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1.
Nat Plants ; 10(5): 736-742, 2024 May.
Article in English | MEDLINE | ID: mdl-38724696

ABSTRACT

Symbiotic nitrogen fixation in legume nodules requires substantial energy investment from host plants, and soybean (Glycine max (L.) supernodulation mutants show stunting and yield penalties due to overconsumption of carbon sources. We obtained soybean mutants differing in their nodulation ability, among which rhizobially induced cle1a/2a (ric1a/2a) has a moderate increase in nodule number, balanced carbon allocation, and enhanced carbon and nitrogen acquisition. In multi-year and multi-site field trials in China, two ric1a/2a lines had improved grain yield, protein content and sustained oil content, demonstrating that gene editing towards optimal nodulation improves soybean yield and quality.


Subject(s)
Glycine max , Plant Root Nodulation , Glycine max/genetics , Glycine max/metabolism , Glycine max/microbiology , Plant Root Nodulation/genetics , Root Nodules, Plant/metabolism , Root Nodules, Plant/genetics , Root Nodules, Plant/microbiology , Symbiosis , Nitrogen Fixation/genetics , Gene Editing , Mutation , Plant Proteins/metabolism , Plant Proteins/genetics , Soybean Proteins/genetics , Soybean Proteins/metabolism
2.
Food Res Int ; 183: 114224, 2024 May.
Article in English | MEDLINE | ID: mdl-38760143

ABSTRACT

During infant formula production, proteins are always heated, potentially affecting their digestibility and the bioactivities of resulting peptides. Although plant proteins are a promising dairy alternative for infant formula, they remain understudied, necessitating further investigations. Therefore, this research aimed to fill this gap by assessing the impact of different heating modes on soy protein (SP) and pea protein (PP), focusing on glycation levels, peptide formation during in vitro infant digestion, and immune protection potential (sRAGE-binding and antimicrobial activities) of the resulting peptides. Consequently, dry heating led to increased glycation and glycated peptide production, particularly with higher glycation in PP than SP. Moreover, PP exhibited an overall stronger sRAGE-binding capacity than SP, regardless of heating and digestion conditions. Regarding antimicrobial activity, both SP and PP-derived peptides displayed reduced effectiveness against Enterobacter cloacae after dry heating. Additionally, Staphylococcus epidermidis was differently inhibited, where PP-derived peptides showed inherent inhibition. The primary determinant of sRAGE-binding and antimicrobial potential in digestion-derived peptides was the protein source. Subsequent bioinformatics analysis predicted 519 and 133 potential antimicrobial peptides in SP and PP, respectively. This study emphasises the importance of protein source for infant formula to ensure infant health.


Subject(s)
Digestion , Hot Temperature , Infant Formula , Pea Proteins , Soybean Proteins , Soybean Proteins/metabolism , Humans , Infant Formula/chemistry , Infant , Pea Proteins/metabolism , Pea Proteins/chemistry , Receptor for Advanced Glycation End Products/metabolism , Antimicrobial Peptides/metabolism , Anti-Infective Agents/pharmacology
3.
J Agric Food Chem ; 72(20): 11694-11705, 2024 May 22.
Article in English | MEDLINE | ID: mdl-38723176

ABSTRACT

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.


Subject(s)
Apoptosis , Globulins , Glycine max , Intestinal Mucosa , MicroRNAs , Soybean Proteins , Animals , MicroRNAs/genetics , MicroRNAs/metabolism , Swine , Cell Line , Glycine max/genetics , Glycine max/chemistry , Glycine max/metabolism , Intestinal Mucosa/metabolism , Soybean Proteins/genetics , Soybean Proteins/metabolism , Globulins/genetics , Globulins/metabolism , Seed Storage Proteins/genetics , Epithelial Cells/metabolism , Cell Proliferation/drug effects , Cell Survival/drug effects , Antigens, Plant
4.
Food Chem ; 451: 139507, 2024 Sep 01.
Article in English | MEDLINE | ID: mdl-38696940

ABSTRACT

In the domain of infant nutrition, optimizing the absorption of crucial nutrients such as vitamin D3 (VD3) is paramount. This study harnessed dynamic-high-pressure microfluidization (DHPM) on soybean protein isolate (SPI) to engineer SPI-VD3 nanoparticles for fortifying yogurt. Characterized by notable binding affinity (Ka = 0.166 × 105 L·mol-1) at 80 MPa and significant surface hydrophobicity (H0 = 3494), these nanoparticles demonstrated promising attributes through molecular simulations. During simulated infant digestion, the 80 MPa DHPM-treated nanoparticles showcased an impressive 74.4% VD3 bioaccessibility, delineating the pivotal roles of hydrophobicity, bioaccessibility, and micellization dynamics. Noteworthy was their traversal through the gastrointestinal tract, illuminating bile salts' crucial function in facilitating VD3 re-encapsulation, thereby mitigating crystallization and augmenting absorption. Moreover, DHPM treatment imparted enhancements in nanoparticle integrity and hydrophobic properties, consequently amplifying VD3 bioavailability. This investigation underscores the potential of SPI-VD3 nanoparticles in bolstering VD3 absorption, thereby furnishing invaluable insights for tailored infant nutrition formulations.


Subject(s)
Biological Availability , Cholecalciferol , Digestion , Hydrophobic and Hydrophilic Interactions , Soybean Proteins , Soybean Proteins/chemistry , Soybean Proteins/metabolism , Humans , Cholecalciferol/chemistry , Cholecalciferol/metabolism , Infant , Models, Biological , Nanoparticles/chemistry , Nanoparticles/metabolism
5.
Int J Biol Macromol ; 266(Pt 2): 131308, 2024 May.
Article in English | MEDLINE | ID: mdl-38569996

ABSTRACT

In this work, the acylated anthocyanin (Ca-An) was prepared by enzymatic modification of black rice anthocyanin with caffeic acid, and the binding mechanism of Ca-An to soybean protein isolate (SPI) was investigated by experiments and computer simulation to expand the potential application of anthocyanin in food industry. Multi-spectroscopic studies revealed that the stable binding of Ca-An to SPI induced the folding of protein polypeptide chain, which transformed the secondary structure of SPI trended to be flexible. The microenvironment of protein was transformed from hydrophobic to hydrophilic, while tyrosine played dominant role in quenching process. The binding sites and forces of the complexes were determined by computer simulation for further explored. The protein conformation of the 7S and 11S binding regions to Ca-An changed, and the amino acid microenvironment shifted to hydrophilic after binding. The results showed that more non-polar amino acids existed in the binding sites, while in binding process van der Waals forces and hydrogen bonding played a major role hydrophobicity played a minor role. Based on MM-PBSA analysis, the binding constants of 7S-Ca-An and 11S-Ca-An were 0.518 × 106 mol-1 and 5.437 × 10-3 mol-1, respectively. This information provides theoretical guidance for further studying the interaction between modified anthocyanins and biomacromolecules.


Subject(s)
Anthocyanins , Hydrophobic and Hydrophilic Interactions , Molecular Dynamics Simulation , Protein Binding , Soybean Proteins , Anthocyanins/chemistry , Anthocyanins/metabolism , Soybean Proteins/chemistry , Soybean Proteins/metabolism , Binding Sites , Solubility , Hydrogen Bonding
6.
Food Chem ; 450: 139327, 2024 Aug 30.
Article in English | MEDLINE | ID: mdl-38636380

ABSTRACT

Branched-chain amino acids (BCAAs) are vital components of human and animal nutrition that contribute to the building blocks of proteins. In this study, 170 protease-producing strains were isolated and screened from soy-fermented foods. Bacillus amyloliquefaciens NY130 was obtained from Cheonggukjang with high production of BCAAs. Optimal production of protease from B. amyloliquefaciens NY130 (protease NY130) was achieved at 42 °C and pH 6.0 for 21 h. It was purified and determined as 27- and 40 kDa. Protease NY130 showed maximum activity at pH 9.0 and 45 °C with Km value of 10.95 mg for ISP and 1.69 mg for WPI. Protease-treated ISP and WPI showed increased sweetness and saltiness via electronic tongue analysis and enhanced the protective effect against oxidative stress in C2C12 myocytes by increasing p-mTOR/mTOR protein expression to 160%. This work possesses potential in producing BCAAs by using protease for utilization in food.


Subject(s)
Amino Acids, Branched-Chain , Bacillus amyloliquefaciens , Peptide Hydrolases , Soybean Proteins , Bacillus amyloliquefaciens/metabolism , Bacillus amyloliquefaciens/chemistry , Amino Acids, Branched-Chain/metabolism , Amino Acids, Branched-Chain/chemistry , Peptide Hydrolases/metabolism , Peptide Hydrolases/chemistry , Soybean Proteins/chemistry , Soybean Proteins/metabolism , Animals , Mice , Bacterial Proteins/metabolism , Bacterial Proteins/chemistry , Humans , Oxidative Stress/drug effects , Fermentation
7.
J Agric Food Chem ; 72(15): 8742-8748, 2024 Apr 17.
Article in English | MEDLINE | ID: mdl-38564658

ABSTRACT

Tyrosinase is capable of oxidizing tyrosine residues in proteins, leading to intermolecular protein cross-linking, which could modify the protein network of food and improve the texture of food. To obtain the recombinant tyrosinase with microbial cell factory instead of isolation tyrosinase from the mushroom Agaricus bisporus, a TYR expression cassette was constructed in this study. The expression cassette was electroporated into Trichoderma reesei Rut-C30 and integrated into its genome, resulting in a recombinant strain C30-TYR. After induction with microcrystalline cellulose for 7 days, recombinant tyrosinase could be successfully expressed and secreted by C30-TYR, corresponding to approximately 2.16 g/L tyrosinase in shake-flask cultures. The recombinant TYR was purified by ammonium sulfate precipitation and gel filtration, and the biological activity of purified TYR was 45.6 U/mL. The purified TYR could catalyze the cross-linking of glycinin, and the emulsion stability index of TYR-treated glycinin emulsion was increased by 30.6% compared with the untreated one. The cross-linking of soy glycinin by TYR resulted in altered properties of oil-in-water emulsions compared to emulsions stabilized by native glycinin. Therefore, cross-linking with this recombinant tyrosinase is a feasible approach to improve the properties of protein-stabilized emulsions and gels.


Subject(s)
Cross-Linking Reagents , Gene Expression , Globulins , Hypocreales , Monophenol Monooxygenase , Recombinant Proteins , Soybean Proteins , Monophenol Monooxygenase/biosynthesis , Monophenol Monooxygenase/genetics , Monophenol Monooxygenase/isolation & purification , Monophenol Monooxygenase/metabolism , Cross-Linking Reagents/isolation & purification , Cross-Linking Reagents/metabolism , Hypocreales/classification , Hypocreales/genetics , Hypocreales/growth & development , Hypocreales/metabolism , Globulins/chemistry , Globulins/metabolism , Soybean Proteins/chemistry , Soybean Proteins/metabolism , Electroporation , Cellulose , Ammonium Sulfate , Chromatography, Gel , Fractional Precipitation , Emulsions/chemistry , Emulsions/metabolism , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Protein Stability , Endoplasmic Reticulum/metabolism , Protein Sorting Signals , Oils/chemistry , Water/chemistry
8.
Article in English | MEDLINE | ID: mdl-38306950

ABSTRACT

The specific miRNA regulation triggered by enzyme-treated soybean protein in response to well-known stressors, such as the prophylactic use of the antimicrobial oxytetracycline, remains unknown. Hence, this study aimed to evaluate the regulatory changes of hepatic miRNAs induced by oxytetracycline and enzyme-treated soybean protein in largemouth bass dietary formulations. The experiment was designed with three groups: the normal control (NC), the oxytetracycline exposure treatment group (OTC), and the pre-treatment with enzyme-treated soybean protein before oxytetracycline exposure group (ETSP). miRNA sequencing was employed to characterize the differences between these groups. In conclusion, the NC group exhibited up-regulation of 13 host miRNAs and down-regulation of 1 miRNA compared to the OTC group, whereas the ETSP group showed an increasing trend of 36 host miRNAs and a decreasing trend of 13 host miRNAs compared to the OTC group. Nine miRNAs were identified as prudential targets for enzyme-treated soy protein, protecting the largemouth bass liver from oxytetracycline. Furthermore, gene ontology analysis revealed nine key miRNAs that mediate signaling pathways with significant differences. The cellular lipid metabolic process was identified as the most important biological process, and the propanoate metabolism pathway was highlighted as significant. These results will facilitate further exploration of the mechanism by which enzyme-treated soy protein alleviates the effects of oxytetracycline on largemouth bass in water environments.


Subject(s)
Bass , MicroRNAs , Oxytetracycline , Animals , Bass/genetics , Soybean Proteins/metabolism , Soybean Proteins/pharmacology , Oxytetracycline/pharmacology , Oxytetracycline/metabolism , Liver/metabolism , MicroRNAs/genetics
9.
J Sci Food Agric ; 104(7): 4363-4370, 2024 May.
Article in English | MEDLINE | ID: mdl-38299730

ABSTRACT

BACKGROUND: The two major storage proteins of soymilk are the globulins 7S and 11S. Freeze-thaw fractionation is a simple method for separating these proteins in raw soymilk. In this study, we assessed the freeze-thaw fractionation ability of raw soymilk under various pH (4.3-11.6) conditions and added salt (sodium chloride) concentrations (0.00-0.67 mol L-1). RESULTS: We successfully achieved fractionation within a pH range of 5.8-6.7 and when the salt concentration was 0.22 mol L-1 or lower. Analysis of particle size distribution and microscopic examination of soymilk revealed no direct correlation between particle size and freeze-thaw fractionation ability. Interestingly, it was confirmed that the ranges of zeta potential values associated with successful freeze-thaw fractionation in raw soymilk remained consistent across different pH and salt concentration conditions. These ranges were between -23 and -28 mV at pH levels ranging from 5.8 to 6.7 and between -18 and -29 mV at added salt concentrations ranging from 0 to 0.22 mol L-1. CONCLUSION: The pH and salt concentration in raw soymilk markedly influence the freeze-thaw fractionation process. We confirmed that the range of zeta potential values where fractionation was possible remained consistent under various pH and salt concentration conditions. These findings suggest that the zeta potential value might serve as an indicator for evaluating the freeze-thaw fractionation ability of raw soymilk. © 2024 Society of Chemical Industry.


Subject(s)
Globulins , Soy Milk , Soybean Proteins/metabolism , Sodium Chloride , Soy Milk/metabolism , Globulins/metabolism , Hydrogen-Ion Concentration
10.
Food Chem ; 443: 138523, 2024 Jun 15.
Article in English | MEDLINE | ID: mdl-38286093

ABSTRACT

Microbial fermentation emerges as a promising strategy to elevate the quality of soybean proteins in food industry. This study conducted a comprehensive assessment of the biotransformation of four types of soybean proteins by Bacillus subtilis BSNK-5, a proteinase-rich bacterium. BSNK-5 had good adaptability to each protein. Soluble protein, peptides and free amino acids increased in fermented soybean proteins (FSPs) and dominant after 48-84 h fermentation, enhancing nutritional value. Extensive proteolysis of BSNK-5 also improved antioxidant and antihypertensive activities, reaching peak level after 48 h fermentation. Furthermore, excessive proteolysis effectively enhanced the generation of beneficial spermidine without producing toxic histamine after fermentation, and formed the flavor profile with 56 volatiles in 48 h FSPs. Further degradation of amino acids showed a positive correlation with off-flavors, particularly the enrichment of 3-methylbutanoic acid. These findings establish a theoretical foundation for regulating moderate fermentation by BSNK-5 to enabling the high-value utilization of soybean protein.


Subject(s)
Bacillus subtilis , Soybean Proteins , Soybean Proteins/metabolism , Bacillus subtilis/metabolism , Glycine max , Amino Acids/metabolism , Antioxidants/metabolism , Fermentation
11.
Am J Physiol Endocrinol Metab ; 326(2): E124-E133, 2024 02 01.
Article in English | MEDLINE | ID: mdl-38088866

ABSTRACT

Soy protein has shown remarkable effectiveness in reducing fat mass compared with other protein sources, and exercise has the potential to further enhance this fat loss effect. Previous studies have demonstrated that soy protein intake leads to decreased fatty acid synthesis, which contributes to its fat-loss properties. However, the exact mechanism by which these lipids are consumed remains unclear. To investigate this, we conducted a comprehensive study using C57/BL6 male mice, comparing the effects of soy and casein proteins with and without exercise (Casein-Sed, Casein-Ex, Soy-Sed, and Soy-Ex groups) under high- and low-protein conditions (14% or 40% protein). Our findings revealed that combining soy protein intake with exercise significantly reduced epididymal white adipose tissue (eWAT) weight, particularly in the high-protein diet group. Further analysis revealed that exercise increased the expression of lipid oxidation-regulatory proteins, including mitochondrial oxidative phosphorylation protein (OXPHOS) complexes, in the plantaris muscle regardless of the protein source. Although soy protein intake did not directly affect muscle mitochondrial protein expression, the activity of OXPHOS complex I was additively enhanced by exercise and soy protein under the 40% protein condition. Notably, complex I activity inversely correlated with eWAT weight in the soy protein diet group. These results highlight the potential link between improved complex I activity induced by soy protein and fat mass reduction, which emphasizes the promising benefits of combining soy protein with exercise in promoting fat loss.NEW & NOTEWORTHY The findings revealed that soy protein intake combined with exercise resulted in reduced adipose tissue weight compared with that obtained with casein protein intake. Furthermore, the joint impact of exercise and soy protein consumption resulted in enhanced activity of oxidative phosphorylation protein (OXPHOS) complex I in fast-twitch muscles, which appears to be associated with fat mass reduction. These findings elucidate the potential additive effects of soy protein and exercise on body weight management.


Subject(s)
Caseins , Soybean Proteins , Male , Mice , Animals , Soybean Proteins/pharmacology , Soybean Proteins/metabolism , Caseins/metabolism , Caseins/pharmacology , Intra-Abdominal Fat , Diet , Muscle, Skeletal/metabolism , Eating/physiology
12.
Food Chem ; 440: 138215, 2024 May 15.
Article in English | MEDLINE | ID: mdl-38128428

ABSTRACT

The aim of this work was to assess the potential of nanoemulsions stabilized by mixed soy protein with multi-conformation as curcumin carrier, and the influence of oil volume fraction on stability and gastrointestinal behavior of curcumin-loaded emulsion was investigated. Loading efficiency showed a slight increase with higher oil content, though the difference was not statistically significant. With the increase of oil, the viscosity (Pa‧s), thixotropy (area of hysteresis loop) and particle size of the emulsion increased, which facilitated the physical and chemical stability of curcumin-loaded emulsion. However, the free fatty acid release rate and bioaccessibility of curcumin was negatively correlated with the oil volume fraction and the particle size of emulsion after gastric digestion. Notably, the digestion in stomach did not affect the structure of interfacial protein, demonstrating that protein-based nanoemulsions exhibited resistance to gastric digestion. This study provides theoretical guidance for the application of protein-based emulsion in curcumin delivery.


Subject(s)
Curcumin , Emulsions/chemistry , Curcumin/chemistry , Soybean Proteins/metabolism , Gastrointestinal Tract/metabolism , Stomach , Particle Size , Digestion
13.
ACS Chem Neurosci ; 15(1): 119-133, 2024 Jan 03.
Article in English | MEDLINE | ID: mdl-38109073

ABSTRACT

Fragile X syndrome (FXS), the leading cause of inherited intellectual disability and autism, is caused by the transcriptional silencing of the FMR1 gene, which encodes the fragile X messenger ribonucleoprotein (FMRP). FMRP interacts with numerous brain mRNAs that are involved in synaptic plasticity and implicated in autism spectrum disorders. Our published studies indicate that single-source, soy-based diets are associated with increased seizures and autism. Thus, there is an acute need for an unbiased protein marker identification in FXS in response to soy consumption. Herein, we present a spatial proteomics approach integrating mass spectrometry imaging with label-free proteomics in the FXS mouse model to map the spatial distribution and quantify levels of proteins in the hippocampus and hypothalamus brain regions. In total, 1250 unique peptides were spatially resolved, demonstrating the diverse array of peptidomes present in the tissue slices and the broad coverage of the strategy. A group of proteins that are known to be involved in glycolysis, synaptic transmission, and coexpression network analysis suggest a significant association between soy proteins and metabolic and synaptic processes in the Fmr1KO brain. Ultimately, this spatial proteomics work represents a crucial step toward identifying potential candidate protein markers and novel therapeutic targets for FXS.


Subject(s)
Fragile X Syndrome , Soybean Proteins , Mice , Animals , Soybean Proteins/metabolism , Fragile X Mental Retardation Protein/genetics , Fragile X Mental Retardation Protein/metabolism , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Fragile X Syndrome/metabolism , Proteomics , Mice, Knockout , Disease Models, Animal
14.
Molecules ; 28(24)2023 Dec 08.
Article in English | MEDLINE | ID: mdl-38138505

ABSTRACT

Soybean meal (SBM) is a high-quality vegetable protein, whose application is greatly limited due to its high molecular weight and anti-nutritional properties. The aim of this study was to modify the protein of soybean meal via solid-state fermentation of Bacillus subtilis. The fermentation conditions were optimized as, finally, the best process parameters were obtained, namely fermentation temperature of 37 °C, inoculum amount of 12%, time of 47 h, and material-liquid ratio of 1:0.58, which improved the content of acid-soluble protein. To explore the utilization of modified SBM as a food ingredient, the protein structure and properties were investigated. Compared to SBM, the protein secondary structure of fermented soybean meal (FSBM) from the optimal process decreased by 8.3% for α-helix content, increased by 3.08% for ß-sheet, increased by 2.71% for ß-turn, and increased by 2.51% for random coil. SDS-PAGE patterns showed that its 25-250 KDa bands appeared to be significantly attenuated, with multiple newborn peptide bands smaller than 25 KDa. The analysis of particle size and zeta potential showed that fermentation reduced the average particle size and increased the absolute value of zeta potential. It was visualized by SEM and CLSM maps that the macromolecular proteins in FSBM were broken down into fragmented pieces with a folded and porous surface structure. Fermentation increased the solubility, decreased the hydrophobicity, increased the free sulfhydryl content, decreased the antigenicity, improved the protein properties of SBM, and promoted further processing and production of FSBM as a food ingredient.


Subject(s)
Food Ingredients , Soybean Proteins , Humans , Infant, Newborn , Soybean Proteins/metabolism , Bacillus subtilis/metabolism , Fermentation , Flour , Glycine max , Animal Feed/analysis
15.
Biomater Adv ; 155: 213682, 2023 Dec.
Article in English | MEDLINE | ID: mdl-37925826

ABSTRACT

Chronic wounds are a worldwide problem that affect >40 million people every year. The constant inflammatory status accompanied by prolonged bacterial infections reduce patient's quality of life and life expectancy drastically. An important cell type involved in the wound healing process are mesenchymal stromal cells (MSCs) due to their long-term demonstrated immunomodulatory and pro-regenerative capacity. Thus, in this work, we leveraged and compared the therapeutic properties of MSCs derived from both adipose tissue and hair follicle, which we combined with sponge-like scaffolds (SLS) made of valorized soy protein and ß-chitin. In this regard, the combination of these cells with biomaterials permitted us to obtain a multifunctional therapy that allowed high cell retention and growing rates while maintaining adequate cell-viability for several days. Furthermore, this combined therapy demonstrated to increase fibroblasts and keratinocytes migration, promote human umbilical vein endothelial cells angiogenesis and protect fibroblasts from highly proteolytic environments. Finally, this combined therapy demonstrated to be highly effective in reducing wound healing time in vivo with only one treatment change during all the experimental procedure, also promoting a more functional and native-like healed skin.


Subject(s)
Diabetes Mellitus , Mesenchymal Stem Cells , Humans , Soybean Proteins/pharmacology , Soybean Proteins/therapeutic use , Soybean Proteins/metabolism , Hair Follicle , Chitin/pharmacology , Chitin/therapeutic use , Chitin/metabolism , Quality of Life , Wound Healing , Mesenchymal Stem Cells/metabolism , Adipose Tissue , Diabetes Mellitus/metabolism , Human Umbilical Vein Endothelial Cells
16.
BMC Genomics ; 24(1): 596, 2023 Oct 07.
Article in English | MEDLINE | ID: mdl-37805454

ABSTRACT

BACKGROUND: Soybean is one of the most important oil crops in the world, and its protein and fat are the primary sources of edible oil and vegetable protein. The effective components in soybean protein and fat have positive effects on improving human immunity, anti-tumor, and regulating blood lipids and metabolism. Therefore, increasing the contents of protein and fat in soybeans is essential for improving the quality of soybeans. RESULTS: This study selected 292 soybean lines from different regions as experimental materials, based on SLAF-seq sequencing technology, and performed genome-wide association study (GWAS) on the phenotype data from 2019-2021 Planted at the experimental base of Jilin Agricultural University, such as the contents of protein and fat of soybeans. Through the GLM model and MLM model, four SNP sites (Gm09_39012959, Gm12_35492373, Gm16_9297124, and Gm20_24678362) that were significantly related to soybean fat content were associated for three consecutive years, and two SNP sites (Gm09_39012959 and Gm20_24678362) that were significantly related to soybean protein content were associated. By the annotation and enrichment of genes within the 100 Kb region of SNP loci flanking, two genes (Glyma.09G158100 and Glyma.09G158200) related to soybean protein synthesis and one gene (Glyma.12G180200) related to lipid metabolism were selected. By the preliminary verification of expression levels of genes with qPCR, it is found that during the periods of R6 and R7 of the accumulation of soybean protein and fat, Glyma.09G158100 and Glyma.09G158200 are positive regulatory genes that promote protein synthesis and accumulation, while Glyma.12G180200 is the negative regulatory gene that inhibits fat accumulation. CONCLUSIONS: These results lay the basis for further verifying the gene function and studying the molecular mechanisms regulating the accumulation of protein and fat in soybean seeds.


Subject(s)
Genome-Wide Association Study , Soybean Proteins , Humans , Soybean Proteins/genetics , Soybean Proteins/metabolism , Quantitative Trait Loci , Glycine max/physiology , Genes, Plant , Seeds/metabolism , Polymorphism, Single Nucleotide
17.
Int J Mol Sci ; 24(18)2023 Sep 15.
Article in English | MEDLINE | ID: mdl-37762432

ABSTRACT

Soybean (Glycine max (L.) Merr.) is an important source of plant protein, the nutritional quality of which is considerably affected by the content of the sulfur-containing amino acid, methionine (Met). To improve the quality of soybean protein and increase the Met content in seeds, soybean cystathionine γ-synthase 2 (GmCGS2), the first unique enzyme in Met biosynthesis, was overexpressed in the soybean cultivar "Jack", producing three transgenic lines (OE3, OE4, and OE10). We detected a considerable increase in the content of free Met and other free amino acids in the developing seeds of the three transgenic lines at the 15th and 75th days after flowering (15D and 75D). In addition, transcriptome analysis showed that the expression of genes related to Met biosynthesis from the aspartate-family pathway and S-methyl Met cycle was promoted in developing green seeds of OE10. Ultimately, the accumulation of total amino acids and soluble proteins in transgenic mature seeds was promoted. Altogether, these results indicated that GmCGS2 plays an important role in Met biosynthesis, by providing a basis for improving the nutritional quality of soybean seeds.


Subject(s)
Amino Acids , Glycine max , Glycine max/metabolism , Amino Acids/metabolism , Soybean Proteins/genetics , Soybean Proteins/metabolism , Plant Proteins/metabolism , Seeds/metabolism , Plants, Genetically Modified/metabolism , Gene Expression Regulation, Plant
18.
J Agric Food Chem ; 71(39): 14109-14124, 2023 Oct 04.
Article in English | MEDLINE | ID: mdl-37749803

ABSTRACT

Soil saline-alkalization is a significant constraint for soybean production. Owing to higher genetic diversity of wild soybean, we compared the proteomic landscape of saline-alkaline stress-tolerant (SWBY032) and stress-sensitive (SWLJ092) wild soybean (Glycine soja) strains under saline and saline-alkaline stress. Out of 346 differentially expressed proteins (DEPs) specifically involved in saline-alkaline stress, 159 and 133 DEPs were identified in only SWLJ092 and SWBY032, respectively. Functional annotations revealed that more ribosome proteins were downregulated in SWLJ092, whereas more membrane transporters were upregulated in SWBY032. Moreover, protein-protein interaction analysis of 133 DEPs revealed that 14 protein-synthesis- and 2 TCA-cycle-related DEPs might alter saline-alkaline tolerance by affecting protein synthesis and amino acid metabolism. Furthermore, we confirmed G. soja tonoplast intrinsic protein (GsTIP2-1 and GsTIP2-2), inositol transporter (GsINT1), sucrose transport protein (GsSUC4), and autoinhibited Ca2+-ATPase (GsACA11) as tonoplast transporters can synergistically improve saline-alkaline tolerance in soybean, possibly by relieving the inhibition of protein synthesis and amino acid metabolism. Overall, our findings provided a foundation for molecular breeding of a saline-alkaline stress-tolerant soybean.


Subject(s)
Fabaceae , Glycine max , Glycine max/metabolism , Proteomics , Fabaceae/metabolism , Soybean Proteins/metabolism , Membrane Transport Proteins/metabolism , Genotype , Amino Acids/metabolism , Glycine/metabolism
19.
Sports Med ; 53(12): 2417-2446, 2023 Dec.
Article in English | MEDLINE | ID: mdl-37603200

ABSTRACT

BACKGROUND: Protein supplements are important to maintain optimum health and physical performance, particularly in athletes and active individuals to repair and rebuild their skeletal muscles and connective tissues. Soy protein (SP) has gained popularity in recent years as an alternative to animal proteins. OBJECTIVES: This systematic review evaluates the evidence from randomised controlled clinical trials of the effects of SP supplementation in active individuals and athletes in terms of muscle adaptations, metabolic and antioxidant status, hormonal response and exercise performance. It also explores the differences in SP supplementation effects in comparison to whey protein. METHODS: A systematic search was conducted in PubMed, Embase and Web of Science, as well as a manual search in Google Scholar and EBSCO, on 27 June 2023. Randomised controlled trials that evaluated the applications of SPs supplementation on sports and athletic-related outcomes that are linked with exercise performance, adaptations and biomarkers in athletes and physically active adolescents and young adults (14 to 39 years old) were included, otherwise, studies were excluded. The risk of bias was assessed according to Cochrane's revised risk of bias tool. RESULTS: A total of 19 eligible original research articles were included that investigated the effect of SP supplementation on muscle adaptations (n = 9), metabolic and antioxidant status (n = 6), hormonal response (n = 6) and exercise performance (n = 6). Some studies investigated more than one effect. SP was found to provide identical increases in lean mass compared to whey in some studies. SP consumption promoted the reduction of exercise-induced metabolic/blood circulating biomarkers such as triglycerides, uric acid and lactate. Better antioxidant capacity against oxidative stress has been seen with respect to whey protein in long-term studies. Some studies reported testosterone and cortisol fluctuations related to SP; however, more research is required. All studies on SP and endurance performance suggested the potential beneficial effects of SP supplementation (10-53.3 g) on exercise performance by improving high-intensity and high-speed running performance, enhancing maximal cardiac output, delaying fatigue and improving isometric muscle strength, improving endurance in recreational cyclists, increasing running velocity and decreasing accumulated lactate levels; however, studies determining the efficacy of soy protein on VO2max provided conflicted results. CONCLUSION: It is possible to recommend SP to athletes and active individuals in place of conventional protein supplements by assessing their dosage and effectiveness in relation to different types of training. SP may enhance lean mass compared with other protein sources, enhance the antioxidant status, and reduce oxidative stress. SP supplementation had an inconsistent effect on testosterone and cortisol levels. SP supplementation may be beneficial, especially after muscle damage, high-intensity/high-speed or repeated bouts of strenuous exercise.


Subject(s)
Antioxidants , Soybean Proteins , Adolescent , Adult , Humans , Young Adult , Antioxidants/pharmacology , Athletes , Biomarkers , Dietary Supplements , Hydrocortisone , Lactates , Muscle, Skeletal/metabolism , Soybean Proteins/pharmacology , Soybean Proteins/metabolism , Testosterone/metabolism , Whey Proteins/metabolism , Whey Proteins/pharmacology , Randomized Controlled Trials as Topic
20.
Biol Pharm Bull ; 46(7): 898-906, 2023.
Article in English | MEDLINE | ID: mdl-37394641

ABSTRACT

Food-derived peptides have various biological activities. When food proteins are ingested orally, they are digested into peptides by endogenous digestive enzymes and absorbed by the immune cell-rich intestinal tract. However, little is known about the effects of food-derived peptides on the motility of human immune cells. In this study, we aimed to understand the effects of peptides derived from a soybean protein ß-conglycinin on the motility of human peripheral polymorphonuclear leukocytes. We illustrated that MITL and MITLAIPVNKPGR, produced by digestion using in-vivo enzymes (trypsin and pancreatic elastase) of ß-conglycinin, induces the migration of dibutyryl cAMP (Bt2 cAMP)-differentiated human promyelocytic leukemia 60 (HL-60) cells and human polymorphonuclear leukocytes in a dose- and time-dependent manner. This migration was more pronounced in Bt2 cAMP-differentiated HL-60 cells; mRNA expression of formyl peptide receptor (FPR) 1 increased significantly than in all-trans-retinoic acid (ATRA)-differentiated HL-60 cells. This migration was inhibited by tert-butoxycarbonyl (Boc)-MLP, an inhibitor of FPR, and by pretreatment with pertussis toxin (PTX). However, the effect was weak when treated with WRW4, a selective inhibitor of the FPR2. We then demonstrated that MITLAIPVNKPGR induced intracellular calcium responses in human polymorphonuclear leukocytes and Bt2 cAMP-HL60 cells. Furthermore, pre-treatment by fMLP desensitized the calcium response of MITLAIPVNKPGR in these cells. From the above, MITLAIPVNKPGR and MITL derived from soybean ß-conglycinin induced polymorphonuclear leukocyte migration via the FPR1-dependent mechanism. We found chemotactic peptides to human polymorphonuclear leukocytes, which are the endogenous enzyme digests of soybean protein.


Subject(s)
Neutrophils , Soybean Proteins , Humans , Neutrophils/metabolism , Soybean Proteins/pharmacology , Soybean Proteins/metabolism , Calcium/metabolism , Peptides/pharmacology
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