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1.
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
2.
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 , Ligações 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
3.
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
4.
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
5.
Mar Drugs ; 17(8)2019 Aug 08.
Artigo em Inglês | MEDLINE | ID: mdl-31398788

RESUMO

Angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from natural products have shown a blood pressure lowering effect with no side effects. In this study, two novel ACE inhibitory peptides (His-Leu-His-Thr, HLHT and Gly-Trp-Ala, GWA) were purified from pearl oyster (Pinctada fucata martensii) meat protein hydrolysate with alkaline protease by ultrafiltration, polyethylene glycol methyl ether modified immobilized metal ion affinity medium, and reverse-phase high performance liquid chromatography. Both peptides exhibited high ACE inhibitory activity with IC50 values of 458.06 ± 3.24 µM and 109.25 ± 1.45 µM, respectively. Based on the results of a Lineweaver-Burk plot, HLHT and GWA were found to be non-competitive inhibitor and competitive inhibitor respectively, which were confirmed by molecular docking. Furthermore, the pearl oyster meat protein hydrolysate exhibited an effective antihypertensive effect on SD rats. These results conclude that pearl oyster meat protein is a potential resource of ACE inhibitory peptides and the purified peptides, HLHT and GWA, can be exploited as functional food ingredients against hypertension.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/química , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Peptídeos/química , Peptídeos/farmacologia , Peptidil Dipeptidase A/metabolismo , Pinctada/química , Hidrolisados de Proteína/química , Animais , Anti-Hipertensivos/química , Anti-Hipertensivos/farmacologia , Cromatografia Líquida de Alta Pressão/métodos , Hipertensão/tratamento farmacológico , Masculino , Carne , Simulação de Acoplamento Molecular , Pinctada/metabolismo , Hidrolisados de Proteína/metabolismo , Ratos , Ratos Sprague-Dawley , Ultrafiltração/métodos
6.
Cochrane Database Syst Rev ; 7: CD012412, 2019 07 24.
Artigo em Inglês | MEDLINE | ID: mdl-31339557

RESUMO

BACKGROUND: When human milk is not available for feeding preterm infants, protein hydrolysate, rather than standard cow's milk formulas (with intact proteins), is often used because it is perceived as being tolerated better and less likely to lead to complications. However, protein hydrolysate formulas are more expensive than standard formulas, and concern exists that their use in practice is not supported by high-quality evidence. OBJECTIVES: To assess the effects of feeding preterm infants hydrolysed formula (vs standard cow's milk formula) on risk of feed intolerance, necrotising enterocolitis, and other morbidity and mortality. SEARCH METHODS: We used the standard Cochrane Neonatal search strategy including electronic searches of the Cochrane Central Register of Controlled Trials (CENTRAL; 2019, Issue 1), in the Cochrane Library; Ovid MEDLINE (1966 to 28 January 2019); Ovid Embase (1980 to 28 January 2019); and the Cumulative Index to Nursing and Allied Health Literature (CINAHL) (28 January 2019), as well as conference proceedings and previous reviews. SELECTION CRITERIA: Randomised and quasi-randomised controlled trials that compared feeding preterm infants protein hydrolysate versus standard (non-hydrolysed) cow's milk formula. DATA COLLECTION AND ANALYSIS: Two review authors assessed trial eligibility and risk of bias and extracted data independently. We analysed treatment effects as described in the individual trials and reported risk ratios and risk differences for dichotomous data, and mean differences for continuous data, with respective 95% confidence intervals (CIs). We used a fixed-effect model in meta-analyses and explored potential causes of heterogeneity in sensitivity analyses. We assessed quality of evidence at the outcome level using the GRADE approach. MAIN RESULTS: We identified 11 trials for inclusion in the review. All trials were small (total participants 665) and had various methodological limitations including uncertainty about methods to ensure allocation concealment and blinding. Most participants were clinically stable preterm infants of less than about 34 weeks' gestational age or with birth weight less than about 1750 g. Fewer participants were extremely preterm, extremely low birth weight, or growth restricted. Most trials found no effects on feed intolerance, assessed variously as mean pre-feed gastric residual volume, incidence of abdominal distension or other gastrointestinal signs of concern, or time taken to achieve full enteral feeds (meta-analysis was limited because studies used different measures). Meta-analysis showed no effect on the risk of necrotising enterocolitis (typical risk ratio 1.10, 95% CI 0.36 to 3.34; risk difference 0.00, 95% CI -0.03 to 0.04; 5 trials, 385 infants) (low-certainty evidence; downgraded for imprecision and design weaknesses). AUTHORS' CONCLUSIONS: The identified trials provide only low-certainty evidence about the effects of feeding preterm infants protein hydrolysate versus standard formula. Existing data do not support conclusions that feeding protein hydrolysate affects the risk of feed intolerance or necrotising enterocolitis. Additional large, pragmatic trials are needed to provide more reliable and precise estimates of effectiveness and cost-effectiveness.


Assuntos
Fórmulas Infantis , Fenômenos Fisiológicos da Nutrição do Lactente/fisiologia , Recém-Nascido Prematuro/crescimento & desenvolvimento , Hidrolisados de Proteína/administração & dosagem , Humanos , Lactente , Recém-Nascido , Hidrolisados de Proteína/metabolismo , Ensaios Clínicos Controlados Aleatórios como Assunto
7.
Mar Drugs ; 17(8)2019 Jul 25.
Artigo em Inglês | MEDLINE | ID: mdl-31349695

RESUMO

In this study, three synthetic zinc-chelating peptides (ZCPs) derived from sea cucumber hydrolysates with limited or none of the common metal-chelating amino-acid residues were analyzed by flame atomic absorption spectroscopy, circular dichroism spectroscopy, size exclusion chromatography, zeta-potential, Fourier transform infrared spectroscopy, Raman spectroscopy and nuclear magnetic resonance spectroscopy. The amount of zinc bound to the ZCPs reached maximum values with ZCP:zinc at 1:1, and it was not further increased by additional zinc presence. The secondary structures of ZCPs were slightly altered, whereas no formation of multimers was observed. Furthermore, zinc increased the zeta-potential value by neutralizing the negatively charged residues. Only free carboxyl in C-terminus of ZCPs was identified as the primary binding site of zinc. These results provide the theoretical foundation to understand the mechanism of zinc chelation by peptides.


Assuntos
Quelantes/metabolismo , Peptídeos/metabolismo , Pepinos-do-Mar/metabolismo , Stichopus/metabolismo , Zinco/metabolismo , Animais , Sítios de Ligação , Cromatografia em Gel/métodos , Hidrolisados de Proteína/metabolismo , Espectroscopia de Infravermelho com Transformada de Fourier/métodos
8.
Nutrients ; 11(7)2019 Jul 23.
Artigo em Inglês | MEDLINE | ID: mdl-31340611

RESUMO

Milk proteins have been hypothesized to protect against type 2 diabetes (T2DM) by beneficially modulating glycemic response, predominantly in the postprandial status. This potential is, amongst others, attributed to the high content of whey proteins, which are commonly a product of cheese production. However, native whey has received substantial attention due to its higher leucine content, and its postprandial glycemic effect has not been assessed thus far in prediabetes. In the present study, the impact of a milk protein hydrolysate of native whey origin with alpha-glucosidase inhibiting properties was determined in prediabetics in a randomized, cross-over trial. Subjects received a single dose of placebo or low- or high-dosed milk protein hydrolysate prior to a challenge meal high in carbohydrates. Concentration-time curves of glucose and insulin were assessed. Incremental areas under the curve (iAUC) of glucose as the primary outcome were significantly reduced by low-dosed milk peptides compared to placebo (p = 0.0472), and a minor insulinotropic effect was seen. A longer intervention period with the low-dosed product did not strengthen glucose response but significantly reduced HbA1c values (p = 0.0244). In conclusion, the current milk protein hydrolysate of native whey origin has the potential to modulate postprandial hyperglycemia and hence may contribute in reducing the future risk of developing T2DM.


Assuntos
Glicemia/metabolismo , Suplementos Nutricionais , Inibidores de Glicosídeo Hidrolases/administração & dosagem , Proteínas do Leite/administração & dosagem , Período Pós-Prandial , Estado Pré-Diabético/dietoterapia , Hidrolisados de Proteína/administração & dosagem , Adulto , Idoso , Biomarcadores/sangue , Estudos Cross-Over , Suplementos Nutricionais/efeitos adversos , Método Duplo-Cego , Feminino , Alemanha , Hemoglobina A Glicada/metabolismo , Inibidores de Glicosídeo Hidrolases/efeitos adversos , Inibidores de Glicosídeo Hidrolases/metabolismo , Humanos , Insulina/sangue , Masculino , Pessoa de Meia-Idade , Proteínas do Leite/efeitos adversos , Proteínas do Leite/metabolismo , Estado Pré-Diabético/sangue , Estado Pré-Diabético/diagnóstico , Hidrolisados de Proteína/efeitos adversos , Hidrolisados de Proteína/metabolismo , Fatores de Tempo , Resultado do Tratamento
9.
Food Funct ; 10(7): 4062-4070, 2019 Jul 17.
Artigo em Inglês | MEDLINE | ID: mdl-31225553

RESUMO

Herein, the potential of hydrolysates of chicken feet proteins as natural dipeptidyl-peptidase IV (DPP-IV) inhibitors was investigated; moreover, three hydrolysates were selected due to their high DPP-IV inhibitory capacity (>80% inhibition), showing the IC50 values of around 300 µg estimated protein per mL; one of them (named p4H) was selected for the posterior analysis. In addition, its effect on glucose tolerance was investigated in two rat models (diet and age-induced) of glucose-intolerance and healthy animals; the amount of 300 mg estimated peptide per kg body weight improved the plasma glucose profile in both glucose-intolerance models. Moreover, it stimulated active GLP-1 release in the enteroendocrine STC-1 cells and rat ileum tissue. In conclusion, our results indicate that chicken feet proteins are a good source of bioactive peptides as DPP-IV inhibitors. Moreover, our results highlight the potential of the selected hydrolysate p4H in the management of type 2 diabetes due to its dual function of inhibition of the DPP-IV activity and induction of the GLP-1 release.


Assuntos
Galinhas/metabolismo , Inibidores da Dipeptidil Peptidase IV/farmacologia , , Peptídeo 1 Semelhante ao Glucagon/metabolismo , Hipoglicemiantes/farmacologia , Incretinas/farmacologia , Hidrolisados de Proteína/metabolismo , Animais , Glicemia , Peso Corporal , Linhagem Celular , Diabetes Mellitus Tipo 2 , Dieta , Modelos Animais de Doenças , Sistemas de Liberação de Medicamentos , Feminino , Intolerância à Glucose , Concentração Inibidora 50 , Masculino , Ratos , Ratos Wistar
10.
Nutrients ; 11(5)2019 May 13.
Artigo em Inglês | MEDLINE | ID: mdl-31086034

RESUMO

Collagen is characterized by its high content of glycine, proline and hydroxyproline, and is found to exert beneficial effects on joint pain related to activity and osteoarthritis. However, to exert any beneficial effects it is essential that collagen is optimally absorbed. This study aimed to investigate the postprandial absorption of collagen and elucidate the impact of an exogenous enzymatic hydrolysis on absorption rate and bioavailability. A randomized, blinded, cross-over study was conducted where ten healthy male subjects received either 35 g enzymatically hydrolyzed collagen protein (EHC), 35 g non-enzymatically hydrolyzed collagen protein (NC) or placebo (250 mL water) on three nonconsecutive days. Blood samples were drawn before, and up to 240 min following, ingestion and the blood metabolome was characterized by nuclear magnetic resonance (NMR)-based metabolomics. A significant increase in the plasma concentration of nearly all amino acids (AAs) was observed over a 240 min period for both EHC and NC. In addition, the absorption rate and bioavailability of glycine, proline and hydroxyproline were significantly higher for EHC (p < 0.05). In conclusion, ingestion of collagen hydrolysates increases postprandial plasma concentrations of AAs over a period of 240 min, and an enzymatic hydrolysis increases the absorption rate and bioavailability of the collagen-rich AAs glycine, proline and hydroxyproline.


Assuntos
Colágeno/química , Colágeno/metabolismo , Período Pós-Prandial/fisiologia , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Adulto , Aminoácidos/sangue , Aminoácidos/metabolismo , Glicemia , Estudos Cross-Over , Humanos , Hidrólise , Masculino
11.
Food Funct ; 10(6): 3368-3378, 2019 Jun 19.
Artigo em Inglês | MEDLINE | ID: mdl-31099356

RESUMO

Gut microbiota has been identified as an important factor in the link between nutrient excess and obesity. The aim of this study was to confirm whether bovine α-lactalbumin hydrolysates (LAH) can ameliorate high-fat diet (HFD)-induced endotoxemia and systematic inflammation by modulating the structure of gut microbiota in mice. The results showed that LAH changed the overall structure of gut microbiota in HFD-induced obese mice. LAH increased the Bacteroidetes/Firmicutes ratios and the relative abundance of S24-7, Lachnospiraceae and Blautia. Spearman's correlation analysis revealed significant correlations between the alteration of gut microbiota and obesity-related indexes. LAH decreased the HFD-induced protein expression of G protein-coupled receptor 43 (GPR43) and 41 (GPR41) in the colon tissue. Besides, LAH inhibited the destruction of the gut barrier through the up-regulation of tight junction protein (zonulin/zonula occludens (ZO)-1 and occludin) expression and the decrease of toll-like receptor 4 (TLR4) protein expression in the colon tissue. LAH also significantly reduced the concentration of tumour cell necrosis factor-α (TNF-α) and interleukin-6 (IL-6) in both serum and colon and decreased the level of lipopolysaccharides (LPS) in serum and feces, leading to reduced systematic inflammation and metabolic endotoxemia. In summary, LAH partly modulated the gut microbial composition and structure, and alleviated the obesity-associated inflammation. These findings shed light on bovine α-lactalbumin hydrolysate as a potential functional food ingredient to prevent obesity-related inflammation.


Assuntos
Endotoxemia/dietoterapia , Microbioma Gastrointestinal , Lactalbumina/química , Obesidade/dietoterapia , Hidrolisados de Proteína/metabolismo , Animais , Bactérias/classificação , Bactérias/genética , Bactérias/isolamento & purificação , Bactérias/metabolismo , Bovinos , Dieta Hiperlipídica/efeitos adversos , Endotoxemia/etiologia , Endotoxemia/imunologia , Endotoxemia/microbiologia , Humanos , Lactalbumina/metabolismo , Masculino , Camundongos , Camundongos Endogâmicos C57BL , Obesidade/etiologia , Obesidade/imunologia , Obesidade/microbiologia , Hidrolisados de Proteína/química , Receptores Acoplados a Proteínas-G/genética , Receptores Acoplados a Proteínas-G/imunologia , Fator de Necrose Tumoral alfa/genética , Fator de Necrose Tumoral alfa/imunologia
12.
Nutrients ; 11(4)2019 Apr 04.
Artigo em Inglês | MEDLINE | ID: mdl-30987324

RESUMO

Alcalase- generated potato protein hydrolysate (APPH) is a potential bioactive peptide against diabetes mellitus (DM) and DM-associated secondary effects in animal models. The aim of the present study was to find the efficiency of a deca-peptide DIKTNKPVIF (DF) from APPH against DM. Six-week-old male ICR mice were divided into the following groups: Control, Control+DF (received 50 mg/kg DF), streptozotocin (STZ)-induced DM group, DM+Acarbose group (20 mg/kg of acarbose), DM+DF-L (25 mg/kg of DF), DM+DF-H (50 mg/kg of DF), and DM+APPH (50 mg/kg of APPH). Comparable to APPH, treatment with DF effectively regulated blood glucose level and also controlled plasma total glycerol (TG), total cholesterol (TC), insulin, and HbA1c levels in DM animals. DF treatment also showed evidence of ameliorating DM-associated damages in the pancreatic islets and in the liver, heart, and kidney tissues. Therefore, the results demonstrate that the short synthetic peptide-DF may effectively provide protection against DM-associated damages.


Assuntos
Glicemia/efeitos dos fármacos , Diabetes Mellitus Experimental/prevenção & controle , Hipoglicemiantes/farmacologia , Ilhotas Pancreáticas/efeitos dos fármacos , Oligopeptídeos/farmacologia , Proteínas de Plantas/metabolismo , Hidrolisados de Proteína/metabolismo , Solanum tuberosum/metabolismo , Animais , Biomarcadores/sangue , Glicemia/metabolismo , Diabetes Mellitus Experimental/sangue , Diabetes Mellitus Experimental/induzido quimicamente , Diabetes Mellitus Experimental/patologia , Hemoglobina A Glicada/metabolismo , Hipoglicemiantes/metabolismo , Insulina/sangue , Ilhotas Pancreáticas/metabolismo , Ilhotas Pancreáticas/patologia , Lipídeos/sangue , Masculino , Camundongos Endogâmicos ICR , Oligopeptídeos/metabolismo , Estreptozocina , Subtilisinas/metabolismo
13.
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
14.
Mar Drugs ; 17(4)2019 Apr 13.
Artigo em Inglês | MEDLINE | ID: mdl-31013895

RESUMO

A previous report indicated that collagen hydrolysate fraction (F7) from Spanish mackerel (Scomberomorous niphonius) skins showed high reducing power and radical scavenging activities on 2,2-Diphenyl-1-picrylhydrazyl (DPPH) (EC50 value of 1.57 mg/mL) and hydroxyl (EC50 value of 1.20 mg/mL). In this work, eight peptides were isolated from F7 and identified as Gly-Pro-Tyr (GPY, 335.31 Da), Gly-Pro-Thr-Gly-Glu (GPTGE, 459.47 Da), Pro-Phe-Gly-Pro-Asp (PFGPD, 531.52 Da), Gly-Pro-Thr-Gly-Ala-Lys (GPTGAKG, 586.65 Da), Pro-Tyr-Gly-Ala-Lys-Gly (PYGAKG, 591.69 Da), Gly-Ala-Thr-Gly-Pro-Gln-Gly (GATGPQG, 586.61 Da), Gly-Pro-Phe-Gly-Pro-Met (GPFGPM, 604.73 Da), and Tyr-Gly-Pro-Met (YGPM, 466.50 Da), respectively. Among them, PFGPD, PYGAKG, and YGPM exhibited strong radical scavenging activities on DPPH (EC50 values of 0.80, 3.02, and 0.72 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), hydroxyl (EC50 values of 0.81, 0.66, and 0.88 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), superoxide anion (EC50 values of 0.91, 0.80, and 0.73 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) cation (EC50 values of 0.86, 1.07, and 0.82 mg/mL for PFGPD, PYGAKG, and YGPM, respectively) in a positive concentration-activity relationship. Furthermore, PFGPD, PYGAKG, and YGPM could effectively reduce Fe3+ to Fe2+ and inhibit lipid peroxidation. Hence, eight collagen peptides from hydrolysate of Spanish mackerel skins might be served as antioxidant candidates for various industrial applications.


Assuntos
Antioxidantes/química , Colágeno/química , Colágeno/farmacologia , Peptídeos/química , Peptídeos/farmacologia , Perciformes/metabolismo , Pele/química , Animais , Antioxidantes/farmacologia , Peroxidação de Lipídeos/efeitos dos fármacos , Hidrolisados de Proteína/metabolismo , Superóxidos/metabolismo
15.
J Agric Food Chem ; 67(16): 4671-4678, 2019 Apr 24.
Artigo em Inglês | MEDLINE | ID: mdl-30929424

RESUMO

Collagen-derived hydroxyproline (Hyp)-containing oligopeptides, known to have various physiological functions, are detected in blood at markedly higher concentrations after oral ingestion of collagen hydrolysate. Monitoring the absorption and metabolism of the bioactive peptides is essential to investigate the beneficial effects of collagen hydrolysate. We previously developed an internal standard mixture by sequential protease digestion of stable isotope-labeled collagen, which enabled highly accurate quantitation of collagen-derived oligopeptides by liquid chromatography-mass spectrometry (LC-MS). However, the use of proteases caused a profound imbalance in the generated peptides. Here, we employed partial acid hydrolysis to achieve more efficient and balanced peptide generation. Various stable isotope-labeled oligopeptides were detected after 0.5 h acid hydrolysis, and marked enhancement of peptide generation compared with the previous enzymatic method was observed, especially for Hyp-Gly (27.8 ± 0.6 ng/µg vs 0.231 ± 0.02 ng/µg). The acid hydrolysate was then heated to generate labeled cyclic dipeptides. Using the novel internal standard mixture in LC-MS, we were able to simultaneously quantitate 23 collagen-derived oligopeptides in human plasma and urine after oral administration of collagen hydrolysate.


Assuntos
Colágeno/química , Colágeno/metabolismo , Ácidos/química , Adulto , Animais , Isótopos de Carbono/análise , Cromatografia Líquida de Alta Pressão , Feminino , Humanos , Marcação por Isótopo , Masculino , Isótopos de Nitrogênio/análise , Peptídeos/química , Peptídeos/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Pele/química , Suínos , Espectrometria de Massas em Tandem , Adulto Jovem
16.
Colloids Surf B Biointerfaces ; 178: 421-429, 2019 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-30908998

RESUMO

In this research, bioactive peptides produced from flaxseed protein by alcalase, pancreatin, trypsin and pepsin, were encapsulated by spray drying. After analysis of amino acid composition and antioxidant properties of hydrolysates, the effect of spray-drying encapsulation via different maltodextrin (MD) to hydrolysate ratios (1:1, 2:1 and 3:1 w/w) on the production yield, physicochemical properties, functional activities, chemical structure, and morphology of final powder particles were evaluated. Among the hydrolysates, peptides produced with alcalase had the highest hydrolysis degree (38.2%), hydrophobic amino acids (255 mg/g) and antioxidants (126 mg/g). Among spray-dried samples, the powders obtained by 3:1 w/w ratio (MD: peptide) showed the highest radical scavenging activity for DPPH- (68.93%), ABTS+ (85.62%), hydroxyl (94.97%), nitric oxide (64.03%), reducing power (95.49%), total antioxidant activity (96.68%), and iron (95.31%) and copper (95.49%) chelating activity. Evaluation of chemical structure (FTIR) indicated that hydrolysates were coated and dispersed within maltodextrin matrix. SEM images showed the effect of different carrier ratios on the production of irregular and shrunk particles with different sizes and matrix-type structures.


Assuntos
Linho/enzimologia , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Antioxidantes/química , Compostos de Bifenilo/química , Óxido Nítrico/química , Picratos/química
17.
Mar Drugs ; 17(3)2019 Mar 19.
Artigo em Inglês | MEDLINE | ID: mdl-30893907

RESUMO

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis protein was hydrolyzed by five different proteases (trypsin, pepsin, papain, α-chymotrypsin, alcalase) to prepare peptides; compared with other hydrolysates, the trypsin hydrolysates exhibited the highest ACE inhibitory activity. The hydrolysis conditions were further optimized by response surface methodology (RSM), and the optimum conditions were as follows: pH 8.4, temperature 28.5 °C, enzyme/protein ratio (E/S) 4.0%, substrate concentration 15 mg/mL, and enzymolysis time 5.0 h. After fractionation and purification by ultrafiltration, gel exclusion chromatography and reverse-phase high-performance liquid chromatography, two novel purified ACE inhibitors with IC50 values of 219.35 µM (0.183 mg/mL) and 236.85 µM (0.179 mg/mL) were obtained. The molecular mass and amino acid sequence of the ACE inhibitory peptides were identified as Phe-Gly-Met-Pro-Leu-Asp-Arg (FGMPLDR; MW 834.41 Da) and Met-Glu-Leu-Val-Leu-Arg (MELVLR; MW 759.43 Da) by ultra-performance liquid chromatography-tandem mass spectrometry. A molecular docking study revealed that the ACE inhibitory activities of the peptides were mainly attributable to the hydrogen bond and Zn(II) interactions between the peptides and ACE. The results of this study provide a theoretical basis for the high-valued application of U. intestinalis and the development of food-derived ACE inhibitory peptides.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Anti-Hipertensivos/farmacologia , Peptídeos/farmacologia , Peptidil Dipeptidase A/metabolismo , Ulva , Inibidores da Enzima Conversora de Angiotensina/química , Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Inibidores da Enzima Conversora de Angiotensina/uso terapêutico , Anti-Hipertensivos/química , Anti-Hipertensivos/isolamento & purificação , Anti-Hipertensivos/uso terapêutico , Estabilidade de Medicamentos , Ensaios Enzimáticos , Hidrólise , Hipertensão/tratamento farmacológico , Concentração Inibidora 50 , Simulação de Acoplamento Molecular , Peptídeo Hidrolases/metabolismo , Peptídeos/química , Peptídeos/isolamento & purificação , Peptídeos/uso terapêutico , Peptidil Dipeptidase A/química , Hidrolisados de Proteína/química , Hidrolisados de Proteína/isolamento & purificação , Hidrolisados de Proteína/metabolismo , Alga Marinha/química
18.
Plant Foods Hum Nutr ; 74(2): 225-231, 2019 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-30912008

RESUMO

Effects of ultrasonication, boiling, steaming, microwaving and autoclaving pretreatments on the production of sweet potato protein hydrolysates (SPPH) by single and combined Alcalase (ALC) and Protease (PRO) were investigated, as well as antioxidant activities of SPPH subjected to in vitro gastrointestinal digestion (GID). All pretreatments significantly increased the degree of hydrolysis (DH) and antioxidant activities of SPPH by ALC, PRO and ALC + PRO in the order of autoclaving > steaming, microwaving, boiling > ultrasonication (P < 0.05). GID significantly enhanced antioxidant activities and increased MW <3 kDa peptide fraction contents of all SPPH. Diverse peptides were identified as sporamin A, A precursor and sporamin B before and after GID from LC-QTOF-MS/MS analysis. Peptides with higher antioxidant amino acids of Trp, Tyr, Met, Cys, His and Phe were found after GID. There is a great potential application of SPPH as a novel food ingredient as a natural antioxidant.


Assuntos
Antioxidantes/metabolismo , Ipomoea batatas/metabolismo , Peptídeos/metabolismo , Proteínas de Plantas/metabolismo , Hidrolisados de Proteína/metabolismo , Precursores de Proteínas/metabolismo , Aminoácidos/metabolismo , Digestão , Hidrólise , Peptídeo Hidrolases/metabolismo , Subtilisinas/metabolismo
19.
Food Funct ; 10(3): 1653-1660, 2019 Mar 20.
Artigo em Inglês | MEDLINE | ID: mdl-30839010

RESUMO

Whey protein isolate (WPI) was hydrolyzed by alcalase and trypsin for three hydrolysis degrees (DHs), followed by transglutaminase (TGase) induced cross-linking. The prepared products were measured for surface hydrophobicity and emulsifying and foaming properties, as well as in vitro antigenicity for α-lactalbumin and ß-lactoglobulin. The results indicated that enzymatic hydrolysis of WPI mostly resulted in WPI hydrolysates with significantly decreased antigenicity of α-lactalbumin and ß-lactoglobulin, especially in the case of a higher DH value. Moreover, the TGase-induced cross-linking led to a further antigenicity decrease for these prepared products. Alcalase was always more potent than trypsin to decrease antigenicity. In comparison with WPI, the conducted enzymatic hydrolysis also brought losses to surface hydrophobicity and emulsifying and foaming properties. On the other hand, the conducted cross-linking could partially rescue these properties. It is thus concluded that the assessed enzymatic hydrolysis coupled with TGase-induced cross-linking might be an applicable process for WPI to decrease its potential antigenicity but reserve partial interfacial properties.


Assuntos
Hidrolisados de Proteína/imunologia , Hidrolisados de Proteína/metabolismo , Transglutaminases/metabolismo , Proteínas do Soro do Leite/química , Antígenos , Hidrólise , Hidrolisados de Proteína/química , Proteínas do Soro do Leite/metabolismo
20.
Food Chem ; 287: 76-84, 2019 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-30857721

RESUMO

In this study, the succinic anhydride (SA) modified whey protein isolate (WPI) and whey protein hydrolysates (WPH) were prepared and characterized as novel emulsifiers. After the succinylation, the solubility, emulsibility, and water/oil binding capacity of WPI/WPH were improved. Emulsions with modified and unmodified WPI/WPH were prepared and characterized on rheological property, particle sizes, and droplet distribution using rheometer, zeta-sizer and confocal laser scanning microscopy. A simulated digestion system was utilized to monitor the gastrointestinal fate of emulsions and the bioaccessibility of curcumin loaded in emulsions. The final digestion extents of WPIE-10 and WPHE-10 (emulsions stabilized by modified WPI/WPH with 10% SA addition) were lower than those of WPIE-0 and WPHE-0 (emulsions stabilized by unmodified WPI/WPH). The order of curcumin bioaccessibility was WPIE-10 (79.64%) ≈ WPHE-10 (86.75%) > WPIE-0 (64.23%) ≈ WPHE-0 (60.62%). Our study provided valuable information about novel emulsifiers stabilizing delivery system to improve curcumin bioaccessibility.


Assuntos
Curcumina , Emulsões , Hidrolisados de Proteína , Ácido Succínico , Proteínas do Soro do Leite , Curcumina/química , Curcumina/metabolismo , Emulsificantes , Emulsões/química , Emulsões/metabolismo , Tamanho da Partícula , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Solubilidade , Ácido Succínico/química , Ácido Succínico/metabolismo , Proteínas do Soro do Leite/química , Proteínas do Soro do Leite/metabolismo
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