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1.
Fish Shellfish Immunol ; 150: 109597, 2024 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-38697373

RESUMO

This study investigated the effects of fish protein hydrolysate derived from barramundi on growth performance, muscle composition, immune response, disease resistance, histology and gene expression in white shrimp (Penaeus vannamei). In vitro studies demonstrated FPH enhanced mRNA expressions of key immune-related genes and stimulated reactive oxygen species (ROS) production and phagocytic activity in shrimp hemocytes. To evaluate the effects of substituting fish meal with FPH in vivo, four isoproteic (43 %), isolipidic (6 %), and isoenergetic diets (489 kcal/100 g) were formulated with fish meal substitution levels of 0 % (control), 30 % (FPH30), 65 % (FPH65), and 100 % (FPH100). After 8-week feeding, the growth performance of FPH65 and FPH100 were significantly lower than that of control and FPH30 (p < 0.05). Similarly, the midgut histological examination revealed the wall thickness and villi height of FPH100 were significantly lower than those of control (p < 0.05). The shrimps were received the challenge of AHPND + Vibrio parahaemolyticus at week 4 and 8. All FPH-fed groups significantly enhanced resistance against Vibrio parahaemolyticus at week 4 (p < 0.05). However, this protective effect diminished after long-period feeding. No significant difference of survival rate was observed among all groups at week 8 (p > 0.05). The expressions of immune-related genes were analyzed at week 4 before and after challenge. In control group, V. parahaemolyticus significantly elevated SOD in hepatopancreas and Muc 19, trypsin, Midline-fas, and GPx in foregut (p < 0.05). Moreover, hepatopancreatic SOD of FPH65 and FPH100 were significantly higher than that of control before challenge (p < 0.05). Immune parameters were measured at week 8. Compared with control, the phagocytic index of FPH 30 was significantly higher (p < 0.05). However, dietary FPH did not alter ROS production, phenoloxidase activity, phagocytic rate, and total hemocyte count (p > 0.05). These findings suggest that FPH30 holds promise as a feed without adverse impacts on growth performance while enhancing the immunological response of white shrimp.


Assuntos
Ração Animal , Dieta , Imunidade Inata , Penaeidae , Hidrolisados de Proteína , Vibrio parahaemolyticus , Animais , Penaeidae/imunologia , Penaeidae/crescimento & desenvolvimento , Vibrio parahaemolyticus/fisiologia , Ração Animal/análise , Dieta/veterinária , Hidrolisados de Proteína/química , Hidrolisados de Proteína/administração & dosagem , Resistência à Doença , Suplementos Nutricionais/análise , Proteínas de Peixes/genética , Proteínas de Peixes/imunologia
2.
Meat Sci ; 212: 109469, 2024 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-38428152

RESUMO

The present study examines the bioactive potential of sheep plasma protein hydrolysates (SPPH) produced by in-vitro gastrointestinal digestion as antioxidants, antimicrobials, anti-obesity agents, and inhibitors of lipid oxidation in sausage to address the oxidative stability and shelf-life issues of mutton. The antioxidant and antimicrobial activities, indicate a positive relationship between the degree of hydrolysis and digestion duration. The study finds that SPPH has a potent inhibitory effect on pancreatic lipase and cholesterol esterase. It has higher oil holding capacity than sheep plasma protein, observed at one hour of hydrolysis time. SPPH exhibit an improved behavior in foaming properties along alkaline pH and digestion time while display lower emulsifying activity and stability with hydrolysis advancement. The SPPH act as a natural preservative in developing functional mutton sausage by inhibiting lipid-oxidation. This study showed that the recovery of SPPH can be a cost-effective and sustainable strategy for generating available ingredients for enhanced shelf-life of meat products.


Assuntos
Produtos da Carne , Hidrolisados de Proteína , Animais , Ovinos , Hidrolisados de Proteína/química , Antioxidantes/química , Hidrólise , Lipídeos
3.
Int J Biol Macromol ; 262(Pt 1): 130069, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38340918

RESUMO

Squid pen (SP) is a valuable source of protein and ß-chitin. However, current research has primarily focused on extracting ß-chitin from SP. This study innovatively extracted both SP protein hydrolysates (SPPHs) and SP ß-chitin (SPC) simultaneously using protease hydrolysis. The effects of different proteases on their structural characteristics and bioactivity were evaluated. The results showed that SP alcalase ß-chitin (SPAC) had the highest degree of deproteinization (DP, 98.19 %) and SP alcalase hydrolysates (SPAH) had a degree of hydrolysis (DH) of 24.47 %. The analysis of amino acid composition suggested that aromatic amino acids accounted for 17.44 % in SPAH. Structural characterization revealed that SP flavourzyme hydrolysates (SPFH) had the sparsest structure. SPC exhibited an excellent crystallinity index (CI, over 60 %) and degree of acetylation (DA, over 70 %). During simulated gastrointestinal digestion (SGD), the hydroxyl radical scavenging activity, ABTS radical scavenging activity, Fe2+ chelating activity, and reducing power of the SPPHs remained stable or increased significantly. Additionally, SPFC exhibited substantial inhibitory effects on Staphylococcus aureus and Escherichia coli (S. aureus and E. coli), with inhibition circle diameters measuring 2.4 cm and 2.1 cm. These findings supported the potential use of SPPHs as natural antioxidant alternatives and suggested that SPC could serve as a potential antibacterial supplement.


Assuntos
Peptídeo Hidrolases , Hidrolisados de Proteína , Animais , Peptídeo Hidrolases/metabolismo , Hidrólise , Hidrolisados de Proteína/química , Decapodiformes/química , Quitina , Escherichia coli/metabolismo , Staphylococcus aureus/metabolismo , Antioxidantes/química , Subtilisinas/metabolismo
4.
J Agric Food Chem ; 70(36): 11201-11211, 2022 Sep 14.
Artigo em Inglês | MEDLINE | ID: mdl-36039940

RESUMO

Protein hydrolysates (PHs) are plant biostimulants consisting of oligopeptides and free amino acids exploited in agriculture to increase crop productivity. This work aimed to fractionate a commercial collagen-derived protein hydrolysate (CDPH) according to the molecular mass of the peptides and evaluate the bioactivity of different components. First, the CDPH was dialyzed and/or filtrated and analyzed on maize, showing that smaller compounds were particularly active in stimulating lateral root growth. The CDPH was then fractionated through fast protein liquid chromatography and tested on in vitro grown tomatoes proving that all the fractions were bioactive. Furthermore, these fractions were characterized by liquid chromatography-electrospray ionization-tandem mass spectrometry revealing a consensus sequence shared among the identified peptides. Based on this sequence, a synthetic peptide was produced. We assessed its structural similarity with the CDPH, the collagen, and polyproline type II helix by comparing the respective circular dichroism spectra and for the first time, we proved that a signature peptide was as bioactive as the whole CDPH.


Assuntos
Peptídeos , Hidrolisados de Proteína , Cromatografia Líquida de Alta Pressão , Cromatografia Líquida , Colágeno/química , Peptídeos/química , Hidrolisados de Proteína/química
5.
J Sci Food Agric ; 102(14): 6414-6422, 2022 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-35562860

RESUMO

BACKGROUND: Milk-derived protein hydrolysates have generated a great deal of interest recently due to their numerous beneficial health effects. However, there are few comparative studies on protein hydrolysates from different dairy species, their production, characterization, and bioactivity. In the present study, skimmed milk from both major and minor dairy species was hydrolyzed with alcalase, and its protein profiles were studied using tricine polyacrylamide gel electrophoresis and reverse phase-high protein liquid chromatography. The antioxidant and in vitro immunostimulatory properties were determined. RESULTS: Iron chelation activity was highest in hydrolysates of whey (25.00 ± 0.32 mmol L-1 ), casein (25.14 ± 0.34 mmol L-1 ), colostrum (24.52 ± 0.28 mmol L-1 ), and skimmed cattle milk (24.21 ± 0.26 mmol L-1 ). α,α-Diphenyl-ß-picrylhydrazyl scavenging and 2,2'-azobis(2-amidino-propane) dihydrochloride activity was lowest in skimmed donkey milk protein hydrolysates (MPHs) (IC50 : 5.37 ± 0.05 mg mL-1 and 151.59 ± 2.1 mg mL-1 ). Production of nitric oxide and phagocytosis activity in RAW 264.7 (murine macrophage cell line) was significantly higher among whey and buffalo skimmed milk protein hydrolysate-treated groups as compared with the untreated group. The incorporation of whey protein hydrolysate and skimmed buffalo milk protein hydrolysate were sensorially acceptable at 10% level in beverage mix. CONCLUSION: This study comparatively evaluates the antioxidative and immunomodulatory properties of different skimmed MPHs and their potential applications as ingredients in pediatric, geriatric, and other health-promoting foods. © 2022 Society of Chemical Industry.


Assuntos
Antioxidantes , Hidrolisados de Proteína , Animais , Antioxidantes/química , Búfalos/metabolismo , Caseínas , Bovinos , Hidrólise , Quelantes de Ferro , Camundongos , Leite/química , Proteínas do Leite/química , Óxido Nítrico , Hidrolisados de Proteína/química , Subtilisinas/metabolismo , Proteínas do Soro do Leite
6.
Curr Issues Mol Biol ; 43(3): 1592-1605, 2021 Oct 13.
Artigo em Inglês | MEDLINE | ID: mdl-34698092

RESUMO

Collagen hydrolysates (CHs) are composed of bioactive peptides (BAPs), which possess health enhancing properties. There is a knowledge gap regarding the bioavailability of these BAPs that involves intestinal transport and hepatic first pass effects. A simulated gastrointestinal model was used to generate digesta from two CHs (CH-GL and CH-OPT), which were applied to a novel transwell co-culture of human intestinal epithelium cell line-6 (HIEC-6) and hepatic (HepG2) cells to simulate in vivo conditions of absorption and first pass metabolism. Peptide transport, hepatic first pass effects, and bioavailability were determined by measuring BAPs (Gly-Pro, Hyp-Gly, Ala-Hyp, Pro-Hyp, Gly-Pro-Hyp) using an innovative capillary electrophoresis method. All peptides were transported across the intestinal cell layer to varying degrees with both CHs; however, Gly-Pro-Hyp was transported only with CH-GL, but not CH-OPT. Notable hepatic production was observed for Ala-Hyp with both CH treatments, and for Pro-Hyp and Gly-Pro with CH-GL only. All peptides were bioavailable (>10%), except for Gly-Pro-Hyp after CH-OPT. Overall, a high degree of transport and hepatic first pass effects on CH-derived BAPs were observed. Further research is needed to explore the hepatic mechanisms related to the production of BAPs and the bifunctional effects of the bioavailable BAPs noted in this study.


Assuntos
Metabolismo Basal , Colágeno/química , Digestão , Peptídeos/química , Hidrolisados de Proteína/química , Disponibilidade Biológica , Transporte Biológico , Linhagem Celular , Sobrevivência Celular , Células Cultivadas , Técnicas de Cocultura , Colágeno/metabolismo , Hepatócitos/metabolismo , Humanos , Hidrólise , Mucosa Intestinal/metabolismo , Peptídeos/metabolismo , Hidrolisados de Proteína/metabolismo
7.
Food Chem ; 359: 129852, 2021 Oct 15.
Artigo em Inglês | MEDLINE | ID: mdl-33940471

RESUMO

The generation of biologically active fish protein hydrolysates (FPH) is a useful technique to produce value-added products with potential application in the functional food and nutraceutical industries. Fish muscle is an attractive substrate for the production of protein hydrolysates due to its rich protein content, containing 15-25% of total fish protein. This paper reviews the production of protein hydrolysates from fish muscle, most commonly via enzymatic hydrolysis, and their subsequent bioactivities including anti-obesity, immunomodulatory, antioxidant, angiotensin I-converting enzyme (ACE)-inhibitory, anti-microbial, and anti-cancer activities as measured by in vitro testing methods. Disease prevention with FPH potentially offers a safe and natural alternative to synthetic drugs. Small molecular weight (MW) FPHs generally exhibit favourable bioactivity than large MW fractions via enhanced absorption through the gastrointestinal tract. This review also discusses the relationship between amino acid (AA) composition and AA sequence of FPH and peptides and their exhibited in vitro bioactivity.


Assuntos
Proteínas de Peixes/metabolismo , Músculos/metabolismo , Hidrolisados de Proteína/farmacologia , Animais , Hidrólise , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo
8.
J Agric Food Chem ; 68(12): 3881-3890, 2020 Mar 25.
Artigo em Inglês | MEDLINE | ID: mdl-32119538

RESUMO

Nuclear magnetic resonance (NMR) metabolomics profiling was evaluated as a new tool in sensory assessment of protein hydrolysates. Hydrolysates were produced on the basis of different raw materials (cod, salmon, and chicken), enzymes (Food Pro PNL and Bromelain), and hydrolysis time (10 and 50 min). The influence of raw material and hydrolysis parameters on sensory attributes was determined by traditional descriptive sensory analysis and 1H NMR spectroscopy. The raw material had a major influence on the attribute intensity and metabolite variation, followed by enzyme and hydrolysis time. However, the formation of bitter taste was not affected by the raw material. Partial least-squares regression (PLSR) on 1H NMR and sensory data provided good models (Q2 = 0.55-0.89) for 11 of the 17 evaluated attributes, including bitterness. Significant metabolite-attribute associations were identified. The study confirms the potential prediction of the sensory properties of protein hydrolysates from cod, salmon, and chicken based on 1H NMR metabolomics profiling.


Assuntos
Proteínas de Carne/química , Hidrolisados de Proteína/química , Paladar , Animais , Galinhas/metabolismo , Gadus morhua/metabolismo , Humanos , Proteínas de Carne/metabolismo , Metabolômica , Ressonância Magnética Nuclear Biomolecular , Hidrolisados de Proteína/metabolismo , Proteólise , Salmão/metabolismo
9.
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
10.
J Agric Food Chem ; 66(37): 9738-9749, 2018 Sep 19.
Artigo em Inglês | MEDLINE | ID: mdl-30142267

RESUMO

Hydrolyzed protein-rich byproducts from food production may find a variety of applications, for example, as rich ingredients of fermentation media. We have conducted a study of the enzymatic hydrolysis of three byproducts from Norwegian food industries: chicken byproducts, mixed pork and beef byproducts, and salmon viscera. The efficiency and optimization of the enzymatic hydrolysis were evaluated using endogenous enzymes alone and in combination with commercial proteases. Hydrolysis reactions were conducted with freshly thawed raw materials using short incubation times and including an initial temperature gradient from 4 to 60 °C to both harness the power of endogenous enzymes and minimize microbial contamination. Subsequently, hydrolysates were characterized by analyzing the total recovery of protein, the peptide molecular-weight distribution, and the composition of total and free amino acids. The action of endogenous enzymes played an important role in raw-material hydrolysis, particularly when hydrolyzing salmon viscera but less so when hydrolyzing chicken byproducts. For pork-beef and chicken byproducts, the addition of Alcalase or Papain improved protein recovery, reaching levels up to 90%. Next to showing efficient hydrolysis protocols, the present data also provide a comparison of the amino acid compositions of hydrolysates derived from these three different protein-rich byproducts. Growth studies showed that the obtained protein-rich hydrolysates from meat and fish industries are a promising alternative for expensive nitrogen sources that are commonly used for fermenting yeasts.


Assuntos
Resíduos Industriais/análise , Papaína/química , Peptídeos/química , Hidrolisados de Proteína/química , Subtilisinas/química , Resíduos/análise , Animais , Biocatálise , Biotecnologia , Bovinos , Galinhas , Hidrólise , Noruega , Salmão , Suínos
11.
Br J Nutr ; 116(8): 1336-1345, 2016 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-27751188

RESUMO

The world's fisheries and aquaculture industries produce vast amounts of protein-containing by-products that can be enzymatically hydrolysed to smaller peptides and possibly be used as additives to functional foods and nutraceuticals targeted for patients with obesity-related metabolic disorders. To investigate the effects of fish protein hydrolysates on markers of metabolic disorders, obese Zucker fa/fa rats consumed diets with 75 % of protein from casein/whey (CAS) and 25 % from herring (HER) or salmon (SAL) protein hydrolysate from rest raw material, or 100 % protein from CAS for 4 weeks. The fatty acid compositions were similar in the experimental diets, and none of them contained any long-chain n-3 PUFA. Ratios of lysine:arginine and methionine:glycine were lower in HER and SAL diets when compared with CAS, and taurine was detected only in fish protein hydrolysate diets. Motifs with reported hypocholesterolemic or antidiabetic activities were identified in both fish protein hydrolysates. Rats fed HER diet had lower serum HDL-cholesterol and LDL-cholesterol, and higher serum TAG, MUFA and n-3:n-6 PUFA ratio compared with CAS-fed rats. SAL rats gained more weight and had better postprandial glucose regulation compared with CAS rats. Serum lipids and fatty acids were only marginally affected by SAL, but adipose tissue contained less total SFA and more total n-3 PUFA when compared with CAS. To conclude, diets containing hydrolysed rest raw material from herring or salmon proteins may affect growth, lipid metabolism, postprandial glucose regulation and fatty acid composition in serum and adipose tissue in obese Zucker rats.


Assuntos
Diabetes Mellitus Tipo 2/dietoterapia , Produtos Pesqueiros , Proteínas de Peixes/uso terapêutico , Hiperglicemia/prevenção & controle , Hiperlipidemias/prevenção & controle , Obesidade/dietoterapia , Hidrolisados de Proteína/uso terapêutico , Tecido Adiposo Branco/metabolismo , Adiposidade , Motivos de Aminoácidos , Animais , Fármacos Antiobesidade/efeitos adversos , Fármacos Antiobesidade/química , Fármacos Antiobesidade/economia , Fármacos Antiobesidade/uso terapêutico , Aquicultura/economia , Biomarcadores/sangue , Biomarcadores/metabolismo , Diabetes Mellitus Tipo 2/sangue , Diabetes Mellitus Tipo 2/complicações , Diabetes Mellitus Tipo 2/metabolismo , Suplementos Nutricionais/efeitos adversos , Suplementos Nutricionais/economia , Ácidos Graxos Ômega-3/sangue , Ácidos Graxos Ômega-3/metabolismo , Produtos Pesqueiros/efeitos adversos , Produtos Pesqueiros/economia , Proteínas de Peixes/efeitos adversos , Proteínas de Peixes/química , Proteínas de Peixes/economia , Pesqueiros/economia , Indústria de Processamento de Alimentos/economia , Hiperlipidemias/complicações , Hiperlipidemias/etiologia , Hipoglicemiantes/efeitos adversos , Hipoglicemiantes/química , Hipoglicemiantes/economia , Hipoglicemiantes/uso terapêutico , Resíduos Industriais/análise , Resíduos Industriais/economia , Masculino , Obesidade/complicações , Obesidade/metabolismo , Obesidade/fisiopatologia , Hidrolisados de Proteína/efeitos adversos , Hidrolisados de Proteína/química , Hidrolisados de Proteína/economia , Ratos Zucker , Salmão , Aumento de Peso
12.
Artigo em Inglês | MEDLINE | ID: mdl-27336594

RESUMO

Presently, hydrolyzed formulas (HF) are used primarily in infants that cannot be exclusively breastfed, those with cow's milk allergy and for primary prevention of allergic disease, but HFs are increasingly being used worldwide, begging the question if they may be recommended as the optimal choice for all standard-risk, full-term, non-exclusively breastfed infants. Data regarding the nutritional adequacy of modern-day HFs are scarce and lack long-term data suggesting that growth in infants fed HF versus an intact protein formula (IPF) is different. While human breast milk is the optimal source of nutrition for multiple reasons, a 2006 systematic review determined there were no comparable long-term studies regarding prolonged use of HFs versus breastfeeding. Meta-analyses of formula consumption and risk of atopic dermatitis (AD) have found that infants fed partially HF compared to IPF had a lower risk of AD, but there are significant limitations to these studies, making conclusions about the general use of HFs problematic. Costs should be considered in decision-making regarding the choice of the formula, but global comparison of this is difficult given large cost differences in different countries. Despite the issues raised here, the desire to provide concrete recommendations of widespread HF use needs to be balanced carefully in order not to overstate claims of benefit. Long-term studies are needed to investigate the feasibility of HF as a routine feeding option for healthy, standard-risk infants. Because of the paucity of data, routine use of HF as an equivalent option to breastfeeding or IPF cannot be supported at present based on available scientific evidence.


Assuntos
Fórmulas Infantis/química , Hidrolisados de Proteína/química , Animais , Aleitamento Materno , Bovinos , Desenvolvimento Infantil , Análise Custo-Benefício , Dermatite Atópica/prevenção & controle , Humanos , Lactente , Fenômenos Fisiológicos da Nutrição do Lactente , Metanálise como Assunto , Hipersensibilidade a Leite/dietoterapia , Hipersensibilidade a Leite/prevenção & controle , Proteínas do Leite/administração & dosagem , Proteínas do Leite/química , Ensaios Clínicos Controlados Aleatórios como Assunto , Fatores de Risco
13.
J Sci Food Agric ; 96(9): 2998-3006, 2016 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-26399367

RESUMO

BACKGROUND: Deferriferrichrysin (Dfcy) is a siderophore found in foods fermented by Aspergillus oryzae and is a promising candidate for an antioxidant food additive because of its high binding constant toward iron. However, the Dfcy concentration is typically low in foods and cultures. RESULTS: We optimised culture conditions to improve Dfcy production to 2800 mg L(-1) from 22.5 mg L(-1) under typical conditions. Then, we evaluated the potential of Dfcy as a food additive by measuring its safety, stability, and antioxidant activity. Dfcy was sufficiently stable that over 90% remained after pasteurisation at 63 °C for 30 min at pH 3-11, or after sterilisation at 120 °C for 4 min at pH 4-6. Dfcy showed high antioxidant activity in an oil-in-water model, where inhibition of lipid oxidation was measured by peroxide value (PV) and thiobarbituric acid reactive substances (TBARS) assays. Dfcy decreased PV and TBARS by 83% and 75%, respectively. Antioxidant activity of Dfcy was equal to or higher than that of the synthetic chelator EDTA. CONCLUSION: Our study provides the first practical method for production of Dfcy. Dfcy can be a novel food-grade antioxidant and the first natural alternative to the synthesised iron chelator EDTA. © 2015 Society of Chemical Industry.


Assuntos
Antioxidantes/isolamento & purificação , Aspergillus oryzae/química , Conservantes de Alimentos/isolamento & purificação , Quelantes de Ferro/isolamento & purificação , Modelos Químicos , Peptídeo Hidrolases/metabolismo , Peptídeos Cíclicos/isolamento & purificação , Animais , Antioxidantes/efeitos adversos , Antioxidantes/química , Antioxidantes/economia , Aspergillus oryzae/crescimento & desenvolvimento , Aspergillus oryzae/metabolismo , Fermentação , Conservantes de Alimentos/efeitos adversos , Conservantes de Alimentos/química , Conservantes de Alimentos/economia , Indústria de Processamento de Alimentos/economia , Proteínas Fúngicas/metabolismo , Temperatura Alta/efeitos adversos , Resíduos Industriais/análise , Resíduos Industriais/economia , Quelantes de Ferro/efeitos adversos , Quelantes de Ferro/química , Quelantes de Ferro/economia , Japão , Testes de Mutagenicidade , Oryza/química , Peptídeos Cíclicos/efeitos adversos , Peptídeos Cíclicos/química , Peptídeos Cíclicos/economia , Proteínas de Vegetais Comestíveis/química , Proteínas de Vegetais Comestíveis/economia , Proteínas de Vegetais Comestíveis/isolamento & purificação , Proteínas de Vegetais Comestíveis/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/economia , Hidrolisados de Proteína/isolamento & purificação , Hidrolisados de Proteína/metabolismo , Saccharomyces cerevisiae/crescimento & desenvolvimento , Saccharomyces cerevisiae/metabolismo , Sementes/química , Testes de Toxicidade Aguda , Vinho/análise , Vinho/microbiologia
14.
Food Funct ; 6(6): 1919-27, 2015 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-25965854

RESUMO

Recently, much attention has been given to improving the antioxidant activity of protein hydrolysates via the Maillard reaction, but little is known about the cellular antioxidant activity of Maillard reaction products (MRPs) from protein hydrolysates. We first investigated chemical characterization and the cellular antioxidant activity of MRPs in a shrimp (Litopenaeus vannamei) by-product protein hydrolysate (SBH)-glucose system at 110 °C for up to 10 h of heating. Solutions of SBH and glucose were also heated alone as controls. The Maillard reaction greatly resulted in the increase of hydroxymethylfurfural (HMF) and browning intensity, high molecular weight fraction, and reduction of the total amino acid in SBH with the heating time, which correlated well with the free radical scavenging activity of MRPs. MRPs had stronger inhibiting effects on oxidative stress of human HepG2 cells than the original SBH, and its cellular antioxidant activity strongly correlated with free radical scavenging activity, but less affected by the browning intensity and HMF level. The caramelization of glucose partially affected the HMF level and free radical scavenging activity of MRPs, but it was not related to the cellular antioxidant activity. The cellular antioxidant activity of MRPs for 5 h of heating time appeared to reach a maximum level, which was mainly due to carbonyl ammonia condensation reaction. In conclusion, the Maillard reaction is a potential method to increase the cellular antioxidant activity of a shrimp by-product protein hydrolysate, but the higher HMF levels and the lower amino acid content in MRPs should also be considered.


Assuntos
Antioxidantes/química , Proteínas de Artrópodes/química , Hepatócitos/metabolismo , Estresse Oxidativo , Penaeidae/química , Hidrolisados de Proteína/química , Espécies Reativas de Oxigênio/antagonistas & inibidores , Animais , Antioxidantes/economia , Antioxidantes/isolamento & purificação , Antioxidantes/metabolismo , Proteínas de Artrópodes/economia , Proteínas de Artrópodes/isolamento & purificação , Proteínas de Artrópodes/metabolismo , Sobrevivência Celular , China , Proteínas Alimentares/química , Proteínas Alimentares/economia , Proteínas Alimentares/isolamento & purificação , Proteínas Alimentares/metabolismo , Suplementos Nutricionais/análise , Suplementos Nutricionais/economia , Conservantes de Alimentos/química , Conservantes de Alimentos/economia , Conservantes de Alimentos/isolamento & purificação , Conservantes de Alimentos/metabolismo , Indústria de Processamento de Alimentos/economia , Furaldeído/análogos & derivados , Furaldeído/análise , Furaldeído/química , Glucose/química , Células Hep G2 , Temperatura Alta , Humanos , Resíduos Industriais/análise , Resíduos Industriais/economia , Reação de Maillard , Peso Molecular , Hidrolisados de Proteína/economia , Espécies Reativas de Oxigênio/metabolismo
15.
Mar Drugs ; 13(4): 1993-2009, 2015 Apr 03.
Artigo em Inglês | MEDLINE | ID: mdl-25854645

RESUMO

In the current study, the preparation conditions of neutrase hydrolysate (SMH) from skate (Raja porosa) muscle protein were optimized using orthogonal L9(3)4 tests, and R values indicated that pH was the most important factor affecting HO· scavenging activity of SMH. Under the optimum conditions of pH 7.0, enzymolysis temperature 60 °C, enzyme/substrate ratio (E/S) 2%, and enzymolysis time 5 h, EC50 of SMH on HO· was 2.14 ± 0.17 mg/mL. Using ultrafiltration, gel filtration chromatography, and RP-HPLC, two novel antioxidant nonapeptides (SP-A and SP-B) were isolated from SMH and their amino acid sequences were found to be APPTAYAQS (SP-A) and NWDMEKIWD (SP-B) with calculated molecular masses of 904.98 Da and 1236.38 Da, respectively. Both showed strong antioxidant activities. SP-A and SP-B exhibited good scavenging activities on HO· (EC50 0.390 and 0.176 mg/mL), DPPH· (EC50 0.614 and 0.289 mg/mL), and O2-· (EC50 0.215 and 0.132 mg/mL) in a dose-dependent manner. SP-B was also effective against lipid peroxidation in the model system. The aromatic (2Trp), acidic (2Asp and Glu), and basic (Lys) amino acid residues within the sequences of SP-B might account for its pronounced antioxidant activity. The results of this study suggested that protein hydrolysate and peptides from skate muscle might be effective as food additives for retarding lipid peroxidation occurring in foodstuffs.


Assuntos
Antioxidantes/isolamento & purificação , Proteínas de Peixes/isolamento & purificação , Conservantes de Alimentos/isolamento & purificação , Músculo Esquelético/química , Oligopeptídeos/isolamento & purificação , Fragmentos de Peptídeos/isolamento & purificação , Rajidae , Sequência de Aminoácidos , Animais , Antioxidantes/química , Antioxidantes/metabolismo , Endopeptidases/metabolismo , Proteínas de Peixes/química , Proteínas de Peixes/metabolismo , Conservantes de Alimentos/química , Conservantes de Alimentos/metabolismo , Alimentos Congelados/análise , Alimentos Congelados/economia , Concentração de Íons de Hidrogênio , Peroxidação de Lipídeos , Peso Molecular , Oligopeptídeos/química , Oligopeptídeos/metabolismo , Fragmentos de Peptídeos/química , Fragmentos de Peptídeos/metabolismo , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Alimentos Marinhos/análise , Alimentos Marinhos/economia
16.
J Sci Food Agric ; 95(5): 906-14, 2015 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-24853103

RESUMO

BACKGROUND: Bee larvae are considered to be an important reservoir for proteins. However, little attention has been paid to the release of potential bioactive peptides from bee larva proteins. In this study the major protein in bee larvae was hydrolyzed in vitro by gastrointestinal enzymes. The peptide profile of the hydrolysis was characterized by gel filtration chromatography and tricine-SDS-PAGE. Furthermore, the bioactive peptide was isolated and identified by Q-TOF-MS/MS. RESULTS: The major bee larva protein was identified as apalbumin 2 and was more digestible into peptides with molecular weights lower than 3 kDa. The hydrolysate obtained after 3 h of digestion exhibited angiotensin I-converting enzyme (ACE)-inhibitory activity and was purified sequentially by gel filtration and RP-HPLC. The molecular weights of peptide fractions with ACE-inhibitory activity were distributed between 0.5 and 1.5 kDa. A novel peptide with highest ACE-inhibitory activity (IC50 54.9 µmol L(-1) ) was purified by further RP-HPLC. The amino acid sequence of this peptide was identified as LLKPY (632.40 Da). CONCLUSION: ACE-inhibitory peptides could be formed from bee larvae through gastrointestinal digestion. The most active peptide (LLKPY) is potentially useful as a therapeutic agent in treating hypertension.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Digestão , Descoberta de Drogas , Proteínas de Insetos/isolamento & purificação , Modelos Biológicos , Oligopeptídeos/isolamento & purificação , Fragmentos de Peptídeos/isolamento & purificação , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/química , Inibidores da Enzima Conversora de Angiotensina/metabolismo , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Animais , Anti-Hipertensivos/química , Anti-Hipertensivos/isolamento & purificação , Anti-Hipertensivos/metabolismo , Anti-Hipertensivos/farmacologia , Criação de Abelhas/economia , Abelhas/química , China , Quimotripsina/metabolismo , Proteínas de Insetos/química , Proteínas de Insetos/economia , Proteínas de Insetos/metabolismo , Proteínas de Insetos/farmacologia , Larva/química , Peso Molecular , Oligopeptídeos/química , Oligopeptídeos/metabolismo , Oligopeptídeos/farmacologia , Fragmentos de Peptídeos/química , Fragmentos de Peptídeos/metabolismo , Fragmentos de Peptídeos/farmacologia , Hidrolisados de Proteína/química , Hidrolisados de Proteína/economia , Hidrolisados de Proteína/metabolismo , Hidrolisados de Proteína/farmacologia , Proteólise , Tripsina/metabolismo , Resíduos/análise , Resíduos/economia
17.
Food Chem ; 145: 1076-85, 2014 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-24128587

RESUMO

The objective of this study was to investigate the potential of an instrumental taste-sensing system to distinguish between shrimp processing by-products hydrolysates produced using different proteases and hydrolysis conditions, and the possible association of taste sensor outputs with human gustatory assessment, salt content, and bioactivity. Principal component analysis of taste sensor output data categorised samples according to the proteases used for hydrolysis. High umami sensor outputs were characteristic of bromelain- and Flavourzyme-produced hydrolysates, compared to low saltiness and high bitterness outputs of Alcalase-produced hydrolysates, and high saltiness and low umami outputs of Protamex-produced hydrolysates. Extensively hydrolysed samples showed higher sourness outputs. Saltiness sensor outputs were correlated with conductivity and sodium content, while umami sensor responses were related to gustatory sweetness, bitterness and umami, as well as angiotensin-I converting enzyme inhibitory activity. Further research should explore the dose dependence and sensitivity of each taste sensor to specific amino acids and peptides.


Assuntos
Proteínas Alimentares/análise , Resíduos Industriais/análise , Pandalidae/química , Fragmentos de Peptídeos/análise , Hidrolisados de Proteína/química , Frutos do Mar/análise , Inibidores da Enzima Conversora de Angiotensina/análise , Inibidores da Enzima Conversora de Angiotensina/economia , Inibidores da Enzima Conversora de Angiotensina/metabolismo , Animais , Proteínas de Bactérias/metabolismo , Bromelaínas/metabolismo , Proteínas Alimentares/economia , Proteínas Alimentares/metabolismo , Suplementos Nutricionais/economia , Endopeptidases/metabolismo , Inspeção de Alimentos/métodos , Alimentos Fortificados/economia , Indústria de Processamento de Alimentos/economia , Proteínas Fúngicas/metabolismo , Humanos , Resíduos Industriais/economia , Fragmentos de Peptídeos/economia , Fragmentos de Peptídeos/metabolismo , Proteínas de Plantas/metabolismo , Análise de Componente Principal , Hidrolisados de Proteína/economia , Hidrolisados de Proteína/metabolismo , Proteólise , Estações do Ano , Subtilisinas/metabolismo , Paladar
18.
Artigo em Inglês | MEDLINE | ID: mdl-24779899

RESUMO

The 3-monochloro-1,2-propandiol (3-MCPD) levels in soy sauces which contained hydrolysed vegetable protein were evaluated for the Bulgarian market. For analysis of 3-MCPD, a gas chromatography-mass spectrometry (GC-MS) method was applied with a linear range of 0.03-2.00 µg mL⁻¹ and a limit of detection (LOD) of 2.3 µg kg⁻¹ and a limit of quantification (LOQ) of 3.4 µg kg⁻¹. At these levels, the standard deviation was 5.1%, with recoveries between 81% and 102%. The method was applied to the analysis of 21 samples of soy sauce from the Bulgarian market. Results ranged from 3.7 to 185.6 µg kg⁻¹. Soy sauces produced from hydrolysed soy protein contained higher levels of 3-MCPD than naturally fermented sauces. In 38.4% of samples of Bulgarian origin, the 3-MCPD content was above the EU limit of 20 µg kg⁻¹. In all analysed samples, 33.3% had a 3-MCPD content above the EU limit.


Assuntos
Condimentos/análise , Contaminação de Alimentos , Inspeção de Alimentos/métodos , Alimentos de Soja/análise , alfa-Cloridrina/análise , Métodos Analíticos de Preparação de Amostras , Bulgária , Condimentos/economia , Condimentos/microbiologia , Condimentos/normas , Dieta/etnologia , União Europeia , Fermentação , Cromatografia Gasosa-Espectrometria de Massas , Fidelidade a Diretrizes , Política de Saúde , Promoção da Saúde , Humanos , Limite de Detecção , Hidrolisados de Proteína/química , Hidrolisados de Proteína/metabolismo , Hidrolisados de Proteína/normas , Reprodutibilidade dos Testes , Extração em Fase Sólida , Alimentos de Soja/economia , Alimentos de Soja/microbiologia , Alimentos de Soja/normas , Proteínas de Soja/química , Proteínas de Soja/metabolismo , Proteínas de Soja/normas , Espectrometria de Massas por Ionização por Electrospray
19.
J Sci Food Agric ; 93(3): 535-41, 2013 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-22865342

RESUMO

BACKGROUND: Glutathione (GSH) is composed of the amino acids glutamic acid, cysteine and glycine. This study investigated the usability of chicken feather protein hydrolysate (chicken feather peptone, CFP) as a substrate for GSH production from Saccharomyces cerevisiae. RESULTS: CFP was found to be rich in ash (36.7 g per 100 g), protein (61.1 g per 100 g) and minerals (S, P, K, Ca, Fe, Na and Mg). It also had high contents of cysteine and glycine. CFP augmented biomass and GSH production by 53 and 115% respectively compared with the control medium. The highest biomass (17.4 g l(-1)) and GSH (271 mg L(-1)) concentrations were attained in CFP medium. The second highest biomass (16.8 g l(-1)) and GSH (255 mg L(-1)) concentrations were obtained in fish peptone medium. It was assumed that the high mineral, cysteine and glycine contents of CFP were related to cell growth and GSH synthesis in S. cerevisiae. CONCLUSION: This is the first report on the effect of cysteine- and glycine-rich protein hydrolysates on GSH production from S. cerevisiae. In this regard, CFP was tested for the first time as a GSH production substrate. As an additional contribution, a new hydrolysis process was developed for the preparation of protein hydrolysates.


Assuntos
Cisteína/metabolismo , Plumas/química , Glutationa/biossíntese , Glicina/metabolismo , Hidrolisados de Proteína/química , Saccharomyces cerevisiae/metabolismo , Animais , Galinhas , Custos e Análise de Custo , Cisteína/análise , Glutationa/economia , Glicina/análise , Hidrólise , Minerais/análise , Peptonas/metabolismo , Hidrolisados de Proteína/metabolismo
20.
Pediatr Allergy Immunol ; 23(3): 240-9, 2012 May.
Artigo em Inglês | MEDLINE | ID: mdl-22360663

RESUMO

OBJECTIVE: To estimate the cost-effectiveness of using an extensively hydrolysed formula (eHF; Nutramigen) compared with an amino acid formula (AAF; Neocate) as first-line treatment for cow milk allergy (CMA) in the UK, from the perspective of the National Health Service (NHS). METHOD: A decision model was constructed depicting the treatment paths and associated resource use attributable to first-line management of CMA with the two formulae. The model was based on the case records of 145 AAF-treated infants and 150 matched eHF-treated patients from The Health Improvement Network (THIN) database [a nationally representative database of patients registered with general practitioners (GPs) in the UK]. The model estimated the costs and consequences of patient management over 12 months following their initial GP visit for CMA. RESULTS: Patients presenting with a combination of gastrointestinal symptoms and eczema accounted for 44% of all patients in both groups. Those with gastrointestinal symptoms alone and eczema alone accounted for up to a further 39% and 13%, respectively. Those with urticaria and faltering growth accounted for <5% and ≤6% of all patients, respectively. Patients' age and weight at presentation was a mean 2.6-2.8 months and 4.4 kg, respectively. It took a mean 2.2 months to start a formula after initially seeing a GP. Time to symptom resolution following the start of treatment was 1.2 months in both groups; hence, the mean number of symptom-free months during the 12 months following the initial GP visit was estimated to be 8.6 months in both groups. Patients treated with an eHF had a mean 13.1 GP visits over the 12 months compared to 17.5 visits made by AAF-treated patients (p < 0.001). The NHS cost of managing a CMA infant over the first 12 months following initial presentation to a GP was estimated to be £1853 and £3161 for an eHF-treated and AAF-treated patient, respectively. CONCLUSION: Starting treatment for CMA with an eHF was the cost-effective option, as there were no significant differences in clinical outcomes between the two groups. A prospective, randomized controlled trial would allow a definitive confirmation of these findings.


Assuntos
Aminoácidos/economia , Carboidratos/economia , Gorduras na Dieta/economia , Alimentos Formulados/economia , Fórmulas Infantis/economia , Hipersensibilidade a Leite/dietoterapia , Hidrolisados de Proteína/economia , Aminoácidos/administração & dosagem , Aminoácidos/química , Animais , Carboidratos/administração & dosagem , Carboidratos/química , Bovinos , Análise Custo-Benefício , Gorduras na Dieta/administração & dosagem , Feminino , Humanos , Lactente , Alimentos Infantis/economia , Fórmulas Infantis/química , Recém-Nascido , Masculino , Hipersensibilidade a Leite/fisiopatologia , Hidrolisados de Proteína/administração & dosagem , Hidrolisados de Proteína/química , Reino Unido
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