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The aims of the study were to degrade the anti-nutritional factors (ANFs) such as phytic acid, glycinin, and β-conglycinin and improve the values of soybean meal (SBM). Firstly, in this study, a strain PY-4B which exhibited the best enzymatic activities of protease (403.3 ± 17.8 U/mL) and phytase (62.9 ± 2.9 U/mL) was isolated and screened among the isolates. Based on the analysis of physiological and biochemical characteristics and 16S rDNA sequence, the strain PY-4B was identified and named as Pseudomonas PY-4B. Next, Pseudomonas PY-4B was applied to fermentation of SBM. The results showed that the contents of glycinin and β-conglycinin were decreased by 57–63%, and the phytic acid was remarkably degraded by 62.5% due to the fermentation of SBM by Pseudomonas PY-4B. The degradation of glycinin and β-conglycinin resulted in increase of contents of water-soluble proteins and amino acids in fermented SBM. Moreover, Pseudomonas PY-4B exhibited no hemolytic activity and slight inhibitory effect on the growth of pathogen Staphylococcus aureus and the wide range of pH tolerance (3 to 9). In summary, our study indicates that isolated strain Pseudomonas PY-4B is a safe and applicable strain and has the ability to effectively degrade the ANFs (phytic acid, glycinin, and β-conglycinin) in SBM by fermentation.

Ultrasonic technology is often used to modify proteins. Here, we investigated the effects of ultrasound alone or in combination with other heating methods on emulsifying properties and structure of glycinin (11S globulin). Structural alterations were assessed with Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS–PAGE), intrinsic fluorescence spectroscopy, ultraviolet (UV) absorption spectroscopy, and Fourier transform infrared (FTIR) spectroscopy. The size distribution and zeta-potential of 11S globulin were evaluated with a particle size analyzer. An SDS-PAGE analysis showed no remarkable changes in the primary structure of 11S globulin. Ultrasound treatment disrupted the 11S globulin aggregates into small particles with uniform size, narrowed their distribution and increased their surface charge density. Fluorescent spectroscopy and second-derivative UV spectroscopy revealed that ultrasound coupled with heating induced partial unfolding of 11S globulin, increasing its flexibility and hydrophobicity. FTIR further showed that the random coil and α-helix contents were higher while β-turn and β-sheet contents were lower in ultrasound combined with heating group compared to the control group. Consequently, the oil-water interface entirely distributed protein and reduced the surface tension. Moreover, ultrasound combined with heating at 60 °C increased the emulsifying activity index and emulsifying stability index of 11S globulins by 6.49-folds and 2.90-folds, respectively. These findings suggest that ultrasound combined with mild heating modifies the emulsification properties of 11S globulin.

Ensuring the safety and longevity of food products is a major priority in the meat industry. This paper focused on assessing the soybean-glycinin (SBG) impact on the quality and shelf-life of beef Musculus longissimus thoracis et lumborum ( LTL ) steaks and their potential in-vivo adverse consequences on foodborne pathogens and quantitative minimum biocidal values. Over 15 chilling-days at 4 °C, fresh LTL -steaks were fortified with either 1 mg/g of SBG (SBG1) or 0.5 mg/g (SBG0.5) and compared to control for physicochemical, oxidative, and microbiological attributes. Antibiotic-susceptible pathogens, Staphylococcus aureus, Salmonella enterica , and Escherichia coli were suppressed by 0.98 mg/mL of SBG, whereas antibiotic-resistant Salmonella enterica and Escherichia coli required higher biocidal dosages of 50 and 6.25 mg/mL, respectively. SBG-fortification kept LTL -steaks’ pH below borderline until day 12, increased water-holding capacity, reduced cooking loss at the storage end, and significantly improved tenderness ( p  < 0.05). LTL -steaks’ lightness, redness, and chroma were statistically unaffected by SBG1.0-fortification compared to the control; however, there were notable growing-patterns during the last two storage-periods ( p  < 0.05). Except the sixth- and ninth-day storage-periods, SBG1.0-fortification increased the LTL -steaks yellowness and hue compared to the control, indicating brighter, less red meat ( p  < 0.05). SBG-fortification had a dose-dependent antioxidant and bactericidal impact on both native microflora and inoculated pathogens, Listeria monocytogenes and Salmonella . Conclusively, SBG-fortification activities to improve LTL -steaks oxidative stability and shelf-life beyond 15 days and to inhibit inoculated-pathogens growth by one log CFU/g above or below the inoculation dose, validating SBG as a promising feasible meat preservation strategy.

Summary Cis‐regulatory elements in promoters are major determinants of binding specificity of transcription factors (TFs) for transcriptional regulation. To improve our understanding of how these short DNA sequences regulate gene expression, synthetic promoters consisting of both classical (CACGTG) and variant G‐box core sequences along with different flanking sequences derived from the promoters of three different highly expressing soybean genes, were constructed and used to regulate a green fluorescent protein (gfp) gene. Use of the classical 6‐bp G‐box provided information on the base level of GFP expression while modifications to the 2–4 flanking bases on either side of the G‐box influenced the intensity of gene expression in both transiently transformed lima bean cotyledons and stably transformed soybean hairy roots. The proximal 2‐bp sequences on either flank of the G‐box significantly affected G‐box activity, while the distal 2‐bp flanking nucleotides also influenced gene expression albeit with a decreasing effect. Manipulation of the upstream 2‐ to 4‐bp flanking sequence of a G‐box variant (GACGTG), found in the proximal region of a relatively weak soybean glycinin promoter, significantly enhanced promoter activity using both transient and stable expression assays, if the G‐box variant was first converted into a classical G‐box (CACGTG). In addition to increasing our understanding of regulatory element composition and structure, this study shows that minimal targeted changes in native promoter sequences can lead to enhanced gene expression, and suggests that genome editing of the promoter region can result in useful and predictable changes in native gene expression.

Endoplasmic reticulum (ER) stress is a crucial factor in the pathogenesis of intestinal diseases. Soybean antigenic proteins (β-conglycinin and soy glycinin) induce hypersensitivity reactions and intestinal barrier damage. However, whether this damage is associated with ER stress, autophagy, and the gut microbiome is largely unclear. Therefore, in this study, we aimed to investigate the effect of dietary supplementation with soy glycinin (11S glycinin) and β-conglycinin (7S glycinin) on intestinal ER stress, autophagy, and flora in weaned piglets. Thirty healthy 21-day-old weaned “Duroc × Long White × Yorkshire” piglets were randomly divided into three groups and fed a basic, 7S-supplemented, or 11S-supplemented diet for one week. The results indicated that 7S/11S glycinin disrupted growth performance, damaged intestinal barrier integrity, and impaired goblet cell function in piglets (p < 0.05). Moreover, 7S/11S glycinin induced ER stress and blocked autophagic flux in the jejunum (p < 0.05) and increased the relative abundance of pathogenic flora (p < 0.01) and decreased that of beneficial flora (p < 0.05). In conclusion, 7S/11S glycinin induces intestinal ER stress, autophagic flux blockage, microbiota imbalance, and intestinal barrier damage in piglets.

PurposeSoybean glycinin (11S) and β-conglycinin (7S) are major antigenic proteins in soybean and can induce a variety of allergic reactions in the young animals. This study aimed to investigate the effect of 7S and 11S allergens on the intestine of piglets.MethodsThirty healthy 21-day-old weaned “Duroc × Long White × Yorkshire” piglets were randomly divided into three groups fed with the basic diet, the 7S supplemented basic diet, or the 11S supplemented basic diet for 1 week. Allergy markers, intestinal permeability, oxidative stress, and inflammatory reactions were detected, and we observed different sections of intestinal tissue. The expressions of genes and proteins related to NOD-like receptor thermal protein domain associated protein 3 (NLRP-3) signaling pathway were detected by IHC, RT-qPCR, and WB.ResultsSevere diarrhea and decreased growth rate were observed in the 7S and 11S groups. Typical allergy markers include IgE production and significant elevations of histamine and 5-hydroxytryptamine (5-HT). More aggressive intestinal inflammation and barrier dysfunction were observed in the experimental weaned piglets. In addition, 7S and 11S supplementation increased the levels of 8-hydroxy-2 deoxyguanosine (8-OHdG) and nitrotyrosine, triggering oxidative stress. Furthermore, higher expression levels of NLRP-3 inflammasome ASC, caspase-1, IL-1β, and IL-18 were observed in the duodenum, jejunum, and ileum.ConclusionWe confirmed that 7S and 11S damaged the intestinal barrier of weaned piglets and may be associated with the onset of oxidative stress and inflammatory response. However, the molecular mechanism underlying these reactions deserves further study.

Background: Corn and soybean meal (SBM) are two of the most common feed ingredients used in pig feeds.However, a variety of antinutritional factors (ANFs) present in corn and SBM can interfere with the bioavailability of nutrients and have negative health effects on the pigs. In the present study, two-stage fermentation using Bacillus subtilis followed by Enterococcus faecium was carried out to degrade ANFs and improve the nutritional quality of corn and SBM mixed feed. Furthermore, the microbial composition and in vitro nutrient digestibility of inoculated mixed feed were determined and compared those of the uninoculated controls.Results: During the fermentation process, B. subtilis and lactic acid bacteria (LAB) were the main dominant bacteria in the solid-state fermented inoculated feed, and fermentation produced a large amount of lactic acid (170 mmoL/kg),which resulted in a lower pH (5.0 vs. 6.4) than the fermented uninoculated feed. The amounts of soybean antigenic proteins (β-conglycinin and glycinin) in mixed feed were significantly decreased after first-stage fermentation with B. subtilis. Inoculated mixed feed following two-stage fermentation contained greater concentratioin of crude protein (CP), ash and total phosphorus (P) compared to uninoculated feed, whereas the concentrations of neutral detergent fiber (NDF), hemicellulose and phytate P in fermendted inoculated feed declined (P < 0.05) by 38%, 53%, and 46%,respectively. Notably, the content of trichloroacetic acid soluble protein (TCA-SP), particularly that of small peptides and free amino acids (AA), increased 6.5 fold following two-stage fermentation. There was no difference in the total AA content between fermented inoculated and uninoculated feed. However, aromatic AAs (Phe and Tyr) and Lys in inoculated feed increased, and some polar AAs, including Arg, Asp, and Glu, decreased compared with the uninoculated feed. In vitro dry matter and CP digestibility of inoculated feed improved (P < 0.05) compared with the uninoculated feed.Conclusions: Our results suggest that two-stage fermentation using B. subtilis followed by E. faecium is an effective approach to improve the quality of corn-soybean meal mixed feed.

Soybean proteins are limited by their low contents of methionine and cysteine. Herein, 7S globulin accumulation was reduced using RNA interference to silence CG-β-1 expression, and the content of the A2B1a subunit was largely increased under the soybean seed-specific oleosin8 promoter. The results showed that the sulfur-containing amino acid content in soybean seeds drastically improved, reaching 79.194 nmol/mg, and the 11S/7S ratio had a 1.89-fold increase compared to the wild-type acceptor. The secondary structures of 11S globulin were also altered, and the β-sheet content increased with decreasing β-turn content, which was confirmed by Fourier transform infrared spectroscopy, Raman spectroscopy and circular dichroism analysis. Our findings suggested that raising the accumulation of 11S glycinin at the expense of reducing the content of 7S globulin is an attractive and precise engineering strategy to increase the amount of sulfur-containing amino acids, and soybean proteins with A2B1a subunits of 11S isolates improved, and β-subunits of 7S fractions reduced simultaneously might be an effective new material for food production.

High temperatures during seed development can affect the seed yield and quality in many crops. Here, we analyzed how high temperature alters the main seed storage compounds (lipid and protein) in soybean. At five days after R5 stage (initial seed filling stage), soybean plants were treated with control (20/20ºC day/night) and high temperature (30/30ºC day/night). After treatment, immature seed was sampled, analyzed for lipid and protein contents and for expression of seed storage compounds related genes. High temperature during seed filling increased lipid content but decreased protein content, associating with yield reduction. It increased the expression of two genes related to seed lipid biosynthesis (GmBCCP2 and GmKAS1) and genes for a lipid biosynthesis regulator (GmWRI1) and its transcription factor (GmDREBL), and decreased the expression of genes related to lipid degradation such as GmACXs. High temperature downregulated genes related to seed storage protein (GmGy1, GmGy2, GmGy4, GmGy5 and Gmβ-conglycinin) and upregulated genes for cysteine and aspartate proteinases. Therefore, high temperature during seed filling preferentially accumulates lipid than protein content in seed, although seed yield reduction was associated with lower seed protein content in soybean. Our study provides insights for further improvements of soybean seed oil under abiotic stress such as heat stress. Abbreviations: DAT: days after treatment; TF: transcription factor; DREBL: Dehydration-responsive Element-binding L; WRI1: Wrinkled 1; PK: Ketoacyl acyl carrier protein synthase 1; PEP: phosphoenolpyruvate; BCCP2: Biotin carboxyl carrier protein; KAS1: ketoacyl acyl carrier protein synthase 1; ACX: Acyl-coenzyme A peroxidase; MS: Malate synthase; PEPCK: Phosphoenolpyruvate carboxykinase; Gy: Glycinin; CysP: Cysteine Proteinase; SoyAP: Aspartic Proteinase; EF1b: Elongation factor 1b.

Soy glycinin (11S) is involved in immune regulation. As an additive, sodium butyrate (SB) can relieve inflammation caused by 11S. To further delve into the mechanisms. A diet containing 50% fishmeal was the control group (FM group), and the experimental groups consisted of the FM group baseline plus 2% glycinin (GL group), 8% glycinin (GH group), and 8% glycinin + 0.13% sodium butyrate (GH-SB group). The specific growth ratio (SGR), feed utilization, and density of distal intestinal (DI) type II mucous cells were increased in the GL group. In the serum, IFN-γ was significantly upregulated in the GL group, and IgG and IL-1β were upregulated in the GH group. IgG, IL-1β, and TNF-α in the GH-SB group were significantly downregulated compared to those in the GH group. The mRNA levels of mTOR C1, mTOR C2, and Deptor were upregulated in the GL, GH, and GH-SB groups in the DI compared with those in the FM group, while the mRNA levels of mTOR C1 and Deptor in the GH group were higher than those in the GL and GH-SB groups. 4E-BP1, RICTOR, PRR5, MHC II, and CD4 were upregulated in the GH group. TSC1, mLST8, and NFY mRNA levels in the GL and GH-SB groups were upregulated compared with those in the FM and GH groups. Western blotting showed P-PI 3 K Ser294 /T-PI 3 K, P-Akt Ser473 /T-Akt, and P-mTOR Ser2448 /T-mTOR were upregulated in the GH group. Collectively, our results demonstrate that low-dose 11S could improve serum immune by secreting IFN-γ. The overexpression of IgG and IL-1β is the reason that high-dose 11S reduces serum immune function, and supplementing SB can suppress this overexpression. Low-dose 11S can block the relationship between PI 3 K and mTOR C2. It can also inhibit the expression of 4E-BP1 through mTOR C1. High-dose 11S upregulates 4E-BP2 through mTOR C1, aggravating intestinal inflammation. SB could relieve inflammation by blocking PI 3 K/mTOR C2 and inhibiting 4E-BP2. Generally speaking, the hybrid grouper obtained different serum and DI immune responses under different doses of 11S, and these responses were ultimately manifested in growth performance. SB can effectively enhance serum immunity and relieve intestinal inflammation caused by high dose 11S.