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1.
J Sci Food Agric ; 100(3): 1320-1327, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31742702

RESUMO

BACKGROUND: Potato protein hydrolysates (PPHs) were preparedwith Alcalase on intact potato protein isolates (PPI), with differenthydrolysis times (0.5-4 h), and functional and conformational properties of resultant hydrolysates were investigated. RESULTS: The degree of hydrolysis changed during incubation. Peptide bond cleavage increased and hydrolysis progressed rapidly. Gel electrophoresis showed that, by increasing the hydrolysis time, peptides with an apparent molecular weight below 20 kDa increased. It also revealed that, among potato protein components, patatin was more sensitive to Alcalase® hydrolysis than protease inhibitors. Enzymatic hydrolysis significantly enhanced the solubility and foam capacity of PPHs, but impaired foam stability (P < 0.05). Limited enzymatic hydrolysates (0.5PPH) at the interface improved the emulsion activity and stability index. These emulsions also had the smallest z-average and polydispersity index and showed the highest zeta potential. Fourier-transform infrared spectrometry (FTIR) analysis indicated extensive disruption of hydrogen bonds in PPHs, besides augmentation of α-helices and ß-turns, and a decline in the ß-sheets in the secondary structure of the PPHs was shown. CONCLUSION: Potato protein isolate, especially 0.5PPH, has good functional and conformational properties. Overall, our results provide new insights into the use of potato protein hydrolysates as a functional food component in the food industry. © 2019 Society of Chemical Industry.


Assuntos
Proteínas de Plantas/química , Solanum tuberosum/química , Subtilisinas/química , Biocatálise , Manipulação de Alimentos , Hidrólise , Peso Molecular , Peptídeos/química , Hidrolisados de Proteína/química , Solubilidade
2.
Food Chem Toxicol ; 135: 110932, 2020 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31682935

RESUMO

Immunomodulatory peptides with the sequences TSeMMM and SeMDPGQQ from selenium (Se)-enriched rice protein hydrolysates (SPHs) were identified in our previous study. We synthesized these two peptides to study whether they have neuroprotective effects on Pb2+-induced oxidative stress in mouse hippocampal HT22 cells, SPHs and a purified SPH fraction (SPHs-2) were used to compare the effects. Peptides pretreatments significantly suppressed Pb2+-induced cytotoxicity by increasing cell viability and decreasing cell apoptosis. TSeMMM and SeMDPGQQ reduced nitric oxide (NO) levels by 37.47% and 14.72% of Pb2+ group, as well as lactate dehydrogenase (LDH) release by 12.98% and 6.32% of Pb2+ group. TSeMMM and SeMDPGQQ could increase the activities of antioxidant enzymes; for example, the activity of superoxide dismutase (SOD) increased by 47.79% and 13.93%, respectively, and that of glutathione peroxidase (GSH-Px) increased by 94.7% and 78.73% of Pb2+ group. Additionally, nuclear factor erythroid 2-related factor (Nrf2) nuclear translocation and heme oxygenase 1 (HO-1) expression were triggered. These results suggest that TSeMMM and SeMDPGQQ can suppress oxidative damage caused by Pb2+; moreover, TSeMMM showed better neuroprotective potential than SeMDPGQQ.


Assuntos
Fármacos Neuroprotetores/farmacologia , Oligopeptídeos/farmacologia , Estresse Oxidativo/efeitos dos fármacos , Selenoproteínas/farmacologia , Animais , Apoptose/efeitos dos fármacos , Linhagem Celular , Sobrevivência Celular/efeitos dos fármacos , Chumbo/toxicidade , Camundongos , Fator 2 Relacionado a NF-E2/metabolismo , Óxido Nítrico/metabolismo , Oryza/química , Oxirredutases/metabolismo , Proteínas de Plantas/química , Hidrolisados de Proteína/química
3.
Food Chem ; 306: 125613, 2020 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-31610331

RESUMO

Reduction of bitter taste in protein hydrolysates is a challenging task. The aim of this study was to apply a simple two-step approach to prepare low bitter hydrolysates and investigate the influence of peptide modifications on taste characteristics. Protein hydrolysates were prepared from porcine muscle and plasma through simultaneous hydrolysis using endo- and exo-peptidases combined with peptide glycation by glucosamine (GlcN). Spectroscopic analysis and quantification of major alpha-dicarbonyl compounds (α-DCs) indicated the relatively low extent of Maillard reaction in GlcN-glycated protein hydrolysates. Thermal degradation of high MW peptides (>10 kDa) might play a major role in Maillard reaction, reflected by the formation of more Maillard reacted peptides (1-5 kDa), especially in plasma samples. Sensory evaluation indicated that glycation by GlcN can alter taste profiles of protein hydrolysates, which may be attributed to the formation of Maillard reacted peptides and peptide modifications revealed by LC-MS/MS analysis.


Assuntos
Exopeptidases/química , Músculo Esquelético/química , Paladar , Animais , Aspergillus oryzae/enzimologia , Exopeptidases/metabolismo , Glucosamina/química , Glucosamina/metabolismo , Glicosilação , Hidrólise , Reação de Maillard , Músculo Esquelético/metabolismo , Peptídeos/química , Peptídeos/metabolismo , Hidrolisados de Proteína/química , Suínos
4.
J Agric Food Chem ; 68(3): 759-768, 2020 Jan 22.
Artigo em Inglês | MEDLINE | ID: mdl-31841328

RESUMO

In this study, we investigated the antihypertensive effects in vitro and in vivo of novel angiotensin-converting enzyme inhibitory (ACEI) peptides purified and identified from bovine bone gelatin hydrolysate (BGH). Thirteen ACEI peptides were identified from BGH, and among which, RGL-(Hyp)-GL and RGM-(Hyp)-GF exhibited high ACE inhibition with IC50 values of 1.44 and 10.23 µM. Molecular docking predicted that RGM-(Hyp)-GF and ACE residues of Glu384, His513, and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99, and 2.42 + 3.0 Å. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03 + 1.93 Å. The maximal decrements in systolic blood pressure in spontaneously hypertensive rats induced by one-time gavage of RGL-(Hyp)-GL and RGM-(Hyp)-GF at 30 mg/kg were 31.3 and 38.6 mmHg. RGL-(Hyp)-GL had higher enzyme degradation resistance than that of RGM-(Hyp)-GF in vitro incubation in rat plasma, and they were sequentially degraded into pentapeptides and tetrapeptides within 2 h. Our results indicate that BGH can serve as a nutritional candidate to control blood pressure.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/química , Anti-Hipertensivos/química , Osso e Ossos/química , Gelatina/química , Peptídeos/química , Inibidores da Enzima Conversora de Angiotensina/administração & dosagem , Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Animais , Anti-Hipertensivos/administração & dosagem , Anti-Hipertensivos/isolamento & purificação , Pressão Sanguínea/efeitos dos fármacos , Bovinos , Humanos , Hipertensão/tratamento farmacológico , Hipertensão/fisiopatologia , Masculino , Simulação de Acoplamento Molecular , Peptídeos/administração & dosagem , Peptídeos/isolamento & purificação , Peptidil Dipeptidase A/química , Hidrolisados de Proteína/química , Ratos , Ratos Endogâmicos SHR
5.
J Sci Food Agric ; 100(1): 59-73, 2020 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-31435933

RESUMO

BACKGROUND: Jiuzao is the residue after Bajiu distillation which is usually used as forage for livestock. However, it is not fully utilized yet considering the content of protein remained. The present study aimed to isolate antioxidant peptides from Jiuzao protein hydrolysates, then add these peptides into Baijiu product to enhance the healthy value of Baiju. Meanwhile environmental pollution caused by massive Jiuzao can be mitigated indirectly. RESULTS: Four peptides Ala-Tyr-Ile(Leu) (AYI(L)) and Asp-Arg-Glu-Ile(Leu) (DREI(L)) were identified from Jiuzao protein hydrolysates, the extraction contents of AYI + AYL and DREI + DREL were 896.10 and 110.51 mg kg-1 Jiuzao, respectively. On the one hand, antioxidant activities of these peptides were investigated. For in vitro antioxidant assays, AYI, AYL and DREI exhibited strong capacities in oxygen radical absorbance capacity (ORAC) assay. Furthermore, three levels of four peptides were assessed by 2,2'-azobis(2-methylpropanimidamidine) (AAPH)-induced HepG2 cells model. The results showed that these peptides exerted a degree of antioxidant activities in cells. Meanwhile, selected peptides concentrations according to cell assays remined at effective doses after in vitro digestion. On the other hand, the influence of these four peptides on the characteristic aroma compounds in Baijiu was studied. Most characteristic aroma compounds releases were increased with the addition of peptides. CONCLUSION: In the study, antioxidant activities of peptides were evaluated, the feasibility of utilizing Jiuzao protein hydrolysates to obtain beneficial peptides was also proved. Healthy effect of Baijiu or other food can be increased by adding these functional substances. The findings might contribute to food application and Baijiu industries. © 2019 Society of Chemical Industry.


Assuntos
Antioxidantes/química , Peptídeos/química , Hidrolisados de Proteína/química , Resíduos/análise , Vinho/análise , Antioxidantes/farmacologia , Sobrevivência Celular/efeitos dos fármacos , Células Hep G2 , Humanos , Peptídeos/farmacologia , Hidrolisados de Proteína/farmacologia
6.
J Sci Food Agric ; 100(1): 50-58, 2020 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-31435937

RESUMO

BACKGROUND: Protein hydrolysate powder was prepared from non-penaeid shrimp (Acetes indicus) by enzymatic hydrolysis using Alcalase enzyme. Extraction conditions such as pH (6.5, 7.5 and 8.5), enzyme to substrate ratio (1.0, 1.5 and 2.0) and temperature (40, 50 and 60 °C) were optimized against the degree of hydrolysis using response surface methodology. RESULTS: Protein hydrolysate comprised of 740 g kg-1 protein, 150 g kg-1 ash and 90 g kg-1 fat contents. The amino acid score showed superior attributes with 56% essential amino acids. Furthermore, the functional properties of spray-dried protein hydrolysates were evaluated. Protein solubility was found to be the 90.20% at pH 2 and 96.92% at pH 12. Emulsifying properties were found to vary with the concentration of protein hydrolysates and the highest emulsifying capacity (26.67%) and emulsion stability (23.33%) were found at a concentration of 20 mg mL-1 . The highest and the lowest foaming capacity were observed at pH 6 and pH 10 with a concentration of 20 mg mL-1 . The water holding capacity of protein hydrolysate was found to increase with concentration, with a value of 5.4 mL g-1 at a concentration of 20 mg mL-1 . CONCLUSION: The results of the present study indicate that the use of A. indicus for the production of protein hydrolysate has good functional properties and nutritional value, rendering it suitable for broad industrial food applications. © 2019 Society of Chemical Industry.


Assuntos
Crustáceos/química , Proteínas de Frutos do Mar/química , Aminoácidos/análise , Animais , Biocatálise , Emulsões/química , Manipulação de Alimentos , Hidrólise , Valor Nutritivo , Hidrolisados de Proteína/química , Solubilidade , Subtilisinas/química
7.
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
8.
J Agric Food Chem ; 68(2): 623-632, 2020 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-31846317

RESUMO

The combined effects of succinic anhydride (SA) succinylation and linear dextrin (LD) glycation on whey protein hydrolysates (WPH) and their stabilized emulsions were evaluated. Degree of succinylation (DS), degree of glycation (DG), and degree of browning of samples suggested that a competitive displacement of reactive groups existed when WPH reacted with SA and LD in different orders. Attenuated total reflection Fourier transform infrared (ATR-FTIR) and far-UV circular dichroism (CD) indicated that the order of modification methods had a significant effect on secondary structures of WPH. Succinylation combined with glycation effectively reduced the surface hydrophobicity and increased the molecular flexibility of WPH. Meanwhile, the total free -SH content decreased, and the exposed free -SH content increased. Results of storage stability and gastrointestinal fate of the curcumin-loaded emulsion revealed that the modified WPH with higher DS was more effective for improving the curcumin bioaccessibility, while that with higher DG was more effective for enhancing the stability of the emulsion.


Assuntos
Curcumina/química , Anidridos Succínicos/química , Proteínas do Soro do Leite/química , Curcumina/metabolismo , Dextrinas/química , Emulsões/química , Trato Gastrointestinal/metabolismo , Glicosilação , Humanos , Interações Hidrofóbicas e Hidrofílicas , Hidrolisados de Proteína/química
9.
J Agric Food Chem ; 68(2): 541-548, 2020 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-31860295

RESUMO

Besides their nutritional value, whey protein (WP) peptides are food components retaining important pharmacological properties for controlling hypertension. We herein report how the use of complementary experimental and theoretical investigations allowed the identification of novel angiotensin converting enzyme inhibitory (ACEI) peptides obtained from a WP hydrolysate and addressed the rational design of even shorter sequences based on molecular pruning. Thus, after bromelain digestion followed by a 5 kDa cutoff ultrafiltration, WP hydrolysate with ACEI activity was fractioned by RP-HPLC; 2 out of 23 collected fractions retained ACEI activity and were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). In the face of 128 identified peptides, molecular docking was carried out to prioritize peptides and to rationally guide the design of novel shorter and bioactive sequences. Therefore, 11 peptides, consisting of 3-6 amino acids and with molecular weights in the range from 399 to 674 Da, were rationally designed and then purchased to determine the IC50 value. This approach allowed the identification of two novel peptides: MHI and IAEK with IC50 ACEI values equal to 11.59 and 25.08 µM, respectively. Interestingly, we also confirmed the well-known ACEI IPAVF with an IC50 equal to 9.09 µM. In light of these results, this integrated approach could pave the way for high-throughput screening and identification of new peptides in dairy products. In addition, the herein proposed ACEI peptides could be exploited for novel applications both for food production and pharmaceuticals.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/química , Peptídeos/química , Proteínas do Soro do Leite/química , Animais , Bovinos , Desenho de Drogas , Humanos , Cinética , Simulação de Acoplamento Molecular , Peso Molecular , Peptidil Dipeptidase A/química , Hidrolisados de Proteína/química
10.
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
11.
J Agric Food Chem ; 67(43): 11825-11838, 2019 Oct 30.
Artigo em Inglês | MEDLINE | ID: mdl-31588750

RESUMO

There is now great interest in food protein hydrolysates and food-derived peptides, because they may provide numerous health benefits. Among other foodstuffs, microalgae appear to be sustainable sources of proteins and bioactive peptides that can be exploited in foods and functional formulations. This review considers protein hydrolysates and individual peptides that may be relevant in cardiovascular disease prevention because they mimic the functions of mediators involved in pathologic processes that represent relevant risk factors for cardiovascular disease development, such as hypercholesterolemia, hypertension, diabetes, inflammation, and oxidative status. Some of these peptides are also multifunctional (i.e., they offer more than one benefit). Moreover, the most efficient techniques for protein extraction and hydrolyzation are commented on, as well as the best methodologies for high-throughput detection and quantification. Finally, current challenges and critical issues are discussed.


Assuntos
Doenças Cardiovasculares/tratamento farmacológico , Microalgas/química , Peptídeos/administração & dosagem , Animais , Humanos , Peptídeos/química , Peptídeos/isolamento & purificação , Hidrolisados de Proteína/química
12.
J Agric Food Chem ; 67(43): 11948-11954, 2019 Oct 30.
Artigo em Inglês | MEDLINE | ID: mdl-31577435

RESUMO

Corn gluten hydrolysate (CGH) was prepared by food-grade bacterial proteases, alcalase and neutral protease. Digestion of CGH with carboxypeptidase A and leucine aminopeptidase extensively changed the elution patterns of peptides as observed from reversed phase high performance liquid chromatography-mass spectrometry (LC-MS), whereas digestion with pepsin and trypsin hardly affected the elution patterns. Twenty-five major peptides in CGH were identified. After digestion with exopeptidases, only prolyl dipeptides and pyroglutamyl di- and tripeptides remained, whereas the other 17 peptides completely disappeared. On the other hand, all 25 peptides remained after digestion with pepsin and trypsin. These facts suggest that a majority of short-chain peptides in food protein hydrolysates are degraded by exopeptidases during digestion and absorption processes. Thus, susceptibility to exopeptidases should be considered for prediction of bioactive peptide upon ingestion, which has not been considered in most of previous studies on food-derived bioactive peptides.


Assuntos
Proteínas de Bactérias/química , Glutens/química , Peptídeo Hidrolases/química , Peptídeos/química , Zea mays/química , Bacillus/enzimologia , Biocatálise , Exopeptidases/química , Espectrometria de Massas , Hidrolisados de Proteína/química
13.
J Dairy Sci ; 102(12): 10711-10723, 2019 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-31548055

RESUMO

The objective of this work was to obtain casein hydrolysates with aspartic proteinases present in extracts from the artichoke flower (Cynara scolymus L.) and evaluate their antioxidant, antimicrobial, and angiotensin-I converting enzyme (ACE) inhibitory activity in vitro. The casein hydrolysates produced by the action of C. scolymus had elevated antihypertensive and antioxidant activity due to their high hydrophobic peptide content (93.84, 96.58, and 90.54% at 2, 4, and 16 h of hydrolysis, respectively). Hydrolysis time and molecular weight (<3 kDa) had a significant influence on the hypertensive and antioxidant activity of the hydrolysates, which were greater at hydrolysis times of 4 and 16 h and corresponding to the <3 kDa fractions. The <3 kDa fraction of the 16 h hydrolysate had an ACE inhibitory activity with a half-maximal inhibitory concentration (IC50) of 71.77 µg peptides per mL; DPPH and ABTS•+ radical scavenging activities of 6.27 µM and 6.21 mM Trolox equivalents per mg of peptides, respectively; and iron (II) chelation activity with an IC50 of 221.49 µg of peptides per mL. Antimicrobial activity against Enterococcus faecalis was also observed in the hydrolysates. From the peptide sequences identified in the hydrolysates, we detected 22 peptides (from the BIOPEP database) that were already in their bioactive form (AMKPWIQPK, AMKPWIQPKTKVIPYVRYL, ARHPHPHLSFM, DAQSAPLRVY, FFVAPFPEVFGK, GPVRGPFPII, KVLPVPQK, LLYQEPVLGPVRGPFPIIV, MAIPPKKNQDK, NLHLPLPLL, PAAVRSPAQILQ, RELEELNVPGEIVESLSSSEESITR, RPKHPIKHQ, RPKHPIKHQGLPQEVLNENLLRF, SDIPNPIGSENSEK, TPVVVPPFLQP, VENLHLPLPLL, VKEAMAPK, VLNENLLR, VYPFPGPIH, VYQHQKAMKPWIQPKTKVIPYVRY, VYQHQKAMKPWIQPKTKVIPYVRYL) and are reported to display antioxidant, antimicrobial, and ACE inhibitory activity. We also identified 12,116, 14,513, and 25,169 peptide sequences in the hydrolysates at 2, 4, and 16 h, respectively, that were contained in the primary sequence, and these are reported to display ACE inhibitory, antioxidant, dipeptidyl peptidase IV inhibition, antithrombotic, opioid, immunomodulation, antiamnesic, anticancer, chelating, and hemolytic bioactivity.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Anti-Infecciosos/farmacologia , Antioxidantes/farmacologia , Caseínas/farmacologia , Cynara scolymus/enzimologia , Peptídeo Hidrolases/metabolismo , Hidrolisados de Proteína/farmacologia , Inibidores da Enzima Conversora de Angiotensina/química , Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Animais , Anti-Infecciosos/isolamento & purificação , Anti-Hipertensivos/isolamento & purificação , Anti-Hipertensivos/farmacologia , Antioxidantes/química , Caseínas/isolamento & purificação , Bovinos , Peso Molecular , Hidrolisados de Proteína/química , Hidrolisados de Proteína/isolamento & purificação
14.
J Dairy Sci ; 102(12): 10748-10759, 2019 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-31548068

RESUMO

Novel bioactive peptides from camel milk protein hydrolysates (CMPH) were identified and tested for inhibition of cholesterol esterase (CEase), and their possible binding mechanisms were elucidated by molecular docking. Papain-generated CMPH showed the highest degree of hydrolysis. All CMPH produced upon enzymatic degradation demonstrated a dramatic enhancement of CEase inhibition compared with intact camel milk proteins, with papain-generated hydrolysate P9 displaying the highest inhibition. Peptide identification and their modeling through PepSite 2 revealed that among 20 potential bioactive peptides in alcalase-generated hydrolysate A9, only 3 peptides, with sequences KFQWGY, SQDWSFY, and YWYPPQ, showed the highest binding toward CEase catalytic sites. Among 43 peptides in 9-h papain-generated hydrolysate P9, 4 peptides were found to be potent CEase inhibitors. Molecular docking revealed that WPMLQPKVM, CLSPLQMR, MYQQWKFL, and CLSPLQFR from P9 hydrolysates were able to bind to the active site of CEase with good docking scores and molecular mechanics-generalized born surface area binding energies. Overall, this is the first study reporting CEase inhibitory potential of peptides generated from milk proteins.


Assuntos
Camelus , Inibidores Enzimáticos/isolamento & purificação , Proteínas do Leite/química , Peptídeos/química , Esterol Esterase/antagonistas & inibidores , Animais , Camelus/metabolismo , Inibidores Enzimáticos/química , Feminino , Leite/química , Simulação de Acoplamento Molecular , Papaína/química , Peptídeos/isolamento & purificação , Hidrolisados de Proteína/química , Subtilisinas/química
15.
J Agric Food Chem ; 67(37): 10313-10320, 2019 Sep 18.
Artigo em Inglês | MEDLINE | ID: mdl-31502448

RESUMO

A peptide fraction with molecular masses below 3 kDa (PSH-3 kDa) from a peach seed hydrolysate demonstrated high angiotensin converting enzyme (ACE) inhibitory activity (concentration to inhibit 50% ACE (IC50) = 16.4 µg/mL) in our previous work. This work proposes a further study of this highly active fraction. RP-HPLC enabled two fractions (F3 and F4) with high inhibitory activity (IC50 = 2.0 ± 0.5 and 1.2 ± 0.2 µg/mL, respectively) to be isolated. Peptide analysis by LC-Q-TOF-MS/MS using reverse-phase and hydrophilic interaction chromatography enabled 33 peptides within both fractions to be identified. Among them, peptide isoleucine-tyrosine-serine-proline-histidine (IYSPH) showed the highest capacity. The lack of cytotoxicity of peptides was demonstrated in three different cell lines (HeLa, HT-29, and HK-2). Oral administration of PSH-3 kDa fraction or peptide IYSPH caused a significant systolic blood pressure reduction (-30 mmHg) on spontaneously hypertensive rats after 3-6 h treatment.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/administração & dosagem , Inibidores da Enzima Conversora de Angiotensina/química , Anti-Hipertensivos/administração & dosagem , Anti-Hipertensivos/química , Hipertensão/tratamento farmacológico , Extratos Vegetais/administração & dosagem , Extratos Vegetais/química , Prunus persica/química , Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Animais , Anti-Hipertensivos/isolamento & purificação , Pressão Sanguínea/efeitos dos fármacos , Humanos , Hipertensão/enzimologia , Hipertensão/fisiopatologia , Masculino , Peptidil Dipeptidase A/metabolismo , Extratos Vegetais/isolamento & purificação , Hidrolisados de Proteína/química , Ratos , Ratos Endogâmicos SHR , Sementes/química
16.
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
17.
Molecules ; 24(16)2019 Aug 19.
Artigo em Inglês | MEDLINE | ID: mdl-31430869

RESUMO

Protein hydrolysates from fish by-products have good process suitability and bioavailability in the food industry. The objective of this work was to develop a method for protein recovery from fish scales and evaluate the hydrolysis of the scale protein. The effect of the hydrothermal process on protein recovery, degree of hydrolysis (DH) and structural properties of the hydrolysates was investigated. Results showed that hydrothermal treatment could enhance protein recovery of tilapia scales without demineralization and dramatically improve the DH of the hydrolysates. The hydrothermal treated scales showed a better protein recovery (84.81%) and DH (12.88%) and released peptides more efficiently than that of the conventional treated samples. The obtained gelatin hydrolysates mainly distributed in the range of 200-2000 Da with an angiotensin I-converting enzyme (ACE) IC50 value of 0.73 mg/mL. The ACE inhibitory activity of gelatin hydrolysates was stable under high temperature, pH and gastrointestinal proteases. Hydrothermal treatment followed by enzymatic hydrolysis offers a potential solution for preparation of gelatin hydrolysates for food ingredients from fish processing by-products.


Assuntos
Peixes/metabolismo , Gelatina/química , Hidrolisados de Proteína/química , Inibidores da Enzima Conversora de Angiotensina/química , Animais , Hidrólise , Peptídeo Hidrolases/química , Peptídeos/química , Peptidil Dipeptidase A/metabolismo
18.
Molecules ; 24(16)2019 Aug 19.
Artigo em Inglês | MEDLINE | ID: mdl-31430953

RESUMO

Schizochytrium limacinum residue was hydrolyzed with various proteases (papain, trypsin, Flavourzyme, Protamex, and Alcalase 2.4L) to obtain antioxidative peptides. The results showed that the S. limacinum hydrolysates (SLHs) prepared with compound proteases (Protamex and Alcalase 2.4L) had the highest antioxidant activity, which was measured using methods such as 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging ability (IC50 = 1.28 mg/mL), hydroxyl radical scavenging ability (IC50 = 1.66 mg/mL), and reducing power (1.42 at 5.0 mg/mL). The hydrolysates were isolated and purified by ultrafiltration, gel filtration chromatography, and reverse-phase high-performance liquid chromatography (RP-HPLC). Through analysis of electrospray ionization-mass spectrometer (ESI-MS/MS), the purified antioxidant peptide was identified as Pro-Tyr-Lys (406 Da). Finally, the identified peptide was synthesized for evaluating its antioxidant activity. The •OH scavenging ability and reducing power of Pro-Tyr-Lys were comparable to those of reduced L-glutathione (GSH). These results demonstrated that the antioxidant peptides from SLHs could potentially be used as effective antioxidants.


Assuntos
Antioxidantes/química , Microalgas/química , Peptídeos/química , Hidrolisados de Proteína/química , Compostos de Bifenilo/química , Depuradores de Radicais Livres/química , Glutationa/química , Hidrólise , Radical Hidroxila/química , Peroxidação de Lipídeos , Peptídeo Hidrolases/química , Picratos/química , Espectrometria de Massas por Ionização por Electrospray , Superóxidos/química
19.
J Agric Food Chem ; 67(36): 10195-10206, 2019 Sep 11.
Artigo em Inglês | MEDLINE | ID: mdl-31436982

RESUMO

Pea protein hydrolysate (PPH) is successfully conjugated with gum arabic (GA) through Maillard-driven chemistry. The effect of cross-linking conjugation on the structure, solubility, volatile substances, emulsification, and antioxidative activity of glyco-PPH is investigated, and found to improve all properties. The formation of glyco-PPH is confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier-transform infrared (FTIR), and scanning electron microscopy (SEM). Size exclusion chromatography-multi angle light scattering (SEC-MALS) unveils that the maximum molecular mass of glyco-PPH occurs after 1 day of conjugation and approximately 1.2 mol of gum arabic conjugates on one mole of PPH. Headspace solid-phase microextraction gas chromatography-mass spectrometry (HS-SPME-GC-MS) reveals the odor changes of glycoprotein before and after cross-linking. We have also prepared oil-in-water emulsions using glyco-PPH, which have enhanced physical stability against pH changes and chemical stability against lipid oxidation. The mechanism proposed involves Maillard-driven synthesis of the cross-linked PPH-GA conjugates, which increase the surface hydrophilicity and steric hindrance of glyco-PPH. These findings could provide a rational foundation for tailoring the physicochemical properties and functionalities of plant-based protein, which are attractive for food and functional materials applications.


Assuntos
Aromatizantes/síntese química , Goma Arábica/química , Proteínas de Ervilha/química , Antioxidantes/química , Emulsões/química , Aromatizantes/química , Interações Hidrofóbicas e Hidrofílicas , Reação de Maillard , Hidrolisados de Proteína/química , Solubilidade
20.
Food Chem ; 301: 125222, 2019 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-31382108

RESUMO

Collagen hydrolysates (peptides) derived from food processing byproducts have been used to produce commercially valuable food ingredients due to their potential to trigger certain desirable physiological responses in the body. Low-molecular-weight (LMW) collagen hydrolysates are generally thought to exert better bioactivities than their larger counterparts. However, the preparation of LMW collagen hydrolysates is often impeded by their special structure, cross-linking, and hydroxyproline. This review briefly introduces the motivation of the food industry to prepare LMW collagen hydrolysate from food processing byproducts. We further summarize recent progress on the preparation of LMW collagen hydrolysates and methods to determine the molecular weight. We then discuss the challenges and then provide perspectives on future directions in preparing LMW collagen hydrolysates.


Assuntos
Colágeno/química , Indústria de Processamento de Alimentos/métodos , Hidrolisados de Proteína/química , Animais , Hidroxiprolina/química , Peso Molecular , Peptídeos/química
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