Development of a Soy Protein Hydrolysate with an Antihypertensive Effect.
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ABSTRACT:
SUBMITTER: Daliri EB
PROVIDER: S-EPMC6470933 | biostudies-literature |
REPOSITORIES: biostudies-literature
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Project description:Fish skin, a by-product from fish processing industries, still contains a significant amount of protein-rich material. Gelatin was extracted from Nile tilapia skin with the yield 20.77?±?0.80 % wet weight. Gelatin was then separately hydrolyzed by proteases, including bromelain, papain, trypsin, flavourzyme, alcalase and neutrase. Low molecular weight gelatin hydrolysate (<10 kDa) has a great potential as an antioxidant agent. Flavourzyme hydrolysate has potent activity on ABTS radical scavenging (1,413.61?±?88.74 ?g trolox/mg protein) and also inhibits the oxidation of linoleic acid at a high level (59.74?±?16.57 % inhibition). The greatest reducing power is in alcalase hydrolysate (4.951?±?1.577 mM trolox/mg protein). While, bromelain hydrolysate has the highest ferrous ion chelating activity (86.895?±?0.061 %). Evaluation of the angiotensin-I-converting enzyme's inhibitory activity indicates that all hydrolysates have great potency as an antihypertensive agent. All studied tilapia skin gelatin hydrolysates contain potent antioxidant and anti-hypertensive effects.
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Project description:Spent hens are a major byproduct of the egg industry but are rich in muscle proteins that can be enzymatically transformed into bioactive peptides. The present study aimed to develop a spent hen muscle protein hydrolysate (SPH) with antihypertensive activity. Spent hen muscle proteins were hydrolyzed by nine enzymes, either individually or in combination; 18 SPHs were assessed initially for their in vitro angiotensin-converting enzyme (ACE) inhibitory activity, and three SPHs, prepared by Protex 26L (SPH-26L), pepsin (SPH-P), and thermoase (SPH-T), showed promising activity and peptide yield. These three hydrolysates were further assessed for their angiotensin-converting enzyme 2 (ACE2) upregulating, antioxidant, and anti-inflammatory activities; only SPH-T upregulated ACE2 expression, while all three SPHs showed antioxidant and anti-inflammatory activities. During simulated gastrointestinal digestion, ACE2 upregulating, ACE inhibitory and antioxidant activities of SPH-T were not affected, but those of SPH-26L and SPH-P were reduced. ACE inhibitory activity of gastrointestinal-digested SPH-T was not affected after the permeability study in Caco-2 cells, while ACE2 upregulating, antioxidant and anti-inflammatory activities were improved; nine novel peptides with five-eight amino acid residues were identified from the Caco-2 permeate. Among these three hydrolysates, only SPH-T reduced blood pressure significantly when given orally at a daily dose of 1000 mg/kg body weight to spontaneously hypertensive rats. SPH-T can be developed into a promising functional food ingredient against hypertension, contributing to a more sustainable utilization for spent hens while generating extra revenue for the egg industry.
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Project description:BackgroundProteases are important for hydrolysis of proteins to generate peptides with many bioactivities. Thus, the development of novel proteases with high activities is meaningful to discover bioactive peptides. Because natural isolation from animal, plant and microbial sources is impractical to produce large quantities of proteases, gene cloning and expression of target protease are preferred.ResultsIn this study, an alkaline serine protease gene (GsProS8) from Geobacillus stearothermophilus was successfully cloned and expressed in Bacillus subtilis. The recombinant GsProS8 was produced with high protease activity of 3807?U/mL after high cell density fermentation. GsProS8 was then purified through ammonium sulfate precipitation and a two-step chromatographic method to obtain the homogeneous protease. The molecular mass of GsProS8 was estimated to be 27.2?kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and 28.3?kDa by gel filtration. The optimal activity of GsProS8 was found to be pH?8.5 and 50?°C, respectively. The protease exhibited a broad substrate specificity and different kinetic parameters to casein and whey protein. Furthermore, the hydrolysis of whey protein using GsProS8 resulted in a large amount of peptides with high angiotensin-I-converting enzyme (ACE) inhibitory activity (IC50 of 0.129?mg/mL).ConclusionsGsProS8 could be a potential candidate for industrial applications, especially the preparation of antihypertensive peptides.
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Project description:This study presents the state-of-art research about the assembly of soy proteins in nanocarriers, liposomes, and its design includes different physicochemical strategies and approaches: two-step enzymatic hydrolysis of soy concentrate, hydrolysate encapsulation by using phospholipids and cholesterol, and application of ultrasonication. Achieved results revealed that ultrasonication, together with cholesterol addition into phospholipid layers, improved the stability of nanoliposomes, and a maximum EE value of 60.5 % was obtained. Average size of peptide-loaded nanoliposomes was found to be from 191.1 to 286.7 nm, with a ζ potential of -25.5 to -34.6 mV, and a polydispersity index of 0.250-0.390. Ultrasound-assisted encapsulation process did not lead to a decrease in the antioxidant activity of the trapped peptides. FTIR has indicated an effective hydrophobic interaction between phosphatidylcholine and hydrolysate peptides. TEM and SEM have confirmed the spherical nanocarrier structure and unilamelarity. Prolonged gastrointestinal release and stability of peptides have been enabled by liposome nanocarriers.
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Project description:This study was to develop novel soy protein isolate-based films for packaging using halloysite nanotubes (HNTs), poly-vinyl alcohol (PVA), and 1,2,3-propanetriol-diglycidyl-ether (PTGE). The structural, crystallinity, opacity, micromorphology, and thermal stability of the resultant SPI/HNTs/PVA/PTGE film were analyzed by the Attenuated total reflectance-Fourier transformed infrared (ATR-FTIR) spectroscopy, X-ray diffraction (XRD), UV-Vis spectrophotometry, scanning electron microscopy (SEM), and thermo-gravimetric analysis (TGA). The SPI/HNTs/PVA/PTGE film illustrated that HNTs were uniformly dispersed in the SPI matrix and the thermal stability of the film was enhanced. Furthermore, the tensile strength (TS) of the SPI/HNTs/PVA/PTGE film was increased by 329.3% and the elongation at the break (EB) remained unchanged. The water absorption (WA) and the moisture content (MC) were decreased by 5.1% and 10.4%, respectively, compared to the unmodified film. The results highlighted the synergistic effects of SPI, HNTs, PVA, and PTGE on the mechanical properties, water resistance, and thermal stability of SPI films, which showed excellent strength and flexibility. In short, SPI films prepared from HNTs, PVA, and PTGE showed considerable potential as packaging materials.
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Project description:Soybeans (Glycine max) are an excellent source of dietary proteins and peptides with potential biological activities, such as antihypertensive, anti-cholesterol, and antioxidant activity; moreover, they could prevent cancer. Also, soy contains all the essential amino acids for nutrition; therefore, it represents an alternative to animal proteins. The goal of this paper was the comprehensive characterization of medium-sized and short peptides (two to four amino acids) obtained from simulated gastrointestinal digestion. Two different analytical approaches were employed for peptide characterization, namely a common peptidomic analysis for medium-sized peptides and a suspect screening analysis for short peptides, employing an inclusion list of exact m/z values of all possible amino acid combinations. Moreover, fractionation by preparative reversed-phase liquid chromatography was employed to simplify the starting protein hydrolysate. Six fractions were collected and tested for antioxidative activity by an innovative antioxidant assay on human gastric adenocarcinoma AGS cell lines. The two most active fractions (2 and 3) were then characterized by a peptidomic approach and database search, as well as by a suspect screening approach, in order to identify potential antioxidant amino acid sequences. Some of the peptides identified in these two fractions have been already reported in the literature for their antioxidant activity.
| S-EPMC8148578 | biostudies-literature
Project description:Little research has focused on infant developmental effects, other than growth, of formulas that differ substantially in the form of protein. To examine development of infants fed formulas differing in free amino acid content, we randomized 0.5-month-old infants (n = 79) to either a control group who fed only cow milk formula (CMF) during the first 8 months (CMF8), or to one of two experimental groups: one experimental group fed extensively protein hydrolyzed formula (EHF) for 1-3 months during first 4.5 months (EHF1-3) of life, and the other fed EHF for 8 months (EHF8). The Mullen Scales of Early Learning were administered monthly from 1.5 to 8.5 months to assess fine (FM) and gross (GM) motor control, receptive (RL) and expressive (EL) language, visual reception (VR), and an early learning composite (ELC). Across the 5.5-8.5-month time period, when compared to CMF8 infants, GM scores in EHF1-3 infants averaged 1.5 points higher (95 % CI 0.1, 3.0) and in EHF8 infants 2.2 points higher (95 % CI 0.3, 4.0). Similarly, VR scores averaged 1.9 points higher (95 % CI 0.1, 3.8) in EHF1-3 infants and 2.2 points higher (95 % CI -0.2, 4.5) in EHF8 infants. EHF8 infants' RL scores averaged 1.8 points lower (95 % CI 0.1, 3.6) than CMF8 infants. These data suggest that the form of protein in infant formula may impact cognitive development and that the higher free amino acid content in breast milk may be a contributing factor to the differential cognitive development between breastfed and CMF-fed infants.clinicaltrials.gov NCT00994747.
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Project description:There are concerns regarding possible reproductive toxicity from consumption of soy including an increased risk of endometriosis and endometrial cancer. We used global uterine gene expression profiles in adult ovariectomized (OVX) female rats assessed by RNAseq to examine the estrogenicity of soy protein isolate (SPI) and the potential for feeding SPI to alter estrogen signaling in the uterus. Rats were fed AIN93G diets made with casein (CAS) or SPI from postnatal day (PND) 30. Rats were OVX on PND 50 and infused with 17 beta-estradiol (E2) or vehicle. E2 increased uterine wet weight (P<0.05) and significantly altered expression of 2084 uterine genes. In contrast, SPI feeding had no effect on uterine weight and only altered expression of 177 genes. Overlap between E2 and SPI genes was limited to 69 genes (3%). GO analysis indicated significant differences in uterine biological processes affected by E2 and SPI and little evidence for recruitment of ER alpha to the promoters of ER-responsive genes after SPI feeding. The major E2 up-regulated uterine pathways were cancer pathways and extracellular organization. SPI feeding up-regulated uterine PPAR signaling and fatty acid metabolism. The combination of E2 and SPI feeding resulted in significant regulation of 715 fewer genes relative to E2 alone. In a separate experiment, the combination of E2 and SPI reversed the ability of E2 to induce uterine proliferation in response to the carcinogen dimethybenz(a)anthracene (DMBA). These data suggest SPI does not act as a weak estrogen in the uterus but appears to be a selective estrogen receptor modulator (SERM) interacting with a small sub-set of E2-regulated genes and to be anti-estrogenic in the presence of endogenous estrogens.
2015-06-13 | GSE69819 | GEO
Project description:The linkage between nutrition and cancer prevention is an intriguing concept that is gaining widespread support based on epidemiological and animal studies. Multiple mechanisms likely underlie dietary protection against cancer, with effects influenced by target tissue response, cell-cell interactions and developmental context. Given the negative correlation between breast cancer incidence and intake of soy foods by Asian women, and the increasing consumption of soy protein-based formula by infants in the Western world, we have studied soy protein isolate (SPI) used in most infant formula as a paradigm to evaluate diet as a risk factor in a rodent model of mammary cancer. We previously demonstrated that lifetime exposure to dietary SPI reduced the incidence of N-methyl-N-nitrosourea-induced mammary tumors in young adult rats relative to those fed the control diet Casein (CAS). This protection was associated with increased tumor suppressor PTEN and decreased Wnt signaling component expression in mammary epithelial cells at postnatal day (PND) 50 prior to carcinogen insult. To identify early events contributing to mammary tumor suppression by diet, we used Affymetrix RAE230A GeneChips containing 14280 probe sets and the GeneSpring Robust Multi-array program to analyze genomic profiles of mammary glands of prepubertal (PND21) rats lifetime exposed to SPI or CAS. Experiment Overall Design: Female SD rats are exposed to either casein/soy protein isolate based AIN-93G diet since gestation day 4 till weaning. Whole mammary gland were harvested for the gene analysis by microarray.
2009-08-07 | E-GEOD-12217 | biostudies-arrayexpress
Project description:There are concerns regarding possible reproductive toxicity from consumption of soy including an increased risk of endometriosis and endometrial cancer. We used global uterine gene expression profiles in adult ovariectomized (OVX) female rats assessed by RNAseq to examine the estrogenicity of soy protein isolate (SPI) and the potential for feeding SPI to alter estrogen signaling in the uterus. Rats were fed AIN93G diets made with casein (CAS) or SPI from postnatal day (PND) 30. Rats were OVX on PND 50 and infused with 17 beta-estradiol (E2) or vehicle. E2 increased uterine wet weight (P<0.05) and significantly altered expression of 2084 uterine genes. In contrast, SPI feeding had no effect on uterine weight and only altered expression of 177 genes. Overlap between E2 and SPI genes was limited to 69 genes (3%). GO analysis indicated significant differences in uterine biological processes affected by E2 and SPI and little evidence for recruitment of ER alpha to the promoters of ER-responsive genes after SPI feeding. The major E2 up-regulated uterine pathways were cancer pathways and extracellular organization. SPI feeding up-regulated uterine PPAR signaling and fatty acid metabolism. The combination of E2 and SPI feeding resulted in significant regulation of 715 fewer genes relative to E2 alone. In a separate experiment, the combination of E2 and SPI reversed the ability of E2 to induce uterine proliferation in response to the carcinogen dimethybenz(a)anthracene (DMBA). These data suggest SPI does not act as a weak estrogen in the uterus but appears to be a selective estrogen receptor modulator (SERM) interacting with a small sub-set of E2-regulated genes and to be anti-estrogenic in the presence of endogenous estrogens. Rat uterus mRNA of ovariectomized adult female rats subject to four different diets (Caseine, Caseine + E2, Soy and Soy+E2 ) were sequenced, in triplicate, in an Illumina GAIIx sequencer.
2015-06-13 | E-GEOD-69819 | biostudies-arrayexpress