Your browser doesn't support javascript.
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 590
Filtrar
1.
Adv Exp Med Biol ; 1155: 643-659, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31468437

RESUMO

Batillus cornutus (B. cornutus) is one of the gastropoda, which are distributed along the coast of China, Japan and South Korea and northeast area. In this study, we first identified the antioxidant effects of a B. cornutus meat (BM) enzymatic hydrolysate in H2O2-treated Vero cells. First of all, we prepared an Alcalase hydrolysate from BM (BMA) and revealed a high taurine content. Also, taurine rich BMA dose-dependently increased 2,2-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid (ABTS) radical scavenging activity, reducing power and the higher oxygen radical absorbance capacity (ORAC) value. In addition, BMA significantly increased the cell viability via the down-regulation of intracellular reactive oxygen species (ROS) production, as well as the decreased formation of apoptotic bodies and sub-G1 DNA population in H2O2-treated Vero cells. Furthermore, BMA increased the expression of the anti-apoptotic molecule, Bcl-2, and decreased the expressions of Bax, p53 and cleaved PARP, all of which are pro-apoptotic molecules, in H2O2-treated Vero cells. Based on these results, this study suggests that BMA may be used as a potential protector on damage caused by oxidative stress.


Assuntos
Antioxidantes/farmacologia , Gastrópodes/química , Estresse Oxidativo , Hidrolisados de Proteína/farmacologia , Animais , Cercopithecus aethiops , Peróxido de Hidrogênio , Carne , Espécies Reativas de Oxigênio/metabolismo , Subtilisinas , Células Vero
2.
Food Chem ; 299: 124985, 2019 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-31279127

RESUMO

Dietary protein peptides from quinoa yoghurt beverage (QYB) fermented with probiotic lactic acid bacteria strains play a protective role against diabetes and hypertension. In this study, the α-glucosidase and ACE inhibitory activities of germination-based protein hydrolysates of QYB were investigated. All protein hydrolysates exhibited a dose and strain-dependent inhibition on the enzymes. The inhibition of α-glucosidase was the highest in QLCSY13 (IC50 = 8.86 mg/mL), while ACE inhibition was the highest in QLCZ (IC50 = 0.03 mg/mL). Overall, QLCSY13 had the highest inhibitory activities, which was ascribed to its relatively higher amino acid contents and hydrophobicity. In addition, the ACE and α-glucosidase inhibitory activities of peptide fractions identified by RP-HPLC were 127 ±â€¯4.29 mg/mL and 10.39 ±â€¯4.73 mg/mL respectively. Among the potent inhibitory peptide sequences identified, both LAHMIVAGA and VAHPVF significantly had α-glucosidase and ACE inhibitory activities. Consequently, dietary protein peptides present in QYB had anti-hypertensive and anti-diabetic potentials.


Assuntos
Bebidas/microbiologia , Lactobacillus casei/metabolismo , Peptidil Dipeptidase A/metabolismo , Hidrolisados de Proteína/farmacologia , Iogurte/microbiologia , alfa-Glucosidases/metabolismo , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/química , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Fermentação , Inibidores de Glicosídeo Hidrolases/química , Inibidores de Glicosídeo Hidrolases/farmacologia , Fragmentos de Peptídeos/química , Fragmentos de Peptídeos/farmacologia , Hidrolisados de Proteína/química
3.
Food Chem ; 298: 124868, 2019 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-31260976

RESUMO

This work aimed to evaluate the efficacy of protein hydrolysates from bighead carp gill in inhibiting protein oxidation and quality loss in surimi. Firstly, antioxidant activity of hydrolysates in vitro was assessed, then 1%, 2% hydrolysates with better antioxidant activity and 4% sucrose were added to surimi respectively and stored at -18 °C for 4 months. Peptide sequences of above hydrolysates were also identified. The results suggested that hydrolysates of neutral protease had excellent 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging ability (42.93%) and Fe2+-chelating activity (73.27%). Compared with surimi without treatments, surimi with hydrolysates had higher sulfhydryl and salt-soluble protein concentrations, greater Ca2+-ATPase activity, lower disulfide bonds, carbonyls and hydrophobicity, as well as better gel strength and texture (p < 0.05). This study demonstrated that gill hydrolysate had antioxidant and dose-dependent cryoprotective effects on surimi that were comparable to the effects of sucrose, representing it as an alternative to sugar cryoprotectants in surimi industry.


Assuntos
Antioxidantes/farmacologia , Cyprinidae , Produtos Pesqueiros , Proteínas de Peixes/farmacologia , Hidrolisados de Proteína/farmacologia , Animais , Antioxidantes/química , Crioprotetores/química , Crioprotetores/farmacologia , Proteínas de Peixes/química , Congelamento , Brânquias/química , Interações Hidrofóbicas e Hidrofílicas , Oxirredução , Peptídeos/análise , Hidrolisados de Proteína/química , Compostos de Sulfidrila/química
4.
J Food Sci ; 84(5): 1170-1179, 2019 May.
Artigo em Inglês | MEDLINE | ID: mdl-30997940

RESUMO

High blood pressure can lead to cardiovascular diseases. The objective of this work was to obtain protein hydrolysates with antihypertensive potential from chia oil industry meal byproduct. Chia seed protein isolates (CPIs) were obtained from chia seed meal byproduct. CPI was hydrolyzed using different proteases (alcalase, pepsin, trypsin, and α-chymotrypsin) and their biological potential was evaluated using in vitro and in silico approaches. Chia seed pepsin protein hydrolysate showed the highest angiotensin-converting enzyme inhibition potential IC50 of 0.128 mg/mL (P < 0.05) compared to the rest of hydrolysates. Peptide sequence LIVSPLAGRL presented the lowest predicted binding energy and highest inhibition potential (-9.5 kcal/mol) compared to other sequenced peptides and positive controls (captopril and lisinopril). Chia peptides showed potential to block angiotensin-converting enzyme by interacting with its catalytic site. Chia seed oil industry meal byproduct could be used as an inexpensive source of protein and bioactive peptides with antihypertensive potential. PRACTICAL APPLICATION: This research shows an upcycling alternative for chia oil industry byproduct. Chia meal is a rich source of protein and can be used to generate bioactive peptides with antihypertensive potential. Chia protein isolate was obtained from chia meal and hydrolyzed using different enzymes, pepsin showed the highest antihypertensive potential. Chia meal waste could be a low-cost source of protein and protein hydrolysates that could be used as a food ingredient with antihypertensive potential.


Assuntos
Inibidores da Enzima Conversora de Angiotensina , Anti-Hipertensivos , Pepsina A , Peptidil Dipeptidase A , Proteínas de Plantas , Salvia/química , Inibidores da Enzima Conversora de Angiotensina/química , Inibidores da Enzima Conversora de Angiotensina/metabolismo , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Anti-Hipertensivos/química , Anti-Hipertensivos/metabolismo , Anti-Hipertensivos/farmacologia , Domínio Catalítico , Pepsina A/química , Pepsina A/metabolismo , Pepsina A/farmacologia , Peptidil Dipeptidase A/química , Peptidil Dipeptidase A/metabolismo , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Proteínas de Plantas/farmacologia , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Hidrolisados de Proteína/farmacologia
5.
Int J Mol Sci ; 20(6)2019 Mar 25.
Artigo em Inglês | MEDLINE | ID: mdl-30934634

RESUMO

In this study, we combined enzymatic hydrolysis and lactic acid fermentation to generate an antihypertensive product. Soybean protein isolates were first hydrolyzed by Prozyme and subsequently fermented with Lactobacillus rhamnosus EBD1. After fermentation, the in vitro angiotensin-converting enzyme (ACE) inhibitory activity of the product (P-SPI) increased from 60.8 ± 2.0% to 88.24 ± 3.2%, while captopril (a positive control) had an inhibitory activity of 94.20 ± 5.4%. Mass spectrometry revealed the presence of three potent and abundant ACE inhibitory peptides, PPNNNPASPSFSSSS, GPKALPII, and IIRCTGC in P-SPI. Hydrolyzing P-SPI with gastrointestinal proteases did not significantly affect its ACE inhibitory ability. Also, oral administration of P-SPI (200 mg/kg body weight) to spontaneous hypertensive rats (SHRs) for 6 weeks significantly lowered systolic blood pressure (-19 ± 4 mm Hg, p < 0.05) and controlled body weight gain relative to control SHRs that were fed with physiological saline. Overall, P-SPI could be used as an antihypertensive functional food.


Assuntos
Anti-Hipertensivos/farmacologia , Hidrolisados de Proteína/farmacologia , Proteínas de Soja/farmacologia , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Animais , Pressão Sanguínea/efeitos dos fármacos , Fermentação/efeitos dos fármacos , Trato Gastrointestinal/enzimologia , Coelhos , Suínos , Sístole/efeitos dos fármacos , Fatores de Tempo , Ganho de Peso/efeitos dos fármacos
6.
Mar Drugs ; 17(4)2019 Mar 27.
Artigo em Inglês | MEDLINE | ID: mdl-30934709

RESUMO

In this study, the antihypertensive activity of Purafect®-smooth hound viscera protein hydrolysate (VPH) and its peptide fraction with molecular weight (MW) below 1 kDa (VPH-I) was investigated. In addition, the lipase inhibitory activity, as well the anticoagulant potential, in vitro, were assessed. The antihypertensive effects of VPH and VPH-I were studied during 24 h (short-term effect) and 30 days (long-term effect) using high-salt (18% NaCl) and -fructose (10%) diet (HSFD)-induced hypertension. Data showed that, 4 h post-administration of VPH and VPH-I (200 mg/kg BW), the systolic blood pressure of rats was reduced by about 6 and 9 mmHg, respectively. These effects were similar to that obtained with Captopril (~9 mmHg at t = 4 h). On the other hand, exposing the rats to daily to HSFD, coupled to the administration of viscera peptides, was found to attenuate hypertension. In addition, the proteins' treatments were able to correct lipid and glycemic disorders, by reducing the total cholesterol and triglyceride contents and resorting to the plasma glucose level, compared to the HSFD group. Overall, the present findings demonstrated the preventive effect of VPH-peptides from hypertension complications, as a result of their biological properties.


Assuntos
Anti-Hipertensivos/farmacologia , Colesterol/metabolismo , Hipertensão/tratamento farmacológico , Hipertensão/prevenção & controle , Hidrolisados de Proteína/farmacologia , Animais , Glicemia/metabolismo , Pressão Sanguínea/efeitos dos fármacos , Dieta , Frutose/administração & dosagem , Metabolismo dos Lipídeos/efeitos dos fármacos , Masculino , Ratos , Ratos Wistar , Cloreto de Sódio/administração & dosagem
7.
Mar Drugs ; 17(4)2019 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-30935056

RESUMO

A protein extract was generated from the macroalga Ulva lactuca, which was subsequently hydrolysed using the food-grade enzyme papain and angiotensin-converting Enzyme I and renin inhibitory peptides identified using a combination of enrichment strategies employing molecular weight cutoff filtration and mass spectrometry analysis. The generated hydrolysates with the most promising in vitro activity were further purified using preparative RP-HPLC and characterised. The 1 kDa hydrolysate (1 kDa-UFH), purified and collected by preparative RP-HPLC at minutes 41‒44 (Fr41‒44), displayed statistically higher ACE-I inhibitory activities ranging from 96.91% to 98.06%. A total of 48 novel peptides were identified from these four fractions by LC-MS/MS. A simulated gastrointestinal digestion of the identified peptide sequences was carried out using in silico enzyme cleavage simulation tools, resulting in 86 peptide sequences that were further assessed for their potential activity, toxicity and allergenicity using multiple predictive approaches. All the peptides obtained in this study were predicted to be non-toxic. However, 28 out of the 86 novel peptides released after the in silico gastrointestinal digestion were identified as potential allergens. The potential allergenicity of these peptides should be further explored to comply with the current labelling regulations in formulated food products containing U. lactuca protein hydrolysates.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/metabolismo , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Oligopeptídeos/metabolismo , Oligopeptídeos/farmacologia , Hidrolisados de Proteína/farmacologia , Ulva/metabolismo , Alérgenos/farmacologia , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/química , Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Anti-Hipertensivos/farmacologia , Simulação por Computador , Humanos , Hidrólise , Oligopeptídeos/química , Oligopeptídeos/isolamento & purificação , Hidrolisados de Proteína/química , Hidrolisados de Proteína/isolamento & purificação , Alga Marinha/química , Ulva/química , Ulva/citologia
8.
J Sci Food Agric ; 99(11): 5112-5121, 2019 Aug 30.
Artigo em Inglês | MEDLINE | ID: mdl-30982967

RESUMO

BACKGROUND: Salmon bones, a waste by-product from the salmon industry, were used as a protein hydrolysate source for the production of bioactive peptides. The aim of this work was to evaluate the potential antioxidant and anti-inflammatory properties of salmon bone protein hydrolysate (SBPH). RESULTS: Salmon bones were hydrolyzed by separately using one of four proteases (Alcalase, Favourzyme, Neutrase and papain) at various concentrations (10, 25 and 50 mg mL-1 ), where the SBPH derived from 10 mg mL-1 papain hydrolysis exhibited the highest nitric oxide (NO) radical scavenging activity. After ultrafiltration, the MW < 0.65 kDa fraction showed the strongest NO inhibitory activity and was further fractionated by gel filtration chromatography (G1 and G2 fractions) and reverse-phase high-performance liquid chromatographic fractionation of the G1 fraction, from which the three main peaks (H1, H2 and H3) were found to have a marked NO-inhibitory activity and their peptide sequences were determined. Moreover, the G1 fraction was shown to inhibit both the lipopolysaccharide (LPS)-induced NO production and the LPS-induced inducible NO synthase , interleukin-6, tumor necrosis factor-α and induced NO production and the LPSCOX-2 mRNA levels in RAW 264.7 cells. CONCLUSIONS: Salmon bones from the salmon fisheries and farming industry were utilized by enzymatic hydrolysis for the production of valuable peptides. The results of this study suggested that bioactive peptides derived from salmon bones would be alternative anti-inflammation materials in functional resources. © 2019 Society of Chemical Industry.


Assuntos
Anti-Inflamatórios/farmacologia , Osso e Ossos/química , Proteínas de Peixes/química , Depuradores de Radicais Livres/farmacologia , Hidrolisados de Proteína/farmacologia , Salmão , Animais , Anti-Inflamatórios/química , Anti-Inflamatórios/isolamento & purificação , Biocatálise , Cromatografia em Gel , Cromatografia Líquida de Alta Pressão , Depuradores de Radicais Livres/química , Depuradores de Radicais Livres/isolamento & purificação , Hidrólise , Macrófagos/efeitos dos fármacos , Macrófagos/imunologia , Camundongos , Óxido Nítrico/imunologia , Óxido Nítrico Sintase Tipo II/genética , Óxido Nítrico Sintase Tipo II/imunologia , Peptídeo Hidrolases/química , Peptídeos/química , Peptídeos/isolamento & purificação , Peptídeos/farmacologia , Hidrolisados de Proteína/química , Células RAW 264.7
9.
Food Chem ; 289: 568-574, 2019 Aug 15.
Artigo em Inglês | MEDLINE | ID: mdl-30955650

RESUMO

In this work, a facile approach was developed to synthesized alcalase-inorganic hybrid nanocomposite (alcalase@CaHPO4) by immobilizing alcalase with calcium hydrogen phosphate (CaHPO4). The nanocomposite possessed flower-like morphological features with excellent hydrolysis activity on soybean protein isolates (SPI) with 1.57 fold higher compared to free alcalase. The experiment was evident of alcalase@CaHPO4 hybrid nanoflowers with 90% sustainability after the seven cycles of reusability and 80-100% relative activity at 50-70 °C and with 65% at pH 4 in acidic condition. Soybean protein hydrolysates (SPHs) produced by immobilized alcalase possessed 70% radical-scavenging capacity at 0.8 mg/mL concentration and 20% calcium-binding capacity at pH 6. The solubility of SPHs produced by alcalase@CaHPO4 hybrid nanoflowers was also improved by 15% compared to free alcalase. The high radical scavenging capability, good calcium binding capacity and improved solubility of SPHs prepared through alcalase@CaHPO4 hybrid nanoflowers would be highly promising in food industries.


Assuntos
Nanoestruturas/química , Hidrolisados de Proteína/química , Proteínas de Soja/isolamento & purificação , Subtilisinas/química , Cálcio/metabolismo , Fosfatos de Cálcio/química , Enzimas Imobilizadas/química , Depuradores de Radicais Livres/química , Depuradores de Radicais Livres/farmacologia , Concentração de Íons de Hidrogênio , Hidrólise , Hidrolisados de Proteína/farmacologia , Solubilidade , Proteínas de Soja/química , Soja/química
10.
Mar Drugs ; 17(3)2019 Feb 27.
Artigo em Inglês | MEDLINE | ID: mdl-30818811

RESUMO

The objective of this report was to investigate the isolation and recovery of different biocompounds and bioproducts from wastes (skins and heads) that were obtained from five species discarded by fishing fleets (megrim, hake, boarfish, grenadier, and Atlantic horse mackerel). Based on chemical treatments, enzymatic hydrolysis, and bacterial fermentation, we have isolated and produced gelatinous solutions, oils that are rich in omega-3, fish protein hydrolysates (FPHs) with antioxidant and antihypertensive activities, and peptones. FPHs showed degrees of hydrolysis higher than 13%, with soluble protein concentrations greater than 27 g/L and in vitro digestibilities superior to 90%. Additionally, amino acids compositions were always valuable and bioactivities were, in some cases, remarkable. Peptones that were obtained from FPHs of skin and the heads were demonstrated to be a viable alternative to expensive commercial ones indicated for the production of biomass, lactic acid, and pediocin SA-1 from Pediococcus acidilactici.


Assuntos
Produtos Biológicos/isolamento & purificação , Ácidos Graxos Ômega-3/isolamento & purificação , Peixes , Peptonas/isolamento & purificação , Hidrolisados de Proteína/isolamento & purificação , Animais , Anti-Hipertensivos/economia , Anti-Hipertensivos/isolamento & purificação , Anti-Hipertensivos/farmacologia , Antioxidantes/economia , Antioxidantes/isolamento & purificação , Antioxidantes/farmacologia , Bactérias/metabolismo , Produtos Biológicos/economia , Produtos Biológicos/farmacologia , Ácidos Graxos Ômega-3/economia , Ácidos Graxos Ômega-3/farmacologia , Fermentação , Pesqueiros/economia , Cabeça , Hidrólise , Peptonas/economia , Peptonas/farmacologia , Hidrolisados de Proteína/economia , Hidrolisados de Proteína/farmacologia , Pele/química , Espanha
11.
Mar Drugs ; 17(2)2019 Feb 25.
Artigo em Inglês | MEDLINE | ID: mdl-30823522

RESUMO

Enhanced oxidative stress plays a central role in promoting endothelial dysfunction, leading to the development of atherosclerosis. In this study, we investigated the protective effects of the hydrolysates derived from blue mussel (Mytilus edulis) against H2O2-mediated oxidative injury in human umbilical vein endothelial cells (HUVECs). The blue mussel hydrolysates were prepared by enzymatic hydrolysis with eight proteases, and blue mussel-α-chymotrypsin hydrolysate (BMCH) showed the highest antioxidant activities in DPPH radical scavenging, ABTS⁺ radical scavenging, and ORAC value compared to those of the other hydrolysates. BMCH also inhibited Cu2+-mediated low density lipoprotein (LDL) oxidation. Treatment of H2O2 resulted in the decreased HUVEC viability whereas pre-treatment with BMCH increased HUVEC viability and reduced reactive oxygen species (ROS) generation. BMCH pre-treatment increased cellular antioxidant capacities, including levels of glutathione (GSH), superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx) against H2O2-mediated oxidative stress in HUVECs. Flow cytometry and western blot analysis revealed that BMCH pre-treatment significantly reduced H2O2-mediated HUVEC apoptosis through inhibition of caspase-3 activation. Real-time-qPCR analysis showed that BMCH down-regulated expression of p53 and caspase-3 genes, as well as decreased the bax/bcl-2 ratio. Taken together, these results indicate that BMCH may be useful as functional food ingredients for protecting endothelial dysfunction or related disease.


Assuntos
Aminoácidos/química , Caspase 3/metabolismo , Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos , Mytilus edulis/química , Estresse Oxidativo/efeitos dos fármacos , Hidrolisados de Proteína/farmacologia , Aminoácidos/metabolismo , Aminoácidos/farmacologia , Animais , Antioxidantes/química , Antioxidantes/isolamento & purificação , Antioxidantes/farmacologia , Apoptose/efeitos dos fármacos , Ativação Enzimática/efeitos dos fármacos , Glutationa/metabolismo , Células Endoteliais da Veia Umbilical Humana/patologia , Humanos , Peróxido de Hidrogênio/administração & dosagem , Lipoproteínas LDL/metabolismo , Mytilus edulis/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/isolamento & purificação , Proteínas Proto-Oncogênicas c-bcl-2/metabolismo , RNA Mensageiro , Espécies Reativas de Oxigênio/metabolismo , Proteína Supressora de Tumor p53/metabolismo , Proteína X Associada a bcl-2/metabolismo
12.
Nutrients ; 11(4)2019 Mar 28.
Artigo em Inglês | MEDLINE | ID: mdl-30925798

RESUMO

The application of plant extracts for therapeutic purposes has been used in traditional medicine since the plants are a source of a great variety of chemical compounds that possess biological activity. Actually, the effect of these extracts on diseases such as cancer is being widely studied. Colorectal adenocarcinoma is one of the main causes of cancer related to death and the second most prevalent carcinoma in Western countries. The aim of this work is to study the possible effect of two fenugreek (Trigonella foenum graecum) protein hydrolysates on treatment and progression of colorectal cancer. Fenugreek proteins from seeds were hydrolysed by using two enzymes separately, which are named Purafect and Esperase, and were then tested on differentiated and undifferentiated human colonic adenocarcinoma Caco2/TC7 cells. Both hydrolysates did not affect the growth of differentiated cells, while they caused a decrease in undifferentiated cell proliferation by early apoptosis and cell cycle arrest in phase G1. This was triggered by a mitochondrial membrane permeabilization, cytochrome C release to cytoplasm, and caspase-3 activation. In addition, the hydrolysates of fenugreek proteins displayed antioxidant activity since they reduce the intracellular levels of ROS. These findings suggest that fenugreek protein hydrolysates could be used as nutraceutical molecules in colorectal cancer treatment.


Assuntos
Proliferação de Células/efeitos dos fármacos , Neoplasias do Colo/tratamento farmacológico , Suplementos Nutricionais , Proteínas de Plantas/química , Hidrolisados de Proteína/farmacologia , Trigonella/química , Apoptose/efeitos dos fármacos , Células CACO-2 , Caspase 3 , Neoplasias do Colo/metabolismo , Citocromos c , Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos , Humanos , Hidrolisados de Proteína/química , Espécies Reativas de Oxigênio , Tiorredoxina Redutase 1/genética , Tiorredoxina Redutase 1/metabolismo
13.
Food Chem ; 285: 266-274, 2019 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-30797344

RESUMO

The present study demonstrated the hydrolysis of peony seed protein isolate (PSPI) by using alcalase and resulted in the generation of an anti-oxidative peptide. In brief, a model was used to illustrate the enzymolysis of PSPI with the determination of kinetic factors as per investigation information. The model proved suitable to explain the PSPI hydrolysis by alcalase. A novel anti-oxidative peptide was obtained successfully by ultrafiltration and a series of chromatography techniques. Subsequently, a purified fragment was identified with the amino acid sequence of SMRKPPG followed by its synthesis and evaluation of its anti-oxidative activities. After hydrolysis, the peony seed protein hydrolysate (PSPH) with the degree of hydrolysis of 18% displayed the most significant antioxidant action which was further used to isolate the anti-oxidative peptide.


Assuntos
Antioxidantes/farmacologia , Paeonia/química , Peptídeos/isolamento & purificação , Hidrolisados de Proteína/farmacologia , Sementes/química , Sequência de Aminoácidos , Antioxidantes/química , Antioxidantes/isolamento & purificação , Hidrólise , Cinética , Modelos Teóricos , Peptídeos/química , Peptídeos/farmacologia , Proteínas de Plantas/química , Proteínas de Plantas/isolamento & purificação , Proteínas de Plantas/farmacologia , Hidrolisados de Proteína/análise , Subtilisinas/química , Subtilisinas/metabolismo , Ultrafiltração
14.
Food Chem ; 285: 290-295, 2019 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-30797347

RESUMO

Germination in the presence of selenium (Se) is an alternative to increase the healthy properties of seeds. This study aimed to compare the Se accumulation in different protein fractions from germinated chickpea (Cicer arietinum L.) and the effect on digestibility and cellular antioxidant activity (CAA) of protein hydrolysates. Chickpeas were germinated during four days after soaking with sodium selenite (0, 1, or 2 mg/100 g seeds). Total protein (TP) and glutelin (Glu), albumin (Alb) and globulin (Glo) fractions were digested and ultrafiltrated through a 10 kDa membrane. Se accumulated in the order of Glu > Alb > Glo. Ultrafiltrated Glu hydrolysate of four days germinated chickpeas treated with 2 mg Na2SeO3/100 g increased CAA (51.47%), demonstrating the potential health benefits of selenization. The intensity of vicilin bands (34-37 kDa) increased from the second to the fourth day compared with the control samples. Glo digestibility was higher in selenized chickpea sprouts.


Assuntos
Antioxidantes/farmacologia , Cicer/química , Proteínas de Plantas/farmacocinética , Hidrolisados de Proteína/farmacologia , Selenito de Sódio/farmacologia , Cicer/efeitos dos fármacos , Cicer/crescimento & desenvolvimento , Germinação/efeitos dos fármacos , Globulinas/metabolismo , Glutens/metabolismo , Glutens/farmacocinética , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Sementes/química , Sementes/efeitos dos fármacos , Sementes/crescimento & desenvolvimento , Selênio/análise
15.
Environ Sci Pollut Res Int ; 26(9): 8875-8884, 2019 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-30715703

RESUMO

Fish protein hydrolysates are digested form of protein with various bioactive properties where, the cleavages of molecular bonds of proteins can be broken by the enzymatic and chemical process. In this study, antioxidant properties of spray dried protein hydrolysate prepared from Pangasius viscera by using enzymatic (papain and pepsin), and chemical methods (hydrochloric acid and sodium hydroxide) were evaluated. Among the different treatments, pepsin-derived visceral protein hydrolysate showed the maximum antioxidant activity when used at higher concentrations. Essential amino acids (EAA) and hydrophobic amino acids are higher in papain-derived visceral protein hydrolysate. In pepsin-derived visceral protein hydrolysate, major proportion was contributed by glycine (Gly), glutamine (Glu), proline (Pro), and asparagine (Asp). Higher amount of aromatic amino acids are found in alkali-derived FVPH. Scanning electron microscopy (SEM) images of pepsin fish visceral protein hydrolysate showed better globular structure than the other treatments. It can be concluded that among the different treatments, the visceral protein hydrolysate prepared with pepsin had better overall quality regarding antioxidant properties and papain in nutritional point of view.


Assuntos
Antioxidantes/farmacologia , Peixes-Gato , Hidrolisados de Proteína/farmacologia , Animais , Antioxidantes/química , Antioxidantes/isolamento & purificação , Papaína/química , Pepsina A/farmacologia , Hidrolisados de Proteína/química , Hidrolisados de Proteína/isolamento & purificação , Alimentos Marinhos/análise
16.
Mar Drugs ; 17(2)2019 Feb 13.
Artigo em Inglês | MEDLINE | ID: mdl-30781881

RESUMO

Antioxidative peptides were produced from false abalone (Volutharpa ampullacea perryi) using enzymatic hydrolysis. Trypsin produced the most bioactive hydrolysates with the highest scavenging ABTS+• free radicals compared to pepsin, alcalase, neutrase, and flavourzyme. The response surface methodology studies on trypsin hydrolysis indicated that the hydrolysis temperature, time, and pH were interacted with each other (p < 0.05), and the optimal conditions were hydrolysis at 51.8 °C for 4.1 h, pH 7.7 and the maximum predicted hydrolysis degree was 13.18% and ABTS+• scavenging activity of 79.42%. The optimized hydrolysate was subjected to ultrafiltration fractionation, and the fraction with MW < 3 kDa showed the highest ABTS+• scavenging activity. There were 193 peptide sequences identified from this peptide fraction and 133 of them were successfully docked onto human myeloperoxidase (MPO), an enzyme involved in forming reactive oxidants in vivo. The highest scored peptide, no. 39, consists of DTETGVPT. Its structure and molecular interactions with MPO active site were compared with previously characterized peptide hLF1-11. The interactions between peptide no. 39 and MPO include electrostatic charge, hydrogen bonds, and covalent bonds. The antioxidative peptide produced in this research may exert antioxidant activity in vivo due to its potential inhibition effect on MPO.


Assuntos
Antioxidantes/farmacologia , Gastrópodes/química , Peptídeos/farmacologia , Hidrolisados de Proteína/farmacologia , Sequência de Aminoácidos , Animais , Antioxidantes/química , Antioxidantes/isolamento & purificação , Benzotiazóis/química , Domínio Catalítico/efeitos dos fármacos , Depuradores de Radicais Livres , Humanos , Ligações de Hidrogênio , Hidrólise , Modelos Moleculares , Simulação de Acoplamento Molecular , Peso Molecular , Peptídeos/química , Peptídeos/isolamento & purificação , Peroxidase/química , Hidrolisados de Proteína/química , Ácidos Sulfônicos/química
17.
Appl Microbiol Biotechnol ; 103(5): 2217-2228, 2019 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-30623204

RESUMO

Antimicrobial peptides (AMPs) have generated growing attention because of the increasing bacterial resistance. However, the discovery and identification of AMPs have proven to be challenging due to the complex purification procedure associated with conventional methods. For the reasons given above, it is necessary to explore more efficient ways to obtain AMPs. We established a new method for discovery and identification of novel AMPs by proteomics and bioinformatics from Zanthoxylum bungeanum Maxim seeds protein hydrolysate directly. This process was initially achieved by employing ultra-performance liquid chromatography-electrospray ionization-mass spectrometry/mass (UPLC-ESI-MS/MS) spectrometry to identify peptides derived from Z. bungeanum Maxim seed protein hydrolysates. Three online servers were introduced to predict potential AMPs. Sixteen potential AMPs ranging from 1.5 to 2.7 kDa were predicted and chemically synthesized, one of which, designated NP-6, inhibited activity against all the tested strains according to antimicrobial assay. Time-killing assay indicated that NP-6 could quickly kill almost all the Escherichia coli within 180 min and Staphylococcus aureus at 360 min. Moreover, the simulation 3D structure of NP-6 was consisted of α-helix and random coil, and this was verified by circular dichroism (CD) spectra. At last, the scanning electron microscope (SEM) images of E. coli and S. aureus treated by NP-6 demonstrated that NP-6 had a significant effect on bacteria cell morphology. Our findings provide an efficient approach for discovery of AMPs, and Z. bungeanum Maxim seeds may be a nature resource to extract antimicrobial agents.


Assuntos
Peptídeos Catiônicos Antimicrobianos/química , Peptídeos Catiônicos Antimicrobianos/farmacologia , Escherichia coli/efeitos dos fármacos , Sementes/química , Staphylococcus aureus/efeitos dos fármacos , Zanthoxylum/química , Cromatografia Líquida de Alta Pressão , Biologia Computacional/métodos , Descoberta de Drogas/métodos , Testes de Sensibilidade Microbiana , Hidrolisados de Proteína/análise , Hidrolisados de Proteína/farmacologia , Espectrometria de Massas por Ionização por Electrospray , Espectrometria de Massas em Tandem
18.
Mar Drugs ; 17(1)2019 Jan 06.
Artigo em Inglês | MEDLINE | ID: mdl-30621347

RESUMO

In the present study, peptide fractions of Cyclina sinensis hydrolysates, with molecular weight (MW) < 3 kDa and highest relative proliferation rate of murine macrophage cell line RAW 264.7, were purified by a series of chromatographic purification methods, to obtain peptide fractions with immunomodulatory activity. The amino acid sequence of the peptide was identified to be Arg-Val-Ala-Pro-Glu-Glu-His-Pro-Val-Glu-Gly-Arg-Tyr-Leu-Val (RVAPEEHPVEGRYLV) with MW of 1750.81 Da, and the novel pentadecapeptide (named SCSP) was synthesized for subsequent immunomodulatory activity experiments. Results showed the SCSP enhanced macrophage phagocytosis, increased productions of nitric oxide (NO), tumor necrosis factor-α (TNF-α), interleukin-6 (IL-6), and interleukin-1ß (IL-1ß), and up-regulated the protein level of inducible nitric oxide synthase (iNOS), nuclear factor κB (NF-κB), and NOD-like receptor protein 3 (NLRP3) in RAW 264.7 cells. Furthermore, the expression of inhibitor of nuclear factor κB-α (IκB-α) was down-regulated. These findings suggest that SCSP might stimulate macrophage activities by activating the NF-κB signaling pathway and can be used as a potential immunomodulatory agent in functional food or medicine.


Assuntos
Bivalves/química , Fatores Imunológicos/química , Fatores Imunológicos/farmacologia , Peptídeos/química , Peptídeos/farmacologia , Hidrolisados de Proteína/química , Hidrolisados de Proteína/farmacologia , Animais , Bivalves/metabolismo , Linhagem Celular , Regulação para Baixo/efeitos dos fármacos , Fatores Imunológicos/metabolismo , Interleucina-1beta/metabolismo , Interleucina-6/metabolismo , Macrófagos/efeitos dos fármacos , Macrófagos/metabolismo , Camundongos , Inibidor de NF-kappaB alfa/metabolismo , NF-kappa B/metabolismo , Proteína 3 que Contém Domínio de Pirina da Família NLR/metabolismo , Óxido Nítrico/metabolismo , Óxido Nítrico Sintase Tipo II/metabolismo , Peptídeos/metabolismo , Fagocitose/efeitos dos fármacos , Hidrolisados de Proteína/metabolismo , Células RAW 264.7 , Transdução de Sinais/efeitos dos fármacos , Fator de Necrose Tumoral alfa/metabolismo , Regulação para Cima/efeitos dos fármacos
19.
Food Chem ; 274: 848-856, 2019 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-30373019

RESUMO

Chia expeller is a by-product of the extrusion process of chia seeds generated during oil production. Typically, this material is non-utilized or used for non-valuable applications. In the present work, the chia expeller was hydrolysed with Papain and the antioxidant properties of the resultant peptides were evaluated. Papain treatment of the chia seed expeller demonstrated an enrichment of low molecular weight peptides (molecular weight <15 kDa) as determined by SDS-PAGE and MALDI-TOF/MS analyses. Such peptides showed a potent radical scavenging effect in vitro against 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) radicals in comparison with those non-hydrolysed samples. Taken together our results demonstrate the generation of functional peptides from the chia expeller by enzymatic hydrolysis with Papain. This value-added hydrolysate can be potentially included as a supplement in functional food and nutraceutical products.


Assuntos
Antioxidantes/farmacologia , Papaína/metabolismo , Peptídeos/farmacologia , Hidrolisados de Proteína/química , Salvia/química , Antioxidantes/química , Eletroforese em Gel de Poliacrilamida , Hidrólise , Peso Molecular , Papaína/química , Peptídeos/química , Hidrolisados de Proteína/farmacologia , Sementes/química , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
20.
J Food Sci ; 84(1): 73-79, 2019 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-30575032

RESUMO

Morchella esculenta protein hydrolysate (MPH) from a valued medicinal and edible fungus M. esculenta (L.) is an excellent material for functional food development. To promote MPH utilization, selenization of MPH was performed by applying a simple and environmentally friendly microwave irradiation procedure. The physicochemical characteristics of selenized MPH (Se-MPH) were investigated by SEM-EDX, FTIR, CD, and amino acid analyzer, and its biological activity were assessed by ABTS, DPPH, H2 O2 scavenging, and reducing power assays, as well as α-glucosidase, α-amylase, and tyrosinase inhibition tests. The results showed that MPH was successfully selenized, Se content in Se-MPH reached 59.0 ± 0.64 mg/g, and amino groups, hydroxyl groups, and sulfur atoms of methionine residues in the MPH molecule may participate in selenization. Furthermore, Se-MPH exhibited significantly enhanced antioxidant, antidiabetic, and tyrosinase inhibitory activities, compared with the native MPH and microwave-irradiated MPH. Thus, the microwave-assisted selenization is a feasible strategy for preparing organic Se and improving the biological activity of MPH. PRACTICAL APPLICATION: In this study, selenized Morchella esculenta protein hydrolysate (Se-MPH) was successfully prepared via conjugation with sodium selenite using the microwave-assisted method. The results showed that Se-MPH, synthesized with the aid of microwave, exhibited favorable selenium content and improved antioxidant, antidiabetic, and tyrosinase inhibitory activities. Therefore, microwave can be employed as an innovative and effective avenue for the production of organic selenium in nutraceutical and functional food industry.


Assuntos
Ascomicetos/metabolismo , Hidrolisados de Proteína/farmacologia , Selênio/metabolismo , Antioxidantes/farmacologia , Manipulação de Alimentos , Hipoglicemiantes/farmacologia , Micro-Ondas , Monofenol Mono-Oxigenase/antagonistas & inibidores , Monofenol Mono-Oxigenase/metabolismo , Selenito de Sódio/metabolismo
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA