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1.
Food Chem ; 343: 128417, 2021 May 01.
Artigo em Inglês | MEDLINE | ID: mdl-33406574

RESUMO

This study aimed to investigate the structural and antimicrobial properties of Maillard reaction products (MRPs) in chicken liver protein (CLP) and its hydrolysate (CLPH) after sonication (SCLPH). The MRPs of CLP (CLPM), CLPH (CLPHM) and SCLPH (SCLPHM) were analyzed by several spectrometric techniques. The molecular weights of the CLPHM and SCLPHM were primarily between 1.35 kDa and 17 kDa. Moreover, the molecular weights in the CLPHM and SCLPHM below 1.35 kDa were increased, which indicated that cross-linking and thermal degradation occurred during the Maillard reaction (MR). The SCLPHM showed an obvious network skeleton, and the surface had many small crystal-shaped particles after ultrasound treatment and MR by scanning electron microscopy. The SCLPHM had more negative charges than the CLPHM, thus effectively inhibiting the growth of S. saprophyticus and E. coli. MR and ultrasound treatment could be a promising technology to expand the application prospects of low-value meat byproducts.


Assuntos
Antibacterianos/química , Fígado/metabolismo , Hidrolisados de Proteína/química , Animais , Antibacterianos/farmacologia , Galinhas , Escherichia coli/efeitos dos fármacos , Reação de Maillard , Peso Molecular , Hidrolisados de Proteína/farmacologia , Sonicação , Staphylococcus saprophyticus/efeitos dos fármacos , Temperatura de Transição
2.
Food Chem ; 339: 128159, 2021 Mar 01.
Artigo em Inglês | MEDLINE | ID: mdl-33152898

RESUMO

During production in Chinese baijiu fermentation process, huge amounts of the by-product vinasse are generated and generally utilized as low-value animal feed. We applied alkaline extraction in combination with ultrasonication to recover vinasse proteins, which were then hydrolyzed by complex protease Corolase PP for 8 h to obtain peptide fractions (VPH-1, -2, -3) displaying high DPPH radical scavenging activity. VPH-3 (<3 kDa) separated by ultrafiltration had EC50 values lower than those of VPH-1 and -2 for reactive oxygen species (ROS) and reactive nitrogen species (RNS) radicals, and significantly inhibited production of NO and pro-inflammatory cytokines in LPS-stimulated RAW264.7 macrophage cells. Active peptides and their amino acid sequences were identified by LC-MS/MS analysis, and five synthesized peptides (particularly KLPDHPKLPK and VDVPVKVPYS) displayed strong anti-inflammatory activity at concentration 0.25 mg/mL. These findings will be useful in future commercial development of baijiu vinasse, including application as a new source of bioactive peptides.


Assuntos
Bebidas Alcoólicas , Anti-Inflamatórios não Esteroides/farmacologia , Antioxidantes/farmacologia , Peptídeos/farmacologia , Animais , Anti-Inflamatórios não Esteroides/química , Antioxidantes/química , Cromatografia Líquida , Avaliação Pré-Clínica de Medicamentos , Hidrólise , Camundongos , Peptídeos/análise , Peptídeos/química , Proteínas de Plantas/análise , Proteínas de Plantas/farmacologia , Hidrolisados de Proteína/análise , Hidrolisados de Proteína/química , Hidrolisados de Proteína/farmacologia , Células RAW 264.7 , Espécies Reativas de Oxigênio , Espectrometria de Massas em Tandem
3.
Food Chem ; 340: 127876, 2021 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-32871354

RESUMO

Jackfruit is a sweet tropical fruit with very pleasant aroma, and the ripe seeds are edible. In this study, jackfruit seed proteins were isolated and subjected to trypsin digestion. The resultant protein hydrolysate was then subjected to antioxidant assay-guided purification, using centrifugal filtration, C18 reverse-phase and strong cation exchange (SCX) fractionations. The purified SCX fraction was further analyzed by de novo peptide sequencing, and two peptide sequences were identified and synthesized. Peptide JFS-2 (VGPWQK) was detected with antioxidant potential, with EC50 value comparable to that of commercial GSH antioxidant peptide. Additionally, the identified peptides were tested with protein protection potential, in an albumin protein denaturation inhibitory assay. Concurrently, we also investigated the pH, temperature, and gastrointestinal-digestion stability profiles for the identified peptide. With further research efforts, the identified peptides could potentially be developed into preservative agent for protein-rich food systems or as health-promoting diet supplements.


Assuntos
Antioxidantes/análise , Artocarpus/química , Peptídeos/análise , Peptídeos/química , Hidrolisados de Proteína/química , Sementes/química , Antioxidantes/química , Cromatografia por Troca Iônica , Digestão , Conservantes de Alimentos , Concentração de Íons de Hidrogênio , Peptídeos/metabolismo , Temperatura , Tripsina
4.
Food Chem ; 337: 128069, 2021 Feb 01.
Artigo em Inglês | MEDLINE | ID: mdl-32950762

RESUMO

Selective enrichment of the highly active antioxidant peptides is required as the lack of an efficient method leads to long screening processes, hampering the research of antioxidant peptides. A simple synthetic metal-organic framework MIL-53 (Cr) was initially applied to extract specific antioxidant peptides from rice dreg protein hydrolysate. The highest active fraction was further purified by reversed-phase high-performance liquid chromatography. The antioxidant peptides with the highest antioxidant activities were identified as Gly-Asp-Met-Asn-Pro and Leu-Leu-Leu-Arg-Trp by LC-MS. These two peptides were synthesized and also exhibited good scavenging activity on the DPPH free radical, superoxide anion free radical and hydroxyl radical, and good chelating ability on Fe2+. The results confirmed that the angling method was effective for antioxidant peptide enrichment from protein hydrolysates.


Assuntos
Antioxidantes/química , Oryza/química , Peptídeos/química , Proteínas de Plantas/química , Hidrolisados de Proteína/química , Cromatografia Líquida , Espectrometria de Massas
5.
Food Chem ; 331: 127216, 2020 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-32650230

RESUMO

The effects of ultrasound working modes using multi-mode S-type ultrasound on the preparation of bioactive peptide from rice protein (RP) were studied with the ACE inhibitory activity of protein-hydrolysate after gastrointestinal simulated digestion as the index. The structure characterizations of protein and enzymolysis products were also studied. Results showed that all the ultrasound working modes pretreatment increased the ACE inhibitory activity significantly (p < 0.05) and 20/40 kHz dual-frequency ultrasound showed the most significant impact, which increased by 38.28% and 27.47% compared to control and ultrasound cleaning machine, respectively. After pretreated by 20/40 kHz dual-frequency ultrasound, the soluble and hydrophobic protein contents, free sulfhydryl content and surface hydrophobicity of RP increased. And the peptide content and hydrophobic amino acid content of protein-hydrolysate after gastrointestinal simulated digestion showed higher value (p < 0.05). In conclusion, the multi-mode S-type ultrasound pretreatment is an effective way in preparation of ACE inhibitory peptide from RP.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/metabolismo , Oryza/metabolismo , Peptídeos/metabolismo , Peptidil Dipeptidase A/metabolismo , Proteínas de Plantas/metabolismo , Inibidores da Enzima Conversora de Angiotensina/química , Interações Hidrofóbicas e Hidrofílicas , Peptídeos/química , Peptidil Dipeptidase A/química , Proteínas de Plantas/química , Ligação Proteica , Hidrolisados de Proteína/química , Sonicação , Propriedades de Superfície
6.
J Food Sci ; 85(7): 1988-1996, 2020 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-32602184

RESUMO

The effects of adding bovine skin gelatin hydrolysate obtained with subtilisin, on water-holding capacity (WHC), in a thermally processed chicken meat model, were investigated. Hydrolysates with different degrees of hydrolysis (DH) (6.57%, 13.14%, and 26.28%) were prepared. The results showed that all the tested hydrolysates improved water retention in the meat matrix. The hydrolysate with 26.28% DH showed similar behavior throughout the full range of concentrations [0% to 5% w/w] compared to that of the positive control (sodium tripolyphosphate [STPP]). In addition, the other hydrolysates [6.57% DH and 13.14% DH at 3% and 2.5% w/w concentrations, respectively] showed behaviors that coincided with that of STPP at its maximum limit allowed. A correlation was observed between the WHC and the pH of the meat samples treated with each hydrolysate or STPP. In addition, it was found that the WHC of the hydrolysates was due to increases in pH and the specific effects of the hydrolysate beyond the typical effects of pH and ionic strength in meat systems. The solubility of all hydrolysates was high (>90%). In conclusion, bovine skin gelatin hydrolysates could serve as an alternative to polyphosphates to improve water retention and the functional properties of thermally processed meat products. PRACTICAL APPLICATION: This study investigated the effects of adding bovine skin gelatin hydrolysate obtained with subtilisin on water-holding capacity (WHC) in a thermally processed chicken meat model. It was found that the hydrolysis of bovine skin gelatin with subtilisin can replace chemical products harmful to health, such as STPP, in terms of water-holding capacity. Therefore, bovine skin gelatin hydrolysate can be used as an ingredient in the formulation of thermally processed meat products.


Assuntos
Gelatina/química , Polifosfatos/química , Pele/química , Animais , Bovinos , Temperatura Alta , Concentração de Íons de Hidrogênio , Hidrólise , Hidrolisados de Proteína/química , Solubilidade , Água/química
7.
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
8.
Food Chem ; 331: 127369, 2020 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-32590262

RESUMO

To make better use of chicken liver, a byproduct of meat processing with rich proteins, the influence of ultrasound pretreatment on the extent of Maillard reaction (MR) and the properties of MR products (MRPs) of chicken liver protein (CLP) and its hydrolysate (CLPH) were investigated. The extent of MR of sonicated CLPH (SCLPHMs) was significantly higher than that of the other two MRPs. The decreased fluorescence intensity (FI) of the SCLPHMs indicated adequate reaction of d-xylose with sonicated CLPH (SCLPH). The particle size of the three MRPs was significantly larger than that of CLP, CLPH, and SCLPH, respectively. Ultrasound treatment increased the utilization of amino acids and enriched the variety of volatile compounds in all groups. Furfural was the main heterocyclic compound in the MRPs. Therefore, ultrasound pretreatment and enzymolysis of chicken liver may be a foundation for high-value development in flavors for the food industry.


Assuntos
Galinhas , Indústria de Processamento de Alimentos/métodos , Fígado/química , Reação de Maillard , Proteínas de Aves Domésticas/química , Compostos Orgânicos Voláteis/química , Aminoácidos/análise , Aminoácidos/química , Animais , Aromatizantes/química , Produtos Finais de Glicação Avançada/química , Produtos Avícolas , Hidrolisados de Proteína/química , Paladar , Ultrassom , Compostos Orgânicos Voláteis/análise , Xilose/química
9.
Food Chem ; 331: 127350, 2020 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-32590267

RESUMO

Fish by-products are excellent sources of collagen. Acid-soluble collagen (ASC) derived from a mixed by-product of different fish species was hydrolyzed to obtain peptide fractions and evaluate their biological and functional activities. All fractions obtained (F1: ≥30, F2: 10-30, F3: 5-10, F4: 1-5, and F5: ≤1kDa) exhibited antioxidant activity at concentrations of 5, 10, and 15 mg/mL. However, F5 registered the highest reducing power (absorbance 0.366) and hydroxyl-radical-scavenging activity (91%) at 15 mg/mL; whereas the highest DPPH scavenging activity (81%) was also detected in F5 at 5 mg/mL. The solubility of F1, F2, and F3 was ≥ 95% at pH 7. The highest foaming capacity (78%), foaming stability (60%), and emulsion stability index (42 min) were registered for F1. However, the highest emulsifying activity index (130 m2/g) was for F3. These results place collagen obtained from a mixed by-product of different fish species as a potential biotechnological alternative for the industry.


Assuntos
Antioxidantes/farmacologia , Colágeno/química , Produtos Pesqueiros , Proteínas de Peixes/química , Peptídeos/química , Peptídeos/farmacologia , Aminoácidos/análise , Animais , Antibacterianos/química , Antibacterianos/farmacologia , Antioxidantes/química , Emulsificantes/química , Proteínas de Peixes/farmacologia , Depuradores de Radicais Livres/química , Concentração de Íons de Hidrogênio , Hidrólise , Radical Hidroxila/química , Hidrolisados de Proteína/química , Solubilidade
10.
Curr Pharm Biotechnol ; 21(12): 1249-1258, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32370711

RESUMO

BACKGROUND: Fish is an essential source of nutrients for human nutrition due to the composition of proteins, vitamins, and minerals, among other nutrients. Enzymatic hydrolysis represents an alternative for the use of by-products of the aquaculture industry. OBJECTIVE: We propose to evaluate the effect of stirring speed, temperature, and initial protein concentration on the degree of hydrolysis of proteins and antioxidant activity of red tilapia (Oreochromis spp.) viscera hydrolysates. METHODS: The effect of stirring speed, temperature, and initial protein concentration on the degree of hydrolysis of proteins and antioxidant activity was evaluated using an experimental design that was adjusted to a polynomial equation. The hydrolysate was fractioned to determine the antioxidant activity of the fractions, and functional properties were also measured. RESULTS: Stirring speed and protein concentration presented a statistically significant effect (p <0.05) on all the response variables. However, the temperature did not present a statistically significant effect on the degree of hydrolysis. DISCUSSION: The best conditions of hydrolysis were stirring speed of 51.44 rpm, a temperature of 59.15°C, and the protein concentration of 10 g L-1. The solubility of the hydrolysate protein was high at different pH, and the hydrolysate fraction with the highest antioxidant activity has a molecular weight <1 kDa. CONCLUSION: The degree of hydrolysis and the biological activity of red tilapia viscera hydrolysates (Oreochromis spp.) are affected by temperature, substrate concentration, and stirring speed. The optimal conditions of hydrolysis allowed to obtain a hydrolysate with antioxidant activity are due to the peptides with low molecular weight.


Assuntos
Antioxidantes/análise , Hidrolisados de Proteína/química , Subtilisinas/metabolismo , Tilápia/crescimento & desenvolvimento , Vísceras/química , Animais , Pesqueiros , Humanos , Hidrólise , Peso Molecular , Peptídeos/química , Reciclagem , Solubilidade , Temperatura , Vísceras/enzimologia , Resíduos
11.
J Food Sci ; 85(6): 1735-1741, 2020 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-32468582

RESUMO

In this study, the antioxidant activity of mungbean protein hydrolysate (MPH) was systematically investigated. MPH was fractionated by ultrafiltration into two major fractions (MPH-1 <3 kDa, MPH-2 >3 kDa). Fraction MPH-1, which exhibited the highest antioxidant activity, was further fractionated by gel column into three fractions (MPH-1A, MPH-1B, and MPH-1C). The antioxidant activity of the MPH-1B fraction was stronger than that of the other fractions. Eight mungbean peptides (P1-P8) were identified in fraction MPH-1B by UPLC-Q-TOF-MS. Among them, peptides Trp-Gly-Asn (WGN, P2), Ala-Trp (AW, P4), Arg-Gly-Trp-Tyr-Glu (RGWYE, P5), and Gly-Val-Pro-Phe-Trp (GVPFW, P7) had high antioxidant activity. Moreover, these four peptides exerted protective effects against H2 O2 -induced cytotoxicity and regulated the MDA content, CAT activity, and total GSH content in HepG2 cells with specific observation. This study demonstrated the potential of MPH as a source of antioxidant peptides. This provides a scientific basis for the preparation of antioxidant peptides from mungbean protein. PRACTICAL APPLICATION: This study demonstrated the potential of the hydrolysate of mungbean protein as a source of antioxidant peptides and provided a scientific basis for the preparation of antioxidant peptides from mungbean protein.


Assuntos
Antioxidantes/química , Antioxidantes/farmacologia , Proteínas de Plantas/química , Vigna/química , Sequência de Aminoácidos , Animais , Antioxidantes/isolamento & purificação , Sobrevivência Celular/efeitos dos fármacos , Células Hep G2 , Humanos , Peptídeos/química , Proteínas de Plantas/farmacologia , Hidrolisados de Proteína/química , Hidrolisados de Proteína/farmacologia
12.
Food Chem ; 328: 127135, 2020 Oct 30.
Artigo em Inglês | MEDLINE | ID: mdl-32473490

RESUMO

Watermelon seed, a watermelon processing industry by-product, is a good protein source for the preparation of antioxidant peptides due to its high protein content, low cost, special amino acid composition. Antioxidant hydrolysates obtained from watermelon seed protein (WSP) after slit divergent ultrasound (SDU) treatment were studied. The stepwise multiple linear regression model verified that the reducing power of watermelon seed protein hydrolysates (WSPHs) is positively related with -SH and ß-turn content of WSP (R2 = 0.931, p < 0.01). Using the degree of hydrolysis (DH) and reducing power as indicators, the WSPHs was prepared under the optimal conditions (ultrasound frequency: 20/28 kHz, time: 60 min, power density: 100 W/L) and divided into three components by ultrafiltration membrane (1 and 5 kDa). Compared with WSPHs and other fractions, WSPHs-I (Mw < 1 kDa) not only significantly protected HepG2 cells from H2O2-induced damage, but also greatly alleviated the liver injury caused by d-galactose in male SD rats.


Assuntos
Antioxidantes/farmacologia , Citrullus/química , Hidrolisados de Proteína/química , Hidrolisados de Proteína/farmacologia , Animais , Antioxidantes/química , Antioxidantes/metabolismo , Doença Hepática Induzida por Substâncias e Drogas/tratamento farmacológico , Enzimas/metabolismo , Galactose/toxicidade , Células Hep G2 , Humanos , Peróxido de Hidrogênio/farmacologia , Hidrólise , Modelos Lineares , Masculino , Proteínas de Plantas/química , Proteínas de Plantas/farmacologia , Ratos Sprague-Dawley , Sementes/química , Ultrassom/instrumentação , Ultrassom/métodos
13.
Poult Sci ; 99(5): 2819-2832, 2020 May.
Artigo em Inglês | MEDLINE | ID: mdl-32359619

RESUMO

Our patented protease A-digested crude chalaza hydrolysates (CCH) show antioxidant abilities in vitro. The prophylactic effects of CCH on cognitive dysfunction and brain oxidative damages were investigated via a D-galactose (DG)-injected mouse model in this study. Fifty-four mice were randomly divided into the following: (1) CON, 0.1 mL 0.9% saline (subcutaneous injection [SC] on the back)+distilled water (oral gavage); (2) DG, 100 mg/kg BW/day D-galactose (Bio-Serv Co., Flemington, NJ, USA) (SC on the back)+distilled water (oral gavage); (3) DG_LCH, 100 mg/kg BW/day D-galactose (SC on the back) + 50 mg CCH/kg BW/day in 0.1 ml distilled water (oral gavage); (4) DG_MCH, 100 mg/kg BW/day D-galactose (SC on the back) + 100 mg CCH/kg BW/day (oral gavage); (5) DG_HCH, 100 mg/kg BW/day D-galactose (SC on the back) + 200 mg CCH/kg BW/day (oral gavage); (6) DG_AG, 100 mg/kg BW/day D-galactose (SC on the back) + 100 mg aminoguanidine hydrochloride/kg BW/day (oral gavage). The experiment lasted for 84 D. CCH, containing antioxidant-free amino acids and anserine, restored (P < 0.05) DG-injected memory injury in the Morris water maze test and attenuated the neuronal degenerations and nucleus shrinkages in the dentate gyrus area. CCH supplementation also reduced amyloid ß-peptide protein levels and accumulation of advanced glycation end products (AGE) in the brain of DG-injected mice, whereas the brain antioxidant capacity was reversed (P < 0.05) by supplementing CCH. Furthermore, AGE receptor (RAGE), NFκb, IL-6, and TNF-α gene expressions were downregulated (P < 0.05) by supplementing CCH. Therefore, CCH show prophylactic effects on the development of oxidative stress-induced cognitive dysfunction.


Assuntos
Disfunção Cognitiva/tratamento farmacológico , Gema de Ovo/química , Hipocampo/efeitos dos fármacos , Neurônios/efeitos dos fármacos , Estresse Oxidativo/efeitos dos fármacos , Substâncias Protetoras/farmacologia , Animais , Anserina/análise , Anti-Inflamatórios/metabolismo , Antioxidantes/metabolismo , Carnosina/análise , Galinhas , Hipocampo/fisiologia , Aprendizagem/efeitos dos fármacos , Masculino , Aprendizagem em Labirinto , Memória/efeitos dos fármacos , Camundongos , Camundongos Endogâmicos ICR , Hidrolisados de Proteína/química
14.
Food Chem ; 327: 127059, 2020 Oct 15.
Artigo em Inglês | MEDLINE | ID: mdl-32447138

RESUMO

The aim of this study was to purify and identify antioxidant peptides from watermelon seed protein hydrolysates (WSPHs-I: Mw < 1 kDa) and further evaluate their cytoprotective effects against H2O2-induced oxidative stress in HepG2 cells. After purification by Sephadex G-15 and semi-preparative reversed-phase high performance liquid chromatography (RP-HPLC), five peptides, RDPEER (P1), KELEEK (P2), DAAGRLQE (P3), LDDDGRL (P4), and GFAGDDAPRA (P5) were sequenced by LC-MS/MS and synthesized with solid-phase synthesis method. These peptides showed desirable 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity (IC50: 0.216 ± 0.01-0.435 ± 0.03), 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging capacity (IC50: 0.54 ± 0.02-1.23 ± 0.03), and oxygen radical absorbance capacity (ORAC) (82.36 ± 1.2-130.67 ± 2.2 µM TE/mg). Among them, peptide P1 exhibited the strongest antioxidant capacity. Moreover, the results suggested that peptide P1 may protect HepG2 cells from H2O2-induced oxidative damage by significantly inhibiting reactive oxygen species (ROS), [Ca2+]i, malondialdehyde (MDA) levels and increasing antioxidative enzyme activities.


Assuntos
Citrullus/química , Peróxido de Hidrogênio/farmacologia , Estresse Oxidativo/efeitos dos fármacos , Peptídeos/química , Hidrolisados de Proteína/química , Sequência de Aminoácidos , Antioxidantes/química , Antioxidantes/isolamento & purificação , Antioxidantes/farmacologia , Cromatografia Líquida de Alta Pressão , Citrullus/metabolismo , Células Hep G2 , Humanos , Oxirredução , Peptídeos/isolamento & purificação , Peptídeos/farmacologia , Proteínas de Plantas/metabolismo , Substâncias Protetoras/química , Substâncias Protetoras/isolamento & purificação , Substâncias Protetoras/farmacologia , Espécies Reativas de Oxigênio/metabolismo , Sementes/química , Sementes/metabolismo , Relação Estrutura-Atividade , Espectrometria de Massas em Tandem
15.
J Food Sci ; 85(4): 1045-1059, 2020 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-32112435

RESUMO

Highland barley brewer's spent grain (BSG), being China's brewing industry's major by-product is the focus of current research. The aim of the present study was to scrutinize the effects of ultrasound and heat pretreatments on enzymatic hydrolysis of highland barley BSG protein hydrolysates (HBSGPH) and evaluate the effect of enzymatic hydrolysis time on the antioxidant activity of hydrolysates by Alcalase. Different ultrasonic waves (40 and 50 kHz) and heat pretreatment temperatures (50 and 100 °C) were chosen and the pretreatment time was 15, 30, and 60 min. The obtained results revealed that the ultrasound pretreatment of highland barley BSG protein at 40 and 50 kHz has significantly (P < 0.05) enhanced about 57 and 67% of oxygen radical absorption capacity of obtained hydrolysate over the untreated substrate. The 1,1-diphenyl-2-picrylhdrazl (DPPH) radical scavenging activity (DRSA) 28%, metal chelating activity (MCA) 54%, superoxide radical scavenging activity (SRSA) 18%, and hydroxyl radical scavenging activity (HRSA) 25% of HBSGPH at 50 kHz were also improved (P < 0.05) significantly. HBSGPH from heat treatment at 100 °C showed no SRSA and HRSA scavenging activities but improved significantly (P < 0.05) about 27% ferric reducing antioxidant power (FRAP) assay values. In the present work, the resultant HBSGPH had stronger antioxidant properties with ultrasound pretreatment at 50 kHz and the enzymatic hydrolysis after 4 hr was facilitating the enzymatic release of antioxidant peptides from HBSGPH. PRACTICAL APPLICATION: Highland barley BSG is attracting toward natural food products due to its potent natural antioxidants to overcome the risk of diseases and are beneficial for human health.


Assuntos
Antioxidantes/análise , Hordeum/química , Extratos Vegetais/análise , China , Manipulação de Alimentos , Hidrólise , Hidrolisados de Proteína/química , Subtilisinas/química , Ultrassom , Resíduos/análise
16.
Poult Sci ; 99(3): 1693-1704, 2020 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-32111333

RESUMO

This study examined the antioxidant capabilities of peptides derived from chicken feather meal (CFM) protein hydrolysates which were produced using 3 different microbial proteases (Neutrase, Alcalase, and flavourzyme) and tested at varying concentrations, namely 1, 2, and 5% by weight. The highest levels of 2,2-diphenyl-1-picrylhydrazl (DPPH) and 2,2'-azino-bis-3-ethylbenzthiazoline-6-sulphonic acid (ABTS) radical scavenging activities were presented by CFM hydrolysate derived using 5 wt% Neutrase and digested for 4 h. Fractionation of this particular hydrolysate was then performed by applying 10, 5, 3, and 0.65 kDa molecular weight cutoff membranes. It was then determined that the molecular weight (MW) < 0.65 kDa fraction achieved the greatest level of free radical scavenging activity in the context of DPPH and ABTS. The MW < 0.65 kDa fraction then underwent additional fractionation using reverse-phase high-performance liquid chromatography to derive 3 main fractions designated as F1, F2, and F3. All of these fractions presented a high level of activity in DPPH radical scavenging, although no significant ABTS scavenging was observed. Quadrupole time-of-flight tandem mass spectrometry was used in determining the peptide contents of the fractions as Phe-Asp-Asp-Arg-Gly-Arg-X for F1 (FDDRGRX, 875 Da), Val-Thr-Leu-Ala-Val-Thr-Lys-His for F2 (VTLAVTKH, 868 Da), and Val-Ser-Glu-Ile-X-Ser-Ile-Pro-Ile-Ser for F3 (VSEIXSIPIS, 1,055 Da). Moreover, the F2 fraction was shown to be capable of preventing DNA damage induced by hydroxyl radicals, as indicated in tests using the plasmids pKS, pUC19, and pBR322 via the Fenton reaction. This outcome was demonstrated through in vitro antiproliferative activity in human cell lines based on SW620 colon cancer, using the 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide assay. The F2 fraction at 0.5 wt.% was also shown to be capable of inducing weak early apoptosis, which could be measured by using the Fluorescein isothiocyanate Annexin V Apoptosis Detection Kit with Propidium Iodide Solution. Furthermore, an increase in caspase-3 and caspase-8 activity was observed in SW620 cells following exposure for 24 h and 48 h.


Assuntos
Plumas/química , Radicais Livres/antagonistas & inibidores , Hidrolisados de Proteína/química , Hidrolisados de Proteína/farmacologia , Animais , Antioxidantes , Apoptose , Linhagem Celular Tumoral , Galinhas , Humanos , Peptídeos/química
17.
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
18.
J Agric Food Chem ; 68(14): 4237-4244, 2020 Apr 08.
Artigo em Inglês | MEDLINE | ID: mdl-32186189

RESUMO

Previous studies demonstrated that peptides produced by the hydrolysis of olive seed proteins using Alcalase enzyme showed in vitro multifunctional lipid-lowering capability. This work presents a deeper insight into the hypolipidemic effect of olive seed peptides. The capability of olive seed peptides to inhibit endogenous cholesterol biosynthesis through the inhibition of HMG-CoA reductase enzyme was evaluated observing a 38 ± 7% of inhibition. Two in vivo assays using different peptides concentrations (200 and 400 mg/kg/day) were designed to evaluate the hypolipidemic effect of olive seed peptides in male and female mice. A low concentration of hydrolysate reduced total cholesterol in male mice in a 20% after 11 weeks compared to the mice feeding with hypercholesterolemic diet. A higher hydrolysate concentration showed a greater reduction in total cholesterol (25%). The analysis of the olive seed hydrolysate by reverse phase high-performance liquid chromatography mass spectrometry (RP-HPLC-MS) enabled the identification of peptides that could be responsible for this hypolipidemic effect.


Assuntos
Hipolipemiantes/química , Olea/química , Peptídeos/química , Extratos Vegetais/química , Sementes/química , Animais , Linhagem Celular , Sobrevivência Celular/efeitos dos fármacos , Colesterol/biossíntese , Colesterol/metabolismo , Cromatografia Líquida de Alta Pressão , Dieta , Avaliação Pré-Clínica de Medicamentos , Feminino , Humanos , Hidrólise , Hidroximetilglutaril-CoA Redutases/metabolismo , Hipolipemiantes/farmacologia , Masculino , Camundongos , Peptídeos/farmacologia , Extratos Vegetais/farmacologia , Hidrolisados de Proteína/química , Espectrometria de Massas em Tandem
19.
Food Chem ; 319: 126534, 2020 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-32193058

RESUMO

The antioxidant peptides extracted from duck plasma hydrolysate (DPH) was investigated. The antioxidant activity of DPH, which was isolated and purified via ultrafiltration, size exclusion chromatography, and reversed-phase high-performance liquid chromatography, was evaluated using its free radical scavenging ability. Nano-liquid chromatography-tandem mass spectrometry was conducted to identify the DPH fractions with the highest antioxidant ability. Seven novel peptides: LDGP, TGVGTK, EVGK, RCLQ, LHDVK, KLGA, and AGGVPAG (400.43, 561.63, 431.48, 260.14, 610.71, 387.47, and 527.57 Da, respectively) were identified and synthesized using a solid-phase peptide produce to evaluate their antioxidant activities. Of these, EVGK exhibited the highest Fe2+ chelating ability (16.35%), and RCLQ presented the highest reducing power, 2,2-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt scavenging activity, and 1,1-diphenyl-2-picrylhydrazyl scavenging rate (0.62, 274.83 mM TE/mg, and 95.12%, respectively). Our results indicated that DPH possessed antioxidant capabilities and could be used to obtain antioxidant peptides, thus adding economic value to duck blood.


Assuntos
Antioxidantes/química , Proteínas Sanguíneas/química , Patos , Peptídeos/química , Animais , Antioxidantes/isolamento & purificação , Compostos de Bifenilo , Proteínas Sanguíneas/isolamento & purificação , Cromatografia em Gel , Peptídeos/isolamento & purificação , Hidrolisados de Proteína/química
20.
J Food Sci ; 85(4): 1328-1337, 2020 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-32220144

RESUMO

Naked oat globulin was hydrolyzed by alcalase, flavourzyme, pepsin, and trypsin in sequence. The hydrolysates (NOGH) were purified using gel chromatography, reversed-phase high performance liquid chromatography (RP-HPLC). Finally, fraction D7d with the highest ACE-inhibitory was subjected to liquid chromatography-mass spectrometry analysis and 14 peptides were identified. Of which, peptide SSYYPFK (890.4 Da) was chose to synthesize based on in silico analysis. The SSYYPFK demonstrated high ACE-inhibitory activity (IC50 : 91.82 µM) with competitive inhibition mode, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 100 to 150 mg/kg body weight. Molecular docking simulation demonstrated that SSYYPFK could bind with the active site S1 of ACE via short hydrogen bonds. It could remain the ACE-inhibitory activity after simulated gastrointestinal hydrolysis. Moreover, SSYYPFK showed acceptable renin and endothelin-1 suppressing capacity (47.59% and 27.88% at 1.5 mg/mL, respectively). These results indicated that SSYYPFK may have similar antihypertensive mechanism with captopril, and could be develop to natural antihypertensive products. PRACTICAL APPLICATION: One novel ACE-inhibitory peptide SSYYPFK (890.4 Da) was identified from naked oat globulin hydrolysates. It exhibited relatively high renin and intracellular endothelin-1 suppressing capacity, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats. This peptide could be used as natural and safe nutraceuticals and/or functional ingredients.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Anti-Hipertensivos/farmacologia , Avena/química , Globulinas/química , Proteínas de Plantas/farmacologia , Animais , Anti-Hipertensivos/química , Avena/metabolismo , Pressão Sanguínea/efeitos dos fármacos , Cromatografia de Fase Reversa , Simulação por Computador , Endotelina-1 , Masculino , Simulação de Acoplamento Molecular , Pepsina A/farmacologia , Peptídeos/química , Peptidil Dipeptidase A/metabolismo , Proteínas de Plantas/química , Hidrolisados de Proteína/química , Distribuição Aleatória , Ratos , Ratos Endogâmicos SHR , Renina , Tripsina
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