Homologous Overexpression of Tyrosinase in Trichoderma reesei and Its Application in Glycinin Cross-Linking.

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.

Albumin to globulin ratio (AGR) in systemic lupus erythematosus: correlation with disease activity.

OBJECTIVE: To investigate the role of albumin-to-globulin ratio (AGR) in systemic lupus erythematosus (SLE) and its relationship with disease activity. METHODS: This retrospective study consecutively selected patients with SLE and healthy controls. Patients were divided into three groups according to the SLE Disease Activity Index 2000 (SLEDAI-2K): group 1 (mild disease activity, SLEDAI-2K ≤ 6), group 2 (moderate disease activity, SLEDAI-2K 7-12) and group 3 (severe disease activity, SLEDAI-2K > 12). Predictors of SLE disease activity were analysed by ordinal logistical regression. RESULTS: A total of 101 Chinese patients with SLE and 75 healthy Chinese controls were included. Patients with SLE had lower AGR values than healthy individuals, and group 3 patients with SLE displayed lower AGR values than those in group 1, but similar values to group 2. AGR was inversely correlated with SLEDAI-2K (r = -0.543). Ordinal logistic regression analysis showed that lower AGR (ß = -1.319) and lower complement C4 (ß = -1.073) were independent risk factors for SLE disease activity. CONCLUSIONS: AGR was decreased in patients with SLE and may be utilized as a useful inflammatory biomarker for monitoring SLE disease activity.

Prefeeding of Clarias gariepinus with Spirulina platensis counteracts petroleum hydrocarbons-induced hepato- and nephrotoxicity.

Petroleum aromatic hydrocarbons are considered one of the most dangerous aquatic pollutants due to their widespread across water bodies, persistence, and extension to the food chain. To our knowledge, there hasn't been any research investigating the hepatorenoprotective effects of Spirulina platensis (SP) against toxicity induced by these environmental toxicants in fish. Thus, we decided to explore its potential safeguarding against benzene and toluene exposure in adult Clarias gariepinus. To achieve this objective, fish were divided into five groups (60 per group; 20 per replicate). The first group served as a control. The second and third groups were intoxicated with benzene and toluene at doses of 0.762 and 26.614 ng/L, respectively for 15 days. The fourth and fifth groups (SP + benzene and SP + toluene, respectively) were challenged with benzene and toluene as previously mentioned following dietary inclusion of SP at a dose of 5 g/kg diet for 30 days. The marked increase in liver metabolizing enzymes, glucose, total protein, albumin, globulin, albumin/globulin ratio, and creatinine confirmed the hepato- and nephrotoxic impacts of benzene and toluene. These outcomes were coupled with cytopathological affections and excessive collagen deposition. The incorporation of SP in ration formulation, on the contrary, restored the previously mentioned toxicological profile due to its antioxidant and cytoprotective attributes. Regardless of SP intervention, the renal tissues still displayed histo-architectural lesions, because of insufficient dose and timeframe. Additional research will be required to identify the ideal SP remediation regimen.

Determining the Impact of Genotype × Environment on Oat Protein Isolate Composition Using HPLC and LC-MS Techniques.

The effect of genotype and environment on oat protein composition was analyzed through size exclusion-high-performance liquid chromatography (SE-HPLC) and liquid chromatography-mass spectrometry (LC-MS) to characterize oat protein isolate (OPI) extracted from three genotypes grown at three locations in the Canadian Prairies. SE-HPLC identified four fractions in OPI, including polymeric globulins, avenins, glutelins, and albumins, and smaller proteins. The protein composition was dependent on the environment, rather than the genotype. The proteins identified through LC-MS were grouped into eight categories, including globulins, prolamins/avenins, glutelins, enzymes/albumins, enzyme inhibitors, heat shock proteins, grain softness proteins, and allergenic proteins. Three main globulin protein types were also identified, including the P14812|SSG2-12S seed storage globulin, the Q6UJY8_TRITU-globulin, and the M7ZQM3_TRIUA-Globulin-1 S. Principal component analysis indicated that samples from Manitoba showed a positive association with the M7ZQM3_TRIUA-Globulin-1 S allele and Q6UJY8_TRITU-globulin, while samples from Alberta and Saskatchewan had a negative association with them. The results show that the influence of G × E on oat protein fractions and their relative composition is crucial to understanding genotypes' behavior in response to different environments.

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.

Effects of pH and salt concentration on freeze-thaw fractionation of soymilk protein.

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.

Lactational performance and nutrients digestibility response of dairy buffaloes fed diets supplemented with probiotic (Streptococcus spp.) and fibrolytic enzymes.

The current study was conducted to explore the productive performance and health status of lactating buffaloes fed diets supplemented with probiotic and/or fibrolytic enzymes. Forty multiparous lactating Egyptian buffaloes (body weight 451 ± 8.5 kg) were equally assigned to four experimental groups: (1) the first group fed control diet, (2) second experimental group fed control diet plus 4 g of probiotic/kg dry matter (DM) (probiotic), (3) third experimental group fed control diet plus 4 g of fibrolytic enzymes/kg DM (enzymes) and (4) fourth experimental group fed control diet plus 2 g of probiotic + 2 g fibrolytic enzymes/kg DM (Mix), The experiment was extended for 63 days. Nutrients digestibility was estimated, daily milk yield was recorded and milk samples were analyzed for total solids, fat protein, lactose and ash. Blood serum samples were analyzed for glucose, total protein, albumin, urea-N, aspartate transaminase, alanine transaminase and cholesterol concentrations. Results showed that adding probiotic and/or fibrolytic enzymes improved nutrients digestibility (p < 0.05). The probiotic, enzymes and mix groups did not affect (p > 0.05) concentrations of serum total protein, albumin (A), globulin (G), albumin/globulin (A/G) ratio and urea-N concentrations. An improvement in daily milk yield (p < 0.0001) and energy-corrected milk (p = 0.0146) were observed with the probiotic and mix groups compared with the control. In conclusion, this study suggests that supplementing lactating buffaloes' diets with probiotic alone or in combination with fibrolytic enzymes would improve their productive performance without adversely impacting their health.

Sub-lethal impacts of lead poisoning on blood biochemistry, immune function and delta-aminolevulinic acid dehydratase (δ-ALAD) activity in Cape (Gyps coprotheres) and white-backed (G. africanus) Vulture chicks.

Although the prevalence of lead poisoning in southern Africa's Gyps vultures is now well-established, its finer physiological effects on these endangered species remain poorly characterised. We evaluated the sub-lethal impact of acute lead exposure on Cape and White-backed Vulture chicks from two breeding colonies in South Africa, by analysing its possible effects on key blood biochemistry parameters, immune function, packed cell volume and δ-aminolevulinic acid dehydratase (δ-ALAD) activity. All 37 White-backed Vulture nestlings sampled displayed elevated lead levels (>10 µg/dL), and seven had blood [Pb] >100 µg/dL. Eight of 28 Cape Vulture nestlings sampled had blood [Pb] exceeding background exposure, with one showing blood [Pb] >100 µg/dL. Delta-aminolevulinic acid dehydratase (δ-ALAD) activity was significantly and negatively related to blood [Pb] in nestlings from both species, with 50% inhibition of the enzyme predicted to occur at blood [Pb] = 52.8 µg/dL (White-backed Vulture) and 18.8 µg/dL (Cape Vulture). Although no significant relationship was found between % packed cell volume (PCV) and blood [Pb], the relatively lower mean PCV of 32.9% in White-backed Vulture chicks, combined with normal serum protein values, is likely indicative of depression or haemolytic anaemia. The leukogram was consistent in both species, although the presence of immature heterophils suggested an inflammatory response in White-backed Vulture chicks with blood [Pb] >100 µg/dL. Values for cholesterol, triglycerides, total serum protein, albumin, globulin, albumin/globulin ratio, alanine aminotransferase (ALT) and gamma-glutamyl transferase (GGT) were consistent with values previously reported. Calcium and phosphorus concentrations suggested no adverse effects on bone metabolism. A significant decrease in urea: uric acid (U:UA) ratio at blood [Pb] >100 µg/dL in White-backed Vulture chicks, brought about by a decrease in urea production, raises the possibility of hepatic abnormality. These results suggest that δ-ALAD activity may serve as a sensitive biomarker of lead toxicity in both species, while highlighting the need to better understand the significant variability in sensitivity that is observed, even between closely related members of the same genus.

Effects of thermal stress responses in goldfish (Carassius auratus): growth performance, total carotenoids and coloration, hematology, liver histology, and critical thermal maximum.

The present study aimed to investigate the effect of thermal stress on growth, feed utilization, coloration, hematology, liver histology, and critical thermal maximum (CTmax) in goldfish (Carassius auratus) cultured at three different acclimation temperatures including 27 °C, 30 °C, and 34 °C for 10 weeks. Goldfish were assigned randomly to tanks with a quadruplicate setup, accommodating 20 fish per tank. The result showed that fish acclimated to different temperatures did not significantly differ in weight gain (WG) and specific growth rate (SGR). However, increasing temperature significantly decreased feed efficiency ratio (FER), protein efficiency ratio (PER), and protein productive value (PPV), but significantly increased feed conversion ratio (FCR) (P < 0.05). The coloration parameters significantly decreased by high temperature in the trunk region with increasing temperature (L* and a* at week 5; L*, a*, and b* at week 10; P < 0.05). Total carotenoid contents in serum, fin, muscle, and skin also significantly decreased with increasing temperature (P < 0.05). Total protein, albumin, and globulin levels exhibited a notable decrease, while the albumin: globulin ratio showed a slight insignificant increase, with increasing temperature. Aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), total cholesterol, and triglycerides significantly increased with increasing temperature (P < 0.05). While, high-density lipoprotein cholesterol (HDL-c) decreased linearly (P < 0.05). Glucose and cortisol levels linearly increased with increasing temperature, the highest levels being observed in the 34 °C group. Liver histology showed swollen hepatocytes, nuclei displacement, and infiltration of inflammation in fish cultured at 34 °C. Goldfish acclimated to 34 °C displayed a higher CTmax of 43.83 °C compared to other groups. The present study showed that temperature should be kept below 34 °C for goldfish culture to prevent high FCR, fading coloration, and liver damages.

Gastrointestinal digestion and absorption of soybean ß-conglycinin in an early weaned piglet model: An initial step to the induction of soybean allergy.

To date, it still remains unknown how ß-conglycinin, a major soybean allergen, crosses intestinal epithelial barrier to reach immune cells. The purpose of this study was to elucidate the pathway and molecular mechanism of ß-conglycinin absorption and transport across intestinal mucosal epithelium using a ß-conglycinin allergic piglet model. Ten-day old piglets were orally sensitized with diets containing 2% and 4% ß-conglycinin. The digestion, absorption and transport of ß-conglycinin in gastrointestinal tract was investigated. The results showed that ß-conglycinin had a certain resistance to gastrointestinal digestion, and the digestion-resistant subunits and fragments were absorbed into the intestinal mucosa and then induced an anaphylaxis in early weaned piglets. The absorption occurred in the form of IgE-allergen immune complex through transcellular pathway with CD23 as the receptor. These results provided important clues for using the pathway and molecule as inhibitor target to prevent and alleviate soybean ß-conglycinin allergy in infants.

Soybean glycinin and ß-conglycinin damage the intestinal barrier by triggering oxidative stress and inflammatory response in weaned piglets.

PURPOSE: Soybean glycinin (11S) and ß-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. METHODS: Thirty 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. RESULTS: Severe 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-1ß, and IL-18 were observed in the duodenum, jejunum, and ileum. CONCLUSION: We 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.

Biomacromolecule assembly of soy glycinin-potato starch complexes: Focus on structure, function, and applications.

The effect of the cross-linking mechanism and functional properties of soy glycinin (11S)-potato starch (PS) complexes was investigated in this study. The results showed that the binding effecting and spatial network structure of 11S-PS complexes via heated-induced cross-linking were adjusted by biopolymer ratios. In particular, 11S-PS complexes with the biopolymer ratios of 2:15, had a strongest intermolecular interaction through hydrogen bonds and hydrophobic force. Moreover, 11S-PS complexes at the biopolymer ratios of 2:15 exhibited a finer three-dimensional network structure, which was used as film-forming solution to enhance the barrier performance and mitigate the exposure to the environment. In addition, the 11S-PS complexes coating was effective in moderating the loss of nutrients, thereby extending their storage life in truss tomato preservation experiments. This study provides helpful to insights into the cross-linking mechanism of the 11S-PS complexes and the potential application of food-grade biopolymer composite coatings in food preservation.

Oat AsDA1-2D enhances heat stress tolerance and negatively regulates seed-storage globulin.

The importance of oats has increased because of their high nutritional value and health benefits in the human diet. High-temperature stress during the reproductive growth period has a detrimental effect on grain morphology by changing the structure and concentration of several seed-storage proteins. DA1, a conserved ubiquitin-proteasome pathway component, plays an important role in regulating grain size by controlling cell proliferation in maternal integuments during the grain-filling stage. However, there have been no reports or studies on oat DA1 genes. In this study, we identified three DA1-like genes (AsDA1-2D, AsDA1-5A, and AsDA1-1D) using genome-wide analysis. Among these, AsDA1-2D was found to be responsible for high-temperature stress tolerance via a yeast thermotolerance assay. The physical interaction of AsDA1-2D with oat-storage-globulin (AsGL-4D) and a protease inhibitor (AsPI-4D) was observed using yeast two-hybrid screening. A subcellular localization assay revealed that AsDA1-2D and its interacting proteins are localized in the cytosol and plasma membrane. An in vitro pull-down assay showed that AsDA1-2D forms a complex with both AsPI-4D and AsGL-4D. An in vitro cell-free degradation assay showed that AsGL-4D was degraded by AsDA1-2D under high-temperature conditions and that AsPI-4D inhibited the function of AsDA1-2D. These results suggest that AsDA1-2D acts as a cysteine protease and negatively regulates oat-grain-storage-globulin under heat stress.

Pulse Globulins 11S and 7S: Origins, Purification Methods, and Techno-functional Properties.

A growing interest in pulse proteins in recent years results from their crucial role in the transition toward sustainable food systems. Consequently, current research is mainly focused on the production of protein ingredients and the evaluation of their nutritional and techno-functional properties for the development of animal product analogues. However, the individual impacts of the major proteins 11S legumin and 7S vicilin on pulse techno-functionalities remains unclear. Thus, this review aims to represent current knowledge on pulse 11S and 7S globulin origins, extraction, separation, and purification methods as well as their techno-functionalities. This paper also discusses the principal challenges related to pulse vicilin and legumin purification methods, such as efficiency and environmental concerns, as well as 11S/7S ratio variability. This review highlights the fact that 11S and 7S fractions serve different purposes in pulse functionality and that more efficient and eco-friendly purification techniques are required to properly assess their respective functional attributes. Such research would allow the determination of optimal 11S/7S ratios for the integration of pulse protein ingredients in various food formulations. Hence, food industries would be able to select species/varieties, agronomical methods, and processing methods to produce ingredients with suitable 11S/7S ratios, catering to consumers' ethical, environmental, and nutritional concerns.

Amino acids induce high seed-specific expression driven by a soybean (Glycine max) glycinin seed storage protein promoter.

KEY MESSAGE: We characterize GFP expression driven by a soybean glycinin promoter in transgenic soybean. We demonstrate specific amino acid-mediated induction of this promoter in developing soybean seeds in vitro. In plants, gene expression is primarily regulated by promoter regions which are located upstream of gene coding sequences. Promoters allow transcription in certain tissues and respond to environmental stimuli as well as other inductive phenomena. In soybean, seed storage proteins (SSPs) accumulate during seed development and account for most of the monetary and nutritional value of this crop. To better study the regulatory functions of a SSP promoter, we developed a cotyledon culture system where media and media addenda were evaluated for their effects on cotyledon development and promoter activity. Stably transformed soybean events containing a glycinin SSP promoter regulating the green fluorescent protein (GFP) were generated. Promoter activity, as visualized by GFP expression, was only observed in developing in planta seeds and in vitro-cultured isolated embryos and cotyledons from developing seeds when specific media addenda were included. Asparagine, proline, and especially glutamine induced glycinin promoter activity in cultured cotyledons from developing seeds. Other amino acids did not induce the glycinin promoter. Here, we report, for the first time, induction of a reintroduced glycinin SSP promoter by specific amino acids in cotyledon tissues during seed development.

Entrapment of cyanidin-3-O-glucoside in ß-conglycinin: From interaction to bioaccessibility and antioxidant activity under thermal treatment.

The thermal-induced interaction between ß-conglycinin (7S) and cyanidin-3-O-glucoside (C3G) on the bioaccessibility and antioxidant capacity of C3G was investigated. High ratio of 7S to C3G (1:100) led to a more ordered secondary structure of 7S. Thermal treatment promoted the formation of 7S-C3G complexes via hydrophobic and hydrogen bonds but did not induce the formation of 7S-C3G covalent products. Thermal treatment at 65 °C and 121 °C enhanced the binding affinity of 7S-C3G complexes by 46.19 % and 1203 % compared with 25 °C. The 7S-C3G interaction decreased C3G bioaccessibility by 4.37 %, 8.74 %, and 46.37 % at 25 °C, 65 °C, and 121 °C. Diphenylpicrylhydrazyl (DPPH) and ABTS antioxidant capacity assay indicated an antagonistic effect between 7S and C3G. The increased binding affinity of C3G to 7S limited the bioaccessibility of C3G and promoted the antagonism of antioxidant capacity between 7S and C3G. 7S addition was detrimental to the antioxidant capacity and bioaccessibility of C3G in vitro after thermal processing.

GC-Globulin/Vitamin D-Binding Protein Is Required for Pancreatic α-Cell Adaptation to Metabolic Stress.

GC-globulin (GC), or vitamin D-binding protein, is a multifunctional protein involved in the transport of circulating vitamin 25(OH)D and fatty acids, as well as actin scavenging. In the pancreatic islets, the gene encoding GC, GC/Gc, is highly localized to glucagon-secreting α-cells. Despite this, the role of GC in α-cell function is poorly understood. We previously showed that GC is essential for α-cell morphology, electrical activity, and glucagon secretion. We now show that loss of GC exacerbates α-cell failure during metabolic stress. High-fat diet-fed GC-/- mice have basal hyperglucagonemia, which is associated with decreased α-cell size, impaired glucagon secretion and Ca2+ fluxes, and changes in glucose-dependent F-actin remodelling. Impairments in glucagon secretion can be rescued using exogenous GC to replenish α-cell GC levels, increase glucagon granule area, and restore the F-actin cytoskeleton. Lastly, GC levels decrease in α-cells of donors with type 2 diabetes, which is associated with changes in α-cell mass, morphology, and glucagon expression. Together, these data demonstrate an important role for GC in α-cell adaptation to metabolic stress.

Binding and sequestration of poison frog alkaloids by a plasma globulin.

Alkaloids are important bioactive molecules throughout the natural world, and in many animals they serve as a source of chemical defense against predation. Dendrobatid poison frogs bioaccumulate alkaloids from their diet to make themselves toxic or unpalatable to predators. Despite the proposed roles of plasma proteins as mediators of alkaloid trafficking and bioavailability, the responsible proteins have not been identified. We use chemical approaches to show that a ~50 kDa plasma protein is the principal alkaloid-binding molecule in blood of poison frogs. Proteomic and biochemical studies establish this plasma protein to be a liver-derived alkaloid-binding globulin (ABG) that is a member of the serine-protease inhibitor (serpin) family. In addition to alkaloid-binding activity, ABG sequesters and regulates the bioavailability of 'free' plasma alkaloids in vitro. Unexpectedly, ABG is not related to saxiphilin, albumin, or other known vitamin carriers, but instead exhibits sequence and structural homology to mammalian hormone carriers and amphibian biliverdin-binding proteins. ABG represents a new small molecule binding functionality in serpin proteins, a novel mechanism of plasma alkaloid transport in poison frogs, and more broadly points toward serpins acting as tunable scaffolds for small molecule binding and transport across different organisms.

In Silico Approach of Glycinin and Conglycinin Chains of Soybean By-Product (Okara) Using Papain and Bromelain.

This study explores utilization of a sustainable soybean by-product (okara) based on in silico approach. In silico approaches, as well as the BIOPEP database, PeptideRanker database, Peptide Calculator database (Pepcalc), ToxinPred database, and AllerTop database, were employed to evaluate the potential of glycinin and conglycinin derived peptides as a potential source of bioactive peptides. These major protein precursors have been found as protein in okara as a soybean by-product. Furthermore, primary structure, biological potential, and physicochemical, sensory, and allergenic characteristics of the theoretically released antioxidant peptides were predicted in this research. Glycinin and α subunits of ß-conglycinin were selected as potential precursors of bioactive peptides based on in silico analysis. The most notable among these are antioxidant peptides. First, the potential of protein precursors for releasing bioactive peptides was evaluated by determining the frequency of occurrence of fragments with a given activity. Through the BIOPEP database analysis, there are several antioxidant bioactive peptides in glycinin and ß and α subunits of ß-conglycinin sequences. Then, an in silico proteolysis using selected enzymes (papain, bromelain) to obtain antioxidant peptides was investigated and then analyzed using PeptideRanker and Pepcalc. Allergenic analysis using the AllerTop revealed that all in silico proteolysis-derived antioxidant peptides are probably nonallergenic peptides. We also performed molecular docking against MPO (myeloperoxidases) for this peptide. Overall, the present study highlights that glycinin and ß and α subunits of ß-conglycinin could be promising precursors of bioactive peptides that have an antioxidant peptide for developing several applications.

Impact of dietary inclusion of Chenopodium quinoa on growth performance and survival of Hubbard chicken.

The poultry sector is the most vibrant segment of the agriculture system plays a vital role in the supply of healthy meat products. Broiler production effectiveness is greatly associated with feed formulation. Although, broiler exhibits a relatively fast growth rate, the nutritional profile of its meat has been criticized under conventional human dietary regimes. In the current study, the dietary inclusion of quinoa was assessed to improve broiler growth performance, carcass quality, and health by analyzing different growth, hematological and biochemical, immunological parameters. In the present study, the chicken was fed with 50 g/kg, 100 g/kg, and 200 g/kg quinoa enriched diets in two different experimental groups during the growth phase or finisher phase while chicken fed with diet without quinoa were as control. The 50 g/kg quinoa supplemented chicken group revealed a substantial difference in growth performance in comparison with the control group. In addition, the examination of quinoa dietary supplementation on carcass quality exhibited variable behavior. Further, all the study groups fed with quinoa during the growth phase revealed no remarkable difference in the hematological profile in contrast to the control group except for the chicken group fed (50 g/Kg) during the finisher phase for hemoglobin levels. Likewise, all the quinoa enriched diet given chicken groups showed no significant difference in serum biochemical profile in contrast to the control group except for the 50 g/Kg quinoa fed chicken group during the finisher phase for total globulin levels. In addition, the examination of quinoa dietary supplementation on the broiler serum lipid profile was also assessed and birds exhibited variable behavior as the result of quinoa dietary supplementation. Evaluation of short-term immune response after quinoa supplementation assessed and birds exhibited no marked significance on expression outcomes of interleukin/cytokines (IL 1 beta, IL-6, IL-10) assessed by qRT-PCR analysis. In conclusion, the dietary supplementation of broiler fed with quinoa seeds can enhance the growth performance and the carcass quality of broiler.