourier-transform infrared spectroscopy (FTIR), fluorescence spectroscopy, surface hydrophobicity (H0) and total sulfhydryl (SHT) results indicated that the spatial structure of the protein was changed by MEF treatment. The protein β-sheet content was reduced, and the Try that was originally buried inside the molecule was exposed, resulting in an increase in H0 and a decrease in SHT. The foaming property of the 7S globulin aggregates was improved by MEF treatment.

Extension Region Domain of Soybean 7S Globulin Contributes to Serum Triglyceride-Lowering Effect via Modulation of Bile Acids Homeostasis.

Soybean 7S globulin (β-conglycinin), a major soybean storage protein, has been demonstrated to exert remarkable triglyceride (TG) and cholesterol-lowering effects, yet the underlying mechanism remains controversial. A comparative investigation is performed to assess the contribution of different structural domains of soybean 7S globulin, including core region (CR) and extension region (ER) domains, to biological effects of soybean 7S globulin using a high-fat diet rat model. The results show that ER domain mainly contributes to the serum TG-lowering effect of soybean 7S globulin, but not for CR domain. Metabolomics analysis reveals that oral administration of ER peptides obviously influences the metabolic profiling of serum bile acids (BAs), as well as significantly increased the fecal excretion of total BAs. Meanwhile, ER peptides supplementation reshapes the composition of gut microbiota and impacts the gut microbiota-dependent biotransformation of BAs which indicate by a significantly increased secondary BAs concentration in fecal samples. These results highlight that TG-lowering effects of ER peptides mainly stem from their modulation of BAs homeostasis. Oral administration of ER peptides can effectively lower serum TG level by regulating BAs metabolism. ER peptides have potential to be used as a candidate pharmaceutical for the intervention of dyslipidemia.

Covalent polyphenol with soybean 11S protein to develop hypoallergenic conjugates for potential immunotherapy

Soybean 11S globulin is one of the most important allergens in soybean. This study investigated the effects of 11S covalent that conjugated covalently with (−)-Epigallo-catechin 3-gallate (EGCG) and chlorogenic acid (CHA) on protein structure, digestibility, and allergenicity. 11S conjugation with EGCG and CHA yielded covalent conjugates and formed cross-linked protein polymers, which changed the structures and increased the digestibility of the protein. In vitro experiments showed that the ability of IgE binding, and stimulation mast cell degranulation were lower for11S-EGCG and 11S-CHA conjugates compared to 11S. In vivo experiments showed that conjugation of EGCG and CHA reduced the allergenicity of 11S. The oral tolerance model showed that hypoallergenic 11S-EGCG conjugates successfully relieved allergic symptoms and induced oral tolerance by affecting antigen presentation, activating Treg cells to produce IL-10, and promoting Th1/Th2 immune balance. This study presented an innovative strategy to develop hypoallergenic food production that induce tolerance for allergen-specific immunotherapy.

Emulsifying properties of glucose-conjugated soybean 11S globulin with maximum antioxidant capacity, obtained under optimal preparatory conditions identified by random-centroid optimization

Emulsifying properties of glucose-conjugated soybean 11S globulin with maximum antioxidant capacity, obtained under optimal preparatory conditions identified by random-centroid optimization

The interaction of trehalose and molten globule state soybean 11S globulin and its impact on foaming capacities.

Soybean 11S globulin has good functional properties, which are widely used in the field of food. However, natural soybean 11S globulin (N-11S) has low flexibility and is easy to aggregate, impacting its foaming process. Studies have shown that soybean 11S globulin in molten globule state (MG-11S) has better molecular flexibility than N-11S, and trehalose has been shown to improve the properties of proteins. Therefore, this study investigated the interaction mechanism between trehalose and MG-11S, and its impact on rheological and foaming properties of MG-11S. The molecular docking and intrinsic fluorescence results showed that hydrogen bonding was the main interaction force at lower than 0.5mol L-1 trehalose added. Meanwhile, rheology and foaming showed that the MG-11S-trehalose complexes had better viscoelasticity, foaming ability (66.67-86.67%) and foaming stability (75.00-89.29%) than N-11S (16.67% foaming ability and 40.00% foaming stability); however, when the trehalose was higher than 0.5mol L-1 , molecular crowding occurred and H-bonds were weakened, resulting in reduction of foaming capacities. Microstructure determination showed that trehalose attached to the surface of foam membrane; meanwhile, the foaming structure of the complex with 0.5mol L-1 trehalose had a thicker liquid film with decreased drainage rate, less agglomeration and disproportionation of foam, illustrating the best foaming ability and foaming stability. The results suggested that trehalose at different concentrations can interact with MG-11S through different mechanisms, and improve the foaming capacity of MS-11S. This provided a reference for the application of MS-11S in foaming food. © 2022 Society of Chemical Industry.

Characterization of structural and functional properties of soybean 11S globulin during the renaturation after the guanidine hydrochloride denaturation

In this study, we explored how 11S globulin undergoes the renaturation with the decrease of guanidine hydrochloride (GuHCl) concentration. To analyze the changes in the structural and functional properties of 11S globulin, circular dichroism spectroscopy (CD), intrinsic fluorescence, particle size, foaming capacity (FC), foam stability (FS), emulsifying activity index (EAI) and emulsion stability index (ESI) at different GuHCl concentrations (8.0 mol/L, 4.0 mol/L, 2.0 mol/L, 0.8 mol/L, and 0.4 mol/L) were performed. 11S globulin was completely denatured after being treated with 8.0 mol/L of GuHCl. The CD spectra and particle size analyses showed that the α-helix and β-sheet contents and particle size of the renaturation process for 11S globulin were gradually close to those of native state protein and the protein structure became more orderly. The α-helix content increased from 0.2 ± 0.1% to 7.8 ± 0.3% and the hydrophobic groups inside the 11S globulin were exposed, which increased the surface hydrophobicity of the 11S globulin and changed its conformation. Regarding the functional properties, when the GuHCl concentration was diluted to 2.0 mol/L, some functional properties were improved compared with those of native state protein. The FC and FS of 11S globulin were increased by 5 and 2.2 times respectively and the EAI and ESI were increased by 1.25 times respectively. This study will provide guidance for the control of renaturation degree during 11S globulin production process to improve functional properties.

Functional alteration of soybean 11S globulin through glycation

Functional alteration of soybean 11S globulin through glycation

Predicting the allergenicity of legume proteins using a PBMC gene expression assay

BackgroundFood proteins differ in their allergenic potential. Currently, there is no predictive and validated bio-assay to evaluate the allergenicity of novel food proteins. The objective of this study was to investigate the potential of a human peripheral blood mononuclear cell (PBMC) gene expression assay to identify biomarkers to predict the allergenicity of legume proteins.ResultsPBMCs from healthy donors were exposed to weakly and strongly allergenic legume proteins (2S albumins, and 7S and 11S globulins from white bean, soybean, peanut, pea and lupine) in three experiments. Possible biomarkers for allergenicity were investigated by exposing PBMCs to a protein pair of weakly (white bean) and strongly allergenic (soybean) 7S globulins in a pilot experiment. Gene expression was measured by RNA-sequencing and differentially expressed genes were selected as biomarkers. 153 genes were identified as having significantly different expression levels to the 7S globulin of white bean compared to soybean. Inclusion of multiple protein pairs from 2S albumins (lupine and peanut) and 7S globulins (white bean and soybean) in a larger study, led to the selection of CCL2, CCL7, and RASD2 as biomarkers to distinguish weakly from strongly allergenic proteins. The relevance of these three biomarkers was confirmed by qPCR when PBMCs were exposed to a larger panel of weakly and strongly allergenic legume proteins (2S albumins, and 7S and 11S globulins from white bean, soybean, peanut, pea and lupine).ConclusionsThe PBMC gene expression assay can potentially distinguish weakly from strongly allergenic legume proteins within a protein family, though it will be challenging to develop a generic method for all protein families from plant and animal sources. Graded responses within a protein family might be of more value in allergenicity prediction instead of a yes or no classification.

The effect of trehalose on the thermodynamic stability and emulsification of soybean 11S globulin in the molten globule state

The molten globule (MG) state of soybean glycinin (11S) is partially folded at pH 1.0, so various polyhydroxyl osmotic agents are often used to maintain the structural stability of the MG state under acidic conditions. In this study trehalose was used as a penetrant, and intrinsic fluorescence spectroscopy and circular dichroism were performed to investigate the effects of a gradient concentration of trehalose on the structure of soybean 11S. The MG soybean 11S maintained a more α-helix structure (94.7%) and a larger hydrophobic area when treated with a high concentration of trehalose (1.3 mol/L) than when untreated, and retained a typical compact MG structure despite the lack of tertiary structural elements. A linear extrapolation model showed that the Gibbs free energy of the high-concentration trehalose-induced compact MG state of soybean 11S was reduced by 3 times, compared with the untreated globulin. This improvement of thermodynamic stability indicated that trehalose stabilized this structure by forming a stable trehalose–soybean 11S MG state system. With the addition of gradient trehalose, the surface tension of the solution was significantly reduced and the viscosity of the solution was increased. The emulsifying properties were optimized when the trehalose concentration was 0.5 mol/L, the emulsifying activity (EAI) and emulsifying stability (ESI) were 76.67 m2/g and 76.67%. The improvement of emulsifying property of 11S MG-trehalose system was further proved by observing the microstructure of emulsion by Cryo-SEM. This study advances the understanding of the 11S MG-trehalose system and provides a theoretical basis to produce proteins with excellent emulsifying properties.

Effects and interaction mechanism of soybean 7S and 11S globulins on anthocyanin stability and antioxidant activity during in vitro simulated digestion

The objective of this study was to investigate the effects of soybean 7S and 11S globulins on the stability and antioxidant capacity of cyanidin-3-O-glucoside (C3G) in the simulated gastrointestinal environment, and further to elucidate their interaction mechanism. The stability and total content of anthocyanins (ACNs) before and after simulated digestion were determined by Ultraviolet–visible (UV–Vis) spectroscopic and pH differential methods, respectively, and free radical scavenging activity of C3G after simulated digestion were measured using ABTS and DPPH assays. The interaction mechanism was further investigated using molecular docking and molecular dynamics simulation. The analysis results showed that soybean 7S and 11S globulins had a protective effect on the stability of C3G during simulated digestion and improved the antioxidant capacity of C3G after simulated digestion. Soybean 11S globulin had a better effect than soybean 7S globulin in protecting the stability and antioxidant capacity of C3G against simulated gastrointestinal environment. In silico results showed that the binding interactions between C3G and 7S and 11S globulins were mainly hydrogen bonds and van der Waals forces, followed by hydrophobic interactions. Among them, ASN69 and THR101 are the key amino acid residues for 7S–C3G binding, and THR82 and PRO86 are the key amino acid residues for 11S–C3G binding. The results suggested that it may be helpful to use soybean 7S and 11S globulins as carriers to improve the stability and antioxidant activity of ACNs.

Effect of reverse micelle on physicochemical properties of soybean 7S globulins

In this paper, the structural, thermodynamic, and rheological properties of soybean 7S globulins extracted by bis(2-ethylhexyl) sulfosuccinate sodium salt (AOT)/isooctane reverse micelle method and alkali extraction-acid precipitation method were studied. Amino acid composition results showed that the 7S globulin produced by reverse micelle had more hydrophobic and sulfur-containing amino acids. Fourier transform infrared spectroscopy results demonstrated that the 7S globulin extracted by reverse micelle had more β-sheets but less turn structure, and formed a more compact conformation. However, lower surface hydrophobicity was observed in the 7S globulin extracted by reverse micelle, indicating that the reverse micelle environment could protect the native folded structure of protein. Thermal stability tests showed that the 7S globulin extracted by reverse micelle had poorer thermostability with lower denaturation temperature, which was in accordance with the results of initial gelling temperature. Final storage modulus (G’) and frequency sweep results revealed that the 7S globulin obtained by reverse micelle produced a harder textured gel.

MTGase Mediated Polymerization of 11S Globulin to Enhance Its Functionalities and the Proteomics

In this paper, the effects of the induced polymerization and modification by microbial transglutaminase (MTGase) on solubility and emulsifiability of soybean 11S globulin was studied. The mechanism was also investigated through proteomics. Using SDS-PAGE and optical density scanning to testify MTGase enzymatic polymerization, the optimum conditions showed that: temperature was 45 °C, ionic condition I was 0.2, pH was 8.0, the amount of enzyme was 30 U/g. The molecular weight of modified 11S globulin subunits concentrated at 15 kDa. The solublity and emulsifiability were significantly enhanced. There were 268 differential protein spots extracted. Ten protein spots had significant differences in expression which totally focused on seed storage proteins, promoting seed germination and maturation proteins, proteins involved in osmotic regulation and alcohol dehydrogenase, which affect solubility and emulsifiability of 11S globulin.