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1.
Food Chem ; 345: 128783, 2021 May 30.
Artigo em Inglês | MEDLINE | ID: mdl-33316714

RESUMO

Egg is the second most common food allergen among infants and young children. This work investigated the influence of plastein reaction on immunoglobulin E (IgE)-binding activities of egg white protein hydrolysates after simulated gastrointestinal (GIT) digestion. Compared to hydrolysate precursors, the IgE-binding activity of Pepsin-Plastein significantly decreased from 35 ± 7% to 8 ± 2% (P < 0.05), and Papain-Plastein from 70 ± 5% to 59 ± 4%. Further GIT hydrolysis of Pepsin-Plastein maintained the reduced IgE-binding activity (7 ± 3%) whereas Papain-Plastein digestion restored the IgE-binding reactivity to 66 ± 7%. This discrepancy is related to the different mechanisms of plastein formation. Covalent modifications (decreased free amino nitrogen and sulfhydryl contents) provided biostability for Pepsin-Plastein, whereas hydrophobic interactions (increased surface hydrophobicity) mainly contributed to Papain-Plastein formation. The latter can be destroyed during GIT digestion leading to re-exposure of hidden IgE-binding epitopes. Taken together, plastein reaction is a promising strategy for inducing structural modifications that reduce the immune reactivity of allergenic proteins.


Assuntos
Digestão , Proteínas do Ovo/metabolismo , Imunoglobulina E/metabolismo , Hidrolisados de Proteína/metabolismo , Alérgenos/metabolismo , Criança , Pré-Escolar , Hipersensibilidade Alimentar , Humanos , Interações Hidrofóbicas e Hidrofílicas , Pepsina A/metabolismo , Ligação Proteica
2.
Food Chem ; 334: 127475, 2021 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-32688176

RESUMO

Although numerous types of organisms have been used to enrich selenium, a low-cost and efficient organism is yet to be identified. This study aimed to develop a new means of selenium enrichment using Tenebrio molitor larvae. Our results indicated that the total selenium content in larvae was increased 83-fold to 54.21 ± 1.25 µg/g, and of this content, organic selenium accounted for over 97% after feeding the larvae with 20 µg/g of sodium selenite. Selenium was distributed unequally in the protein fraction with following order: alkali-soluble protein-bound selenium (36.32%) > salt-soluble protein-bound selenium (19.41%) > water-soluble protein-bound selenium (17.03%) > alcohol-soluble protein-bound selenium (3.21%). Additionally, 81% of the selenium within the soluble proteins was distributed in subunits possessing molecular weights of <40 kDa. After hydrolysis by alcalase, the protein hydrolysate of selenium-enriched larvae possessing 75% selenium recovery exhibited stronger antioxidant and immunoregulatory activities than those of regular larvae.


Assuntos
Antioxidantes/farmacologia , Fatores Imunológicos/farmacologia , Proteínas de Insetos/metabolismo , Hidrolisados de Proteína/farmacologia , Selênio/farmacocinética , Tenebrio/metabolismo , Adulto , Aminoácidos/análise , Aminoácidos/metabolismo , Animais , Antioxidantes/metabolismo , Eritrócitos/efeitos dos fármacos , Hemólise/efeitos dos fármacos , Humanos , Hidrólise , Fatores Imunológicos/metabolismo , Proteínas de Insetos/farmacologia , Larva/efeitos dos fármacos , Larva/metabolismo , Camundongos , Hidrolisados de Proteína/metabolismo , Células RAW 264.7 , Selênio/análise , Subtilisinas/química , Subtilisinas/metabolismo , Tenebrio/efeitos dos fármacos
3.
Food Chem ; 331: 127353, 2020 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-32580127

RESUMO

Aroma defects limit the application of fish protein hydrolysates as flavourings. This study aimed to develop a flavour concentrate from fermented tilapia fish head hydrolysate bymaximising the Maillard reaction production of meaty and roasted aroma associated compounds. We studied the optimal conditions of the Maillard reaction of xylose with cysteine to form meat-like odorants using response surface methodology. A 3-factored and 3-leveled Box Behnken design was employed, where the independent variables were cysteine concentration (A, w/v, %), heating temperature (B, °C) and heating time (C, min). 2-Methyl-3-furanthiol and 2-furfurylthiol were used as response factors. The optimal conditions were obtained as follows: A, 0.80%; B, 183.80 °C; C, 89.34 min. Compared with the controls, Maillard reaction products enriched the meaty and roasted aroma associated compounds in the treated hydrolysate. In conclusion, the treated tilapia fish head hydrolysate may be used as a base in development of new fish-based flavourings.


Assuntos
Cisteína/química , Aromatizantes/química , Reação de Maillard , Odorantes , Tilápia/metabolismo , Xilose/química , Animais , Fermentação , Alimentos e Bebidas Fermentados , Produtos Pesqueiros/microbiologia , Proteínas de Peixes da Dieta/química , Furanos/química , Cabeça , Hidrolisados de Proteína/metabolismo , Compostos de Sulfidrila/química , Paladar , Temperatura
4.
Food Chem ; 330: 127120, 2020 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-32526646

RESUMO

Enzymatic hydrolysis of plant-derived proteins can improve their quality by offering opportunities for food applications. In this study, three proteolytic enzymes (pepsin, trypsin, Alcalase®) were used, alone or combined, to produce faba bean protein hydrolysates (PHs). Their functional, nutritional and antioxidant properties were evaluated, and the peptidomic profile was assessed by LC-MS/MS. Hydrolysis improved solubility of faba proteins at acidic and neutral pH, and their antioxidant properties. Peptidomic analysis identified 2031 peptides in the different PHs. Among them, 9 showed 100% homology with previously known antioxidant peptides and several others had antioxidant motifs in their sequences. Sensory data analysis showed that after addition of PHs to apple juice, no significant differences were perceived between control and some of the PHs. This study demonstrates that enzymatic hydrolysis enhances the functional and antioxidant properties of faba bean proteins. Specifically, hydrolysates can be used as functional food ingredients to produce fortified beverages.


Assuntos
Antioxidantes/química , Sucos de Frutas e Vegetais/análise , Malus/química , Proteínas de Plantas/química , Hidrolisados de Proteína/química , Vicia faba/química , Cromatografia Líquida , Hidrólise , Malus/metabolismo , Proteínas de Plantas/metabolismo , Hidrolisados de Proteína/metabolismo , Sementes/química , Sementes/metabolismo , Vicia faba/metabolismo
5.
Food Chem ; 319: 126563, 2020 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-32172048

RESUMO

Enzymatic hydrolysis of proteins produces bioactive peptides that have the potential to provide health benefits. This study examined the inflammatory- and immune-modulating properties of a flavourzyme-derived sunflower protein hydrolysate (SPH) and peptides. The SPH was fractionated into <1, 1-3, 3-5, and >5 kDa peptides by membrane ultrafiltration. The SPH blunted IL-1ß stimulated NFκB activation and boosted IL-4/GM-CSF induced expression of surface markers CD14 and CD86, indicating maturation into a dendritic cell (DC) phenotype. Testing of SPH membrane ultrafiltration and HPLC fractions indicated that smaller and non-polar peptides were the most potent, respectively. Four novel peptides (YFVP, SGRDP, MVWGP and TGSYTEGWS) were identified and all of them blunted IL-1ß stimulated NFκB activation. The peptides also boosted IL-4/GM-CSF induction of CD14, while only MVWGP and TGSYTEGWS boosted the expression of CD86. MVWGP was the most potent immune-modulatory peptide across all cellular assays, which was attributed to the presence of a methionine residue.


Assuntos
Diferenciação Celular/efeitos dos fármacos , Células Dendríticas/efeitos dos fármacos , Helianthus/metabolismo , Monócitos/efeitos dos fármacos , NF-kappa B/antagonistas & inibidores , Peptídeos/farmacologia , Hidrolisados de Proteína/farmacologia , Linhagem Celular Tumoral , Células Dendríticas/citologia , Células Dendríticas/metabolismo , Humanos , Monócitos/citologia , Monócitos/metabolismo , NF-kappa B/metabolismo , Peptídeos/metabolismo , Hidrolisados de Proteína/metabolismo
6.
Food Chem ; 320: 126654, 2020 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-32222661

RESUMO

Plastein is defined as a protease-induced peptide aggregate and has been explored for over a century. This study investigated the effects of Alcalase and papain on plastein formation in protein hydrolysates of porcine hemoglobin and meat by measuring turbidity, particle size distribution, free amino groups and chemical interactions, as well as identifying the soluble peptides remaining in solution by LC-MS/MS. The results showed that Alcalase induced more peptide aggregation than papain in terms of increases in turbidity and particle size. Porcine hemoglobin was better than meat in inducing plastein formation in a short reaction time. Besides, covalent bonds involving peptide bonds and disulfide bonds were not crucial in the plastein reaction, instead a high proportion of hydrophobic interactions dominated the plastein. Not all peptides of both hydrolysates took part in plastein formation, and the regions of sequence that were prone to aggregation were visualized by Peptigram.


Assuntos
Hemoglobinas/metabolismo , Papaína/metabolismo , Hidrolisados de Proteína/metabolismo , Subtilisinas/metabolismo , Animais , Cromatografia Líquida , Interações Hidrofóbicas e Hidrofílicas , Carne , Papaína/química , Tamanho da Partícula , Peptídeos/química , Peptídeos/metabolismo , Hidrolisados de Proteína/química , Subtilisinas/química , Suínos , Espectrometria de Massas em Tandem
7.
Food Chem ; 319: 126540, 2020 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-32151899

RESUMO

SeMet-Pro-Ser (Se-MPS) is an antioxidant selenopeptide derived from selenized brown rice protein hydrolysates. In this study, the stability of glutathione (GSH), Met-Pro-Ser (MPS), and Se-MPS under different processing conditions, namely, temperature, pH, NaCl, citric acid, light, and gastrointestinal proteases, were evaluated by measuring ABTS+ scavenging and Cr(VI) reduction capacities. The ABTS+ scavenging capacity of GSH under thermal treatment, high salt density, and long-term storage was significantly decreased, while its Cr(VI) reduction activity was relatively stable. No significant change of Se-MPS antioxidant activity was observed under different conditions, except under citric acid. Meanwhile, its Cr(VI) reduction activity was partially or mostly retained under different treatment conditions. However, it displayed negligible ABTS+ scavenging capacity. Se-MPS was superior to GSH and MPS in terms of stability and antioxidant activity and could be a candidate for development of nutraceuticals or functional food.


Assuntos
Antioxidantes/química , Dipeptídeos/química , Oryza/enzimologia , Peptídeos/química , Hidrolisados de Proteína/metabolismo , Antioxidantes/metabolismo , Dipeptídeos/metabolismo , Glutationa/química , Oryza/química , Peptídeos/metabolismo
8.
Int J Mol Sci ; 21(3)2020 Feb 05.
Artigo em Inglês | MEDLINE | ID: mdl-32033479

RESUMO

The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 µM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.


Assuntos
Digestão/fisiologia , Trato Gastrointestinal/metabolismo , Peptidil Dipeptidase A/metabolismo , Sesamum/metabolismo , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Animais , Quimotripsina/metabolismo , Digestão/efeitos dos fármacos , Trato Gastrointestinal/efeitos dos fármacos , Hidrólise/efeitos dos fármacos , Simulação de Acoplamento Molecular/métodos , Pepsina A/metabolismo , Peptídeos/metabolismo , Hidrolisados de Proteína/metabolismo , Coelhos , Tripsina/metabolismo
9.
Food Chem ; 312: 126035, 2020 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-31901822

RESUMO

In this study, we investigated the ability of Enterococcus faecalis 2/28, isolated from artisan cheese, to release biopeptides from whey proteins. We used an in silico approach for predicting the bioactivities of peptides generated by E. faecalis. The results of the in vitro study showed that the whey protein hydrolysates (WPHs) obtained had angiotensin-I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities, with inhibition of ACE being stronger than that of DPP-IV. To identify peptides that may be potential inhibitors of ACE, WPH with the highest ACE inhibitory activity was analysed using Sephadex G-75 gel filtration chromatography, Superdex peptide 10/300 GL size exclusion chromatography, and liquid chromatography-electrospray ionisation tandem mass spectrometry (LC-ESI-MS/MS). Among the identified peptides were ACE-inhibitory peptides (LDAQSAPLR, LKGYGGVSLPEW, and LKALPMH), antimicrobial peptides (AASDISLLDAQSAPLR, IIAEKTKIPAVF, IDALNENK, and VLVLDTDYK), DPP-IV-inhibitory peptides (LKALPMH, LKPTPEGDLEIL, LKGYGGVSLPE, LKPTPEGDLE, ILDKVGINY, and VLVLDTDYK), proliferation stimulating peptide (IDALNENK), and cytotoxic peptide (LIVTQTMK).


Assuntos
Enterococcus faecalis/enzimologia , Lactobacillales/enzimologia , Proteínas do Soro do Leite/metabolismo , Soro do Leite/metabolismo , Animais , Bovinos , Dipeptidil Peptidase 4/metabolismo , Hidrólise , Peptidil Dipeptidase A/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Proteólise , Espectrometria de Massas em Tandem , Soro do Leite/química , Proteínas do Soro do Leite/química
10.
Fish Shellfish Immunol ; 98: 10-18, 2020 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31911287

RESUMO

Two in vitro trials were conducted to identify a peptide with antioxidant activity and immunoenhancement from cottonseed meal protein hydrolysate (CPH) for fish. Primary hepatocytes of Megalobrama amblycephala were treated with CPH. In experiment 1, CPH significantly increased aspartate aminotransferase (GOT), alanine aminotransferase (GPT), total superoxide dismutase (t-SOD), catalase (CAT), and lysozyme activities, as well as up-regulated SOD, CAT, antimicrobial peptides 1 (Leap 1) and Leap 2 mRNA levels (p < 0.05). However, CPH significantly down-regulated the expression of NADPH oxidase-2 (NOX2), Kelch-like-ECH-associated protein 1 (Keap1), NF-E2-related factor 2 (Nrf2) and BTB and CNC homolog 1 (Bach1) mRNA (p < 0.05) in fish hepatocytes. Experiment 2 showed that the molecular mass of CPH was distributed mainly in the 700-1024 Da range. Peptide 1 (P1) and P2 significantly decreased GOT and GPT activities in conditioned medium (p < 0.05); however, P4 and P6 did not affect GOT and GPT activities (p > 0.05). Furthermore, P4 significantly increased hepatocyte GOT, GPT, t-SOD, CAT levels and lysozyme activities (p < 0.05), up-regulated SOD, CAT, Leap1 and Leap2 mRNA expression levels, and down-regulated the expression of Nrf2 and NOX2 mRNA (p < 0.05) in fish hepatocytes. The above results indicated that CPH and P4 enhanced hepatocyte metabolism, as well as improved antioxidant capacities and innate immunity of blunt snout bream hepatocytes.


Assuntos
Antioxidantes/metabolismo , Cyprinidae/imunologia , Imunidade Inata/efeitos dos fármacos , Hidrolisados de Proteína/metabolismo , Ração Animal/análise , Animais , Óleo de Sementes de Algodão/química , Dieta/veterinária , Suplementos Nutricionais/análise , Relação Dose-Resposta a Droga , Hidrolisados de Proteína/administração & dosagem , Distribuição Aleatória
11.
J Food Sci ; 85(1): 21-27, 2020 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31846088

RESUMO

The aminoacidemia resulting from food protein digestion in response to exercise plays an underlying role in the rate of muscle protein synthesis. Whey protein hydrolysate (WPH) has been demonstrated to cause more pronounced postexercise aminoacidemia compared with casein and soy. Although fish protein has been demonstrated to be a great source of amino acids, there is no data available providing information about the postexercise aminoacidemia after fish protein hydrolysate (FPH) intake. The present study investigated the characteristic patterns of postexercise aminoacidemia after WPH and FPH intake in nine physically active subjects (six males and three females). In a crossover, double-blind, and randomized design, all participants received oral doses of either 0.25 g/kg of FPH or WPH or placebo (PLA) immediately after a resistance exercise bout. Blood samples were taken before and at 30, 60, 90, 120 and 180 min after supplementation. There was a significant increase in plasma total amino acids (TAA), essential amino acids (EAA), branched-chain amino acids (BCAA), and leucine concentrations at 30 and 60 min after FPH supplementation, and at 30, 60, 90, and 120 min after WPH as compared to PLA. No significant differences were observed in plasma TAA, EAA, BCAA, and leucine concentrations between FPH and WPH at any time point, and there were no significant difference observed in the area under the curve for TAA, EAA, BCAA, and leucine between FPH and WPH. In conclusion, both FPH and WPH showed a rapid and pronounced postexercise aminoacidemia. FPH presented itself to be an alternative food source of rapidly digested proteins to be used after resistance exercise. PRACTICAL APPLICATION: Fish protein hydrolysate (FPH) demonstrated a rapid and pronounced postexercise aminoacidemia. Whey protein hydrolysate showed similar effects. FPH is presented as an alternative food source of rapidly digested proteins to be consumed by the population, especially physically active individuals.


Assuntos
Proteínas de Peixes/metabolismo , Proteínas Musculares/biossíntese , Hidrolisados de Proteína/metabolismo , Proteínas do Soro do Leite/metabolismo , Adulto , Aminoácidos/metabolismo , Animais , Método Duplo-Cego , Exercício Físico , Feminino , Humanos , Masculino
12.
J Dairy Sci ; 103(2): 1141-1150, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31785876

RESUMO

Food protein allergies are a major global concern. Hydrolysis of food proteins reduces their allergenicity, but another novel approach is the covalent attachment of polysaccharides to proteins via the Maillard reaction (i.e., glycation), which blocks some IgE binding epitopes on the protein allergen. We wanted to examine whether enzymatic hydrolysis, combined with glycation, could further reduce IgE binding for people with a cow milk protein allergy. Whey protein isolate (WPI) was hydrolyzed by immobilized trypsin and chymotrypsin to degree of hydrolysis (DH) values of 17 to 27%. Immobilized enzymes were used to avoid heat-treating the hydrolysate (to inactivate the enzymes, because heating could also affect the IgE binding ability of the protein). The resultant whey protein isolate hydrolysates (WPIH) were then glycated with 10-kDa dextran (DX) in aqueous solutions held at 62°C for 24 h. We analyzed the molar mass (MW) of WPIH samples and their corresponding glycates (WPIH-DX) using size-exclusion chromatography with multi-angle laser light scattering. We obtained blood sera from 8 patients who had been diagnosed with a cow milk protein allergy, and we used a composite serum for IgE binding analysis. The average MW values of samples WPIH-1 to WPIH-3 decreased from 11.15, 9.46, and 7.57 kDa with increasing DH values of 18.7, 22.5, and 27.1%. Glycation significantly reduced the high bitterness of the WPIH samples, as assessed by a trained sensory panel. The WPIH-DX glycates had significantly reduced WPI-specific IgE binding capacity compared to WPI or unglycated WPIH; we found an almost 99% reduction in IgE binding for the WPIH-DX glycate made from WPIH with a DH value of 27.1%. Hydrolysis of WPI followed by glycation with DX via the Maillard reaction significantly decreased the allergenicity of whey proteins.


Assuntos
Dextranos/metabolismo , Hipersensibilidade Alimentar/imunologia , Imunoglobulina E/sangue , Hipersensibilidade a Leite/imunologia , Proteínas do Soro do Leite/metabolismo , Alérgenos/imunologia , Alérgenos/metabolismo , Animais , Bovinos , Criança , Quimotripsina/metabolismo , Epitopos/metabolismo , Feminino , Hipersensibilidade Alimentar/sangue , Glicosilação , Humanos , Hidrólise , Reação de Maillard , Hidrolisados de Proteína/metabolismo , Tripsina/metabolismo , Proteínas do Soro do Leite/imunologia
13.
J Biosci Bioeng ; 129(3): 259-268, 2020 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31630942

RESUMO

Hazelnut proteins are an excellent source of bioactive peptides. Our previous study demonstrated that several novel peptides derived from Corylus heterophylla Fisch (C. heterophylla Fisch) have antioxidant and anti-inflammatory activities. In this study, we purified and identified anti-obesity peptides from hazelnut protein hydrolysates by chromatography and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Subsequently, we evaluated the inhibitory effect of the synthetic peptide on adipogenesis in 3T3-L1 adipocytes by Oil Red O staining, reverse transcription polymerase chain reaction (RT-PCR) and western blot. The results showed that a novel synthetic pentapeptide, Arg-Leu-Leu-Pro-His (RLLPH), derived from the C3 fraction, attenuated adipogenesis by downregulating the expression of several mRNAs related to adipogenesis, including peroxisome proliferator-activated receptor gamma (PPARγ), CCAAT/enhancer binding protein alpha (C/EBPα), adipocyte fatty acid-binding protein 2 (aP2), sterol regulatory element binding protein 1c (SREBP-1c), fatty acid synthase (FAS), acetyl-CoA carboxylase 1 (ACC1), and 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR). Moreover, RLLPH upregulated the levels of phosphorylated adenosine monophosphate-activated protein kinase (AMPK) and its substrate acetyl-CoA carboxylase (ACC) in 3T3-L1 adipocytes. A stability study revealed that RLLPH was relatively stable during pepsin digestion. These findings suggest that RLLPH has potential anti-obesity effects and may help combat metabolic diseases.


Assuntos
Proteínas Quinases Ativadas por AMP/metabolismo , Adipogenia/efeitos dos fármacos , Corylus/química , Peptídeos/farmacologia , Hidrolisados de Proteína/metabolismo , Células 3T3-L1 , Adipócitos/efeitos dos fármacos , Animais , Regulação para Baixo , Ativação Enzimática/efeitos dos fármacos , Camundongos , Peptídeos/química , Fatores de Transcrição/metabolismo
14.
J Sci Food Agric ; 100(1): 315-324, 2020 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-31525262

RESUMO

BACKGROUND: In order to utilize tilapia skin gelatin hydrolysate protein, which is normally discarded as industrial waste in the process of fish manufacture, we study the in vivo and in vitro angiotensin-I-converting enzyme (ACE) inhibitory activity of the peptide Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP). The aim was to provide a pharmacological basis of the development of minimal side effects of ACE inhibitors by comparative analysis with captopril in molecular docking. RESULTS: This peptide from protein-rich wastes showed excellent ACE inhibitory activity (IC50  = 2.577 µmol L-1 ) and exhibited a mixed noncompetitive inhibitory pattern with Lineweaver-Burk plots. Furthermore, LSGYGP and captopril groups both showed significant decreases in blood pressure after 6 h and maintained good digestive stability over 4 h. Molecular bond interactions differentiate competitive captopril upon hydrogen bond interactions and Zn(II) interaction. The C-terminal Pro generates three interactions (hydrogen bonds, hydrophilic interactions and Van der Waals interactions) in the peptide and effectively interacts with the S1 and S2 pockets of ACE. CONCLUSION: LSGYGP, with an IC50 value of 2.577 µmol L-1 , has an antihypertensive effect in spontaneously hypertensive rats. Through comparison with captopril, this study revealed that LSGYGP may be a potential food-derived ACE inhibitory peptide and could act as a functional food ingredient to prevent hypertension. © 2019 Society of Chemical Industry.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/química , Anti-Hipertensivos/química , Captopril/química , Hipertensão/tratamento farmacológico , Peptídeos/química , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/administração & dosagem , Inibidores da Enzima Conversora de Angiotensina/metabolismo , Animais , Anti-Hipertensivos/administração & dosagem , Anti-Hipertensivos/metabolismo , Pressão Sanguínea/efeitos dos fármacos , Captopril/administração & dosagem , Ciclídeos , Digestão , Proteínas de Peixes/química , Trato Gastrointestinal/metabolismo , Humanos , Ligação de Hidrogênio , Interações Hidrofóbicas e Hidrofílicas , Hipertensão/metabolismo , Hipertensão/fisiopatologia , Cinética , Masculino , Simulação de Acoplamento Molecular , Peptídeos/metabolismo , Peptídeos/farmacologia , Peptidil Dipeptidase A/química , Peptidil Dipeptidase A/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Ratos , Ratos Endogâmicos SHR
15.
Food Chem ; 302: 125350, 2020 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-31415999

RESUMO

The aim of the study was to investigate the use of serine protease from Yarrowia lipolytica yeast for reduction of milk proteins allergenicity. Whey protein concentrate (WPC-80), αs-casein and their hydrolysates were analyzed for the capacity to bind IgE and IgG antibodies present in sera from patients with cow milk protein allergy using a competitive ELISA. The hydrolysis of αs-casein and whey protein concentrate contributed to a significant reduction of their immunoreactive epitopes. In case of IgE antibodies, the lowest binding capacity was detected in the 24 h hydrolysates of both proteins in which the inhibition of the reaction was ≤20 and ≤68% for αs-casein and whey protein concentrate respectively. One hour hydrolysis of WPC-80 reduced the protein antigenicity, while the longer time (5 h) might lead to the exposure of new IgE - reactive epitopes.


Assuntos
Hipersensibilidade a Leite/imunologia , Proteínas do Leite/imunologia , Hidrolisados de Proteína/imunologia , Serina Proteases/metabolismo , Alérgenos/imunologia , Alérgenos/metabolismo , Animais , Caseínas/imunologia , Caseínas/metabolismo , Pré-Escolar , Ensaio de Imunoadsorção Enzimática , Epitopos , Feminino , Cabras/imunologia , Humanos , Imunoglobulina E/imunologia , Imunoglobulina E/metabolismo , Imunoglobulina G/imunologia , Imunoglobulina G/metabolismo , Proteínas do Leite/metabolismo , Hidrolisados de Proteína/metabolismo , Proteínas do Soro do Leite/imunologia , Proteínas do Soro do Leite/metabolismo , Yarrowia/enzimologia
16.
Anal Bioanal Chem ; 412(4): 973-982, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31872275

RESUMO

Protein hydrolysates are an important part of the human diet. Often, they are prepared from milk, soy, or collagen. In the present study, four different collagen hydrolysates were tested, varying in the average molecular weight and the animal source. Three types of samples, the dissolved start products, in vitro generated dialysates (containing the digested components that are potentially available for small intestinal absorption), and human serum collected after product ingestion, were analyzed using LC-MS to compare the state of the hydrolysates before and after absorption, i.e., uptake into the blood. It was found that the composition of the collagen hydrolysates prior to and after ingestion was highly complex and dynamic, which made it challenging to predefine a strategy for a targeted analysis. Therefore, we implemented a new analytical approach to first map hydrolysate data sets by performing non-targeted LC-MS analysis followed by non-targeted and targeted data analysis. It was shown that the insight gained by following such a top down (data) analytical workflow could be crucial for defining a suitable targeted setup and considering data trends beyond the defined targets. After having defined and performed a limited targeted analysis, it was found that, in our experimental setup, Hyp-Gly and especially Pro-Hyp contributed significantly as carrier to the total Hyp increase in blood after ingestion of collagen hydrolysate. Graphical abstract.


Assuntos
Colágeno/metabolismo , Hidrolisados de Proteína/metabolismo , Animais , Cromatografia Líquida de Alta Pressão , Colágeno/administração & dosagem , Colágeno/sangue , Colágeno/química , Humanos , Absorção Intestinal , Espectrometria de Massas , Hidrolisados de Proteína/administração & dosagem , Hidrolisados de Proteína/sangue , Hidrolisados de Proteína/química , Proteólise
17.
Int J Mol Sci ; 20(21)2019 Oct 31.
Artigo em Inglês | MEDLINE | ID: mdl-31683554

RESUMO

In our previous research, ten antioxidant pentapeptides including FYKWP, FTGMD, GFEPY, YLPYA, FPPYERRQ, GFYAA, FSGLR, FPYLRH, VPDDD, and GIEWA were identified from the hydrolysate of miiuy croaker (Miichthys miiuy) swim bladder. In this work, their protective function on H2O2-induced oxidative damage to human umbilical vein endothelial cells (HUVECs) was studied. Results indicated that there was no significant difference in the HUVEC viability between the normal group and the treated groups with the 10 pentapeptides at the concentration of 100 µM for 24 h (p < 0.05). Furthermore, FPYLRH of 100 µg/mL extremely significantly (p < 0.001) increased the viability (80.58% ± 5.01%) of HUVECs with H2O2-induced oxidative damage compared with that of the model group. The protective mechanism indicated that FPYLRH could extremely significantly (p < 0.001) increase the levels of superoxide dismutase (SOD) (211.36 ± 8.29 U/mg prot) and GSH-Px (53.06 ± 2.34 U/mg prot) and decrease the contents of reactive oxygen species (ROS) (139.1 ± 11.8% of control), malondialdehyde (MDA) (13.66 ± 0.71 nM/mg), and nitric oxide (NO) (4.36 ± 0.32 µM/L) at the concentration of 100 µM in HUVECs with H2O2-induced oxidative damage compared with those of the model group. In addition, FPYLRH dose-dependently protected DNA in oxidative damage HUVECs model. These results suggested that FPYLRH could significantly attenuate the H2O2-induced stress injury in HUVECs and might be used as a potential natural antioxidant in the functional food industries.


Assuntos
Antioxidantes/farmacologia , Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos , Peróxido de Hidrogênio/farmacologia , Oligopeptídeos/farmacologia , Perciformes/metabolismo , Hidrolisados de Proteína/metabolismo , Sacos Aéreos/química , Sacos Aéreos/metabolismo , Sequência de Aminoácidos , Animais , Sobrevivência Celular/efeitos dos fármacos , Células Cultivadas , Proteínas de Peixes/química , Proteínas de Peixes/metabolismo , Células Endoteliais da Veia Umbilical Humana/citologia , Células Endoteliais da Veia Umbilical Humana/metabolismo , Humanos , Oxidantes/farmacologia , Substâncias Protetoras/farmacologia , Hidrolisados de Proteína/química , Espécies Reativas de Oxigênio/metabolismo , Superóxido Dismutase/metabolismo
18.
J Food Biochem ; 43(12): e13062, 2019 12.
Artigo em Inglês | MEDLINE | ID: mdl-31571257

RESUMO

Metabolic Syndrome (MS) is related to increased risk of early death due to cardiovascular complications, among others. Dietary intervention has been suggested as the safest and most cost-effective alternative for treatment of those alterations in patients with MS. The aim of this study was to investigate the effects of different egg white hydrolysates (HEW1 and HEW2) in obese Zucker rats, focus on the development of cardiovascular complications. Blood pressure, heart rate, basal cardiac function and vascular reactivity in aorta and mesenteric resistance arteries were evaluated. Reactive oxygen species production by dihydroethidium-emitted fluorescence, NOX-1 mRNA levels by qRT-PCR, angiotensin-converting enzyme activity by fluorimetry and kidney histopathology were also analysed. Both hydrolysates improve the endothelial dysfunction occurring in resistance arteries. Additionally, HEW2 reduced vascular oxidative stress. PRACTICAL APPLICATIONS: Egg white is a good source of bioactive peptides, some of them with high antioxidant activity. They may be used as functional foods ingredients and could serve as an alternative therapeutic option to decrease some Metabolic Syndrome-related complications. This study suggests that these hydrolysates could be an interesting non-pharmacological tool to control cardiovascular complications related to Metabolic Syndrome.


Assuntos
Antioxidantes/metabolismo , Aorta/efeitos dos fármacos , Pressão Sanguínea/efeitos dos fármacos , Clara de Ovo/química , Artérias Mesentéricas/efeitos dos fármacos , Obesidade/complicações , Estresse Oxidativo/efeitos dos fármacos , Hidrolisados de Proteína/metabolismo , Animais , Ratos , Ratos Zucker
19.
BMC Complement Altern Med ; 19(1): 283, 2019 Oct 25.
Artigo em Inglês | MEDLINE | ID: mdl-31653214

RESUMO

BACKGROUND: A potato protein hydrolysate, APPH is a potential anti-obesity diet ingredient. Since, obesity leads to deterioration of liver function and associated liver diseases, in this study the effect of APPH on high fat diet (HFD) associated liver damages was investigated. METHODS: Six week old male hamsters were randomly separated to six groups (n = 8) as control, HFD (HFD fed obese), L-APPH (HFD + 15 mg/kg/day of APPH), M-APPH (HFD + 30 mg/kg/day), H-APPH (HFD + 75 mg/kg/day of APPH) and PB (HFD + 500 mg/kg/day of probucol). HFD fed hamsters were administered with APPH 50 days through oral gavage. The animals were euthanized and the number of apoptotic nuclei in liver tissue was determined by TUNEL staining and the extent of interstitial fibrosis was determined by Masson's trichrome staining. Modulation in the molecular events associated with apoptosis and fibrosis were elucidated from the western blotting analysis of the total protein extracts. RESULTS: Hamsters fed with high fat diet showed symptoms of liver damage as measured from serum markers like alanine aminotransferase and aspartate aminotransferase levels. However a 50 day long supplementation of APPH effectively ameliorated the effects of HFD. HFD also modulated the expression of survival and apoptosis proteins in the hamster liver. Further the HFD groups showed elevated levels of fibrosis markers in liver. The increase in fibrosis and apoptosis was correlated with the increase in the levels of phosphorylated extracellular signal-regulated kinases (pERK1/2) revealing a potential role of ERK in the HFD mediated liver damage. However APPH treatment reduced the effect of HFD on the apoptosis and fibrosis markers considerably and provided hepato-protection. CONCLUSION: APPH can therefore be considered as an efficient therapeutic agent to ameliorate high fat diet related liver damages.


Assuntos
Caspase 3/metabolismo , Metaloproteinase 2 da Matriz/metabolismo , Metaloproteinase 9 da Matriz/metabolismo , Obesidade/dietoterapia , Proteínas de Plantas/metabolismo , Proteínas Proto-Oncogênicas c-akt/metabolismo , Solanum tuberosum/metabolismo , Animais , Apoptose , Caspase 3/genética , Cricetinae , Dieta Hiperlipídica/efeitos adversos , Fibrose/dietoterapia , Fibrose/genética , Fibrose/metabolismo , Fibrose/fisiopatologia , Humanos , Fígado/citologia , Fígado/metabolismo , Fígado/patologia , Masculino , Metaloproteinase 2 da Matriz/genética , Metaloproteinase 9 da Matriz/genética , Mesocricetus , Obesidade/genética , Obesidade/metabolismo , Obesidade/fisiopatologia , Proteínas de Plantas/química , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Proteínas Proto-Oncogênicas c-akt/genética , Solanum tuberosum/química
20.
Int J Mol Sci ; 20(20)2019 Oct 20.
Artigo em Inglês | MEDLINE | ID: mdl-31635140

RESUMO

In this study, the potential bioactivities of Portuguese oyster (Crassostrea angulata) proteins were predicted through in silico analyses and confirmed by in vitro tests. C. angulata proteins were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and identified by proteomics techniques. Hydrolysis simulation by BIOPEP-UWM database revealed that pepsin (pH > 2) can theoretically release greatest amount of bioactive peptides from C. angulata proteins, predominantly angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory peptides, followed by stem bromelain and papain. Hydrolysates produced by pepsin, bromelain and papain have shown ACE and DPP-IV inhibitory activities in vitro, with pepsin hydrolysate (PEH) having the strongest activity of 78.18% and 44.34% at 2 mg/mL, respectively. Bioactivity assays of PEH fractions showed that low molecular weight (MW) fractions possessed stronger inhibitory activity than crude hydrolysate. Overall, in vitro analysis results corresponded with in silico predictions. Current findings suggest that in silico analysis is a rapid method to predict bioactive peptides in food proteins and determine suitable enzymes for hydrolysis. Moreover, C. angulata proteins can be a potential source of peptides with pharmaceutical and nutraceutical application.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Crassostrea/metabolismo , Inibidores da Dipeptidil Peptidase IV/farmacologia , Fragmentos de Peptídeos/farmacologia , Hidrolisados de Proteína/metabolismo , Proteoma/análise , Animais , Simulação por Computador , Dipeptidil Peptidase 4/química , Técnicas In Vitro , Peptidil Dipeptidase A/química
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