Tratamento térmico e químico para controle da atividade da poligalacturonase no albedo do maracujá

The objective of this work was to evaluate the use of thermal and chemical treatments with Ca2+, in order to control the activity of polygalacturonase and its effects on extraction yield and degree of pectin esterification from albedo of yellow passion fruit (Passiflora edulis) rind. Rinds of fruit with light‑green peel were washed, sanitized, grind, and left to stand in water for albedo suspension. Albedo was collected and subjected to a temperature of 90oC for 30, 60, and 120 min, or to calcium levels of 0.01 and 1% during 1 hour of stirring, at 400 rpm, at ambient temperature. Thermal treatment of the crude enzymatic extract obtained from the albedo at 65, 75, and 85oC was also performed. The thermal treatment of the albedo at 90oC did not inactivate polygalacturonase after 120 min. The inactivation of the enzyme extracted from the albedo occurred after incubation at 65, 75, and 85oC for 30, 20, and 10 min, respectively. The treatment with calcium ion solution at 1% promoted enzymatic inactivation and a decrease in the content of free carboxylic acids (FCA) of pectin. The treatment of passion fruit albedo with calcium Ca2+ solution at 1% for 1 hour inhibits the polygalacturonase activity and decreases the content of FCA.O objetivo deste trabalho foi avaliar tratamentos térmicos e químicos com Ca2+, no controle da atividade da poligalacturonase e de seus efeitos no rendimento de extração e no grau de esterificação da pectina do albedo da casca de maracujá‑amarelo (Passiflora edulis). Utilizaram-se cascas de frutos com coloração verde‑clara, as quais foram lavadas, sanitizadas, trituradas e deixadas em repouso em água, para suspensão do albedo. O albedo foi recolhido e submetido à temperatura de 90oC a 30, 60 e 120 min, ou a concentrações de cálcio de 0,01 e 1% durante 1 hora de agitação de 400 rpm, em temperatura ambiente. Realizou-se, também, o tratamento térmico do extrato enzimático bruto obtido do albedo a 65, 75 e 85°C. O tratamento térmico do albedo a 90°C não inativou a poligalacturonase após 120 min. A inativação da enzima extraída do albedo ocorreu após incubação a 65, 75 e 85°C por 30, 20 e 10 min, respectivamente. O tratamento com íons de cálcio a 1% promoveu o bloqueio enzimático e a redução no conteúdo de ácidos urônicos livres (AUL) da pectina. O tratamento do albedo de maracujá com solução de 1% de Ca2+ por 1 hora inibe a atividade da poligalacturonase e reduz o conteúdo de AUL

Production of xylooligosaccharides from Brazilian Syrah grape pomace flour

BACKGROUND: The aim of this work was to determine the most favorable conditions for the production of xylooligosaccharides (XOS) from Brazilian Syrah grape pomace. Chemical processes were performed using a rotatable central composite design, where the concentration of sulfuric acid or concentration of sodium hydroxide and grape pomace flour: solvent mass ratio were the dependent variables. Enzymatic production was also evaluated using xylanase produced by Aspergillus niger 3T5B8 and Viscozyme® enzymatic commercial cocktail. RESULTS: Chemical extraction allowed to recover 21.8 to 74.6% and 5.2 to 96.3% of total XOS for acid and alkaline processes, respectively. Enzymatic production using xylanase extracted up to 88.68 ± 0.12% of total XOS and up to 84.09 ± 2.40% with Viscozyme®. CONCLUSION: The present study demonstrated different feasible methods to produce high added value molecules, the xylooligosaccharides, from Syrah grape pomace flour, valorizing this major by‐product. The use of enzymatic cocktails demonstrated to be an alternative to the conventional methods, allowing to obtain an eco‐friendly and sustainable grape pomace extract.info:eu-repo/semantics/acceptedVersio

Antioxidant dietary fibre recovery from Brazilian Pinot noir grape pomace

Brazilian grape pomace was extracted in hot water using a factorial design to evaluate polysaccharide recovery. Dependent variables were temperature, particle size and solute:solvent ratio. Polysaccharide yields varied from 3 to 10%, and the highest sugar content was observed when extraction was carried out at 100 °C, from fine particle sizes (≤249 μm), in a 1:12 solute:solvent ratio. Monosaccharide compositions of the flours afforded, in average, Rha,Ara,Xyl,Man,Gal,Glc,GalA in a 3:32:2:13:11:20:19 molar ratio, with varied Glc:GalA ratios. 13C NMR and HSQC spectra confirmed the presence of pectic and glucose-based polysaccharides in the extracts. Phenolic compounds were found after pomace extractions, and cathechin, gallic acid and epicatechin were the main identified compounds. Extracts also presented ABTS radical scavenging capacity (from 8.00 to 46.60 mMol Trolox/100g pomace), which means that these grape pomace flours are rich in antioxidant dietary fiber and have a potential use as food ingredients.Fil: Beres, Carolina. Universidade Federal do Rio de Janeiro. Centro de Tecnologia. Instituto de Química; BrazilFil: Beres, Carolina. Embrapa Agroindústria de Alimentos; Brazil.Fil: Simas-Tosin, Fernanda F. Universidade Federal do Paraná (UFPR). Departamento de Bioquímica e Biologia Molecular; Brazil.Fil: Cabezudo, Ignacio. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos (IPROBYQ-CONICET); Argentina.Fil: Freitas, Suely P. Universidade Federal do Rio de Janeiro. Centro de Tecnologia. Escola de Química; Brazil.Fil: Iacomini, Marcello. Universidade Federal do Paraná (UFPR). Departamento de Bioquímica e Biologia Molecular; Brazil.Fil: Mellinger-Silva, Caroline. Embrapa Agroindústria de Alimentos; Brazil.Fil: Cabral, Lourdes M. C. Embrapa Agroindústria de Alimentos; Brazil

Gastrointestinal digestion improving the antihypertensive activity of whey peptides

Whey proteins are byproducts of dairy industry, known for presenting bioactivity in several biological systems, including the cardiovascular. Its peptides are able to exert antihypertensive activity directly via the intestinal lumen and also after absorption. Despite all knowledge concerning whey peptides, there are only few products commercially available with this proposal, emphasizing the need of more studies regarding this theme. Aiming to make a better use of this agroindustrial byproduct, together with the need to meet the demands of this market, the present study proposed to evaluate the in vitro vasorelaxant activity of a whey hydrolysate during gastrointestinal digestion. A whey protein concentrate solution (1.25%w/w) was hydrolysed by a low-cost commercial pepsin (1.91%w/w, 37°C, 3h). The hydrolysate obtained was then spray-dried and submitted to in vitro static digestion, including oral, gastric and enteric phases. Samples were collected to chemical analysis and in vitro biological assays, using rat aortic rings. Non digested samples showed varied peptide profiles, with complete α-Lactalbumin hydrolysis and partial β-Lactoglobulin hydrolysis. During gastric digestion, more than 70 peptides were formed, ranging from high to low polarity and a β-Lactoglobulin hydrolysis was also observed. After the addition of pancreatin, peptides were extensively hydrolysed and 2 intense peaks were formed in 2.87 and 9.75min of a RP-HPLC run. The biological assays corroborate with the chromatographic analysis, as the vasorelaxation increased during the digestive process. Non digested samples showed a vasorelaxant activity of 80.45% ±7.12 (10mg.mL-1). This biofunctionality was maintained during in vitro gastric digestion (86.19% ±10.87; 10mg.mL-1, p>0.05), however an increase of approximately 100 times-fold was observed after the enteric phase, achieving 91.59% ± 9.90 (100μg.mL-1) of vasorelaxation. The results showed that the whey hydrolysate with reduced cost of production presented a high vasorelaxant activity after gastrointestinal digestion, which may be of great interest for food and nutraceutical industries

The Influence of Peptidases in Intestinal Brush Border Membranes on the Absorption of Oligopeptides from Whey Protein Hydrolysate: An Ex Vivo Study Using an Ussing Chamber

International audienceFor many years, it was believed that only amino acids, dipeptides, and tripeptides could be absorbed and thus reach the bloodstream. Nowadays, the bioavailability of oligopeptides is also considered possible, leading to new research. This pilot study investigates the activity of brush border enzymes on undigested whey protein hydrolysate (WPH) and on simulated intestinal digested (ID) whey hydrolysate and the subsequent absorption of resultant peptides through the proximal jejunum of a 7-week old piglet setup in an Ussing chamber model. Amongst all samples taken, 884 oligopeptides were identified. The brush border peptidase activity was intense in the first 10 min of the experiment, producing several new peptides in the apical compartment. With respect to the ID substrate, 286 peptides were detected in the basolateral compartment after 120 min of enzyme activity, originating from β-lactoglobulin (60%) and β-casein (20%). Nevertheless, only 0.6 to 3.35% of any specific peptide could pass through the epithelial barrier and thus reach the basolateral compartment. This study demonstrates transepithelial jejunum absorption of whey oligopeptides in an ex vivo model. It also confirmed the proteolytic activity of brush border enzymes on these oligopeptides, giving birth to a myriad of new bioactive peptides available for absorption

Extrusion of λ‐carrageenan gum : physical properties and in vitro bifidogenic effect

Extrusion was used as a tool for modifying carrageenan gum. Increased extrusion temperature and shear led to a considerable decrease in dissolution time (DT) (7,200 to 30 s) and faster solubilization (30 to 7 s) when coarse particle sizes (> 212 mu m) and hot water were used (p 38%), suggesting in vitro bifidogenic effect. In terms of industrial applications, extruded carrageenan is promising as a food supplement fiber product438COORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESFUNDAÇÃO CARLOS CHAGAS FILHO DE AMPARO À PESQUISA DO ESTADO DO RIO DE JANEIRO - FAPERJnão temE-26/112.069/201

Optimizing the development of an antihypertensive whey hydrolysate in semi-pilot scale

Whey proteins and peptides are byproducts of dairy industry recognized for reducing risk factors of numerous diseases, including hypertension Despite the need of better use of this agroindustrial residue and the high prevalence of hypertension worldwide, whey based-products that are able to modulate blood pressure are very scarce in food and nutraceutical markets, emphasizing the need of more research regarding this theme. The development of new products requires several stages in which scaling-up the production is comprised. In this manner, the present study proposed to optimize the process of development of a new antihypertensive whey hydrolysate in semi-pilot scale, assessing the influence of drying technologies and enzyme inactivation conditions on its biofunctionality. A commercial pepsin (1.91% w/w; 0.28μU.mL-1) was used to catalyse the hydrolysis of a 88% whey protein concentrate solution (1.25%; pH2, 1M HCl; 20L). Reactions occurred for 3h at 37°C, then the enzyme was inactivated either by increasing the temperature to 80°C/5min or the pH to 7 (5M NaOH).The drying method (freeze- and spray-drying) was also assessed concerning the vasorelaxant activity, which was evaluated in rat aortic rings. Peptide profiles of the samples inactivated by temperature were more varied than the chemically inactivated ones. In all samples α-Lactalbumin was completely hydrolyzed while β-Lactoglobulin remained partially resistant. Corroborating with the chemical analyses, hydrolysates thermally inactivated showed vascular relaxations of 72.06% ± 11.36 (freeze-dried) and 81.00% ± 14.27 (spray-dried) (p>0.05), while the samples inactivated by pH reached 20.6% ± 5.4 (freeze-dried) and -9.25% ± 10.18 (spray-dried) of vascular relaxation (p>0.05), which may be possibly related to the formation of NaCl. The results showed that it was possible to develop a whey protein hydrolysate in semi-pilot scale with high antihypertensive activity using a more affordable technology to food industrie