Influence of pH on colour and iron content of peptide fractions obtained from bovine Hb concentrate hydrolysates

The effect of pH on colour and iron content (Fe) of peptide fractions obtained from bovine haemoglobin concentrate (BHC) hydrolysates was studied. Four hydrolysates were obtained using three enzymes: Protex- 6-L (P), Fungal?Protease?Concetrate (FC) and Flavourzyme (F). BHC and its hydrolysates (P, FC, P + F, FC + F) were fractioned at pH 4.5, 7.0 and 9.5. Solubility and Fe from different fractions were measured. Correlations between CIELAB colour parameters and Fe from different fractions were analysed. The colour from different fractions varied from red to yellow (a* and b* positives). Lightness values (L*) ranged from twenty-four to seventy. FC4.5 and FC + F4.5 fractions were the clearest and yellow (higher L*, b*, h), while BHC9.5 and P + F9.5 fractions had the lowest values of L*, b* and h. There was an inverse linear relationship between b* and L* parameters and Fe from fractions. This relationship could be associated with the pH of extraction. As pH increases Fe significantly increases and lower b* and L* values were obtained.Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: González, Rolando J.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentin

Bioactive properties of peptides obtained by enzymatic hydrolysis from protein

The traditional method to obtain phycocolloids from seaweeds implies successive extraction steps with cold and hot water. The first cold water extract has no phycocolloids but is rich in proteins and is considered a waste. Four hydrolysates were obtained using trypsin, alcalase and a combination of both sequentially added from a first cold water protein extract (PF) derived from Porphyra columbina. PF hydrolysates (PFH) were enriched in peptides with low molecular weight containing Asp, Ala and Glu. Both PF and PFH showed immunosuppressive effects on rat splenocytes as they enhanced IL-10 production while the production of TNFa and IFNg was inhibited. These immunosuppressive effects were higher for PFH. PFH had antihypertensive activity (> 35% of ACE inhibition) and antioxidant capacity (DPPH, TEAC, ORAC and copper-chelating activity). The hydrolysis could be used as a mean to obtain bioactive peptides from algae protein byproducts and to add value to the phycocolloids extraction process.Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Martínez Augustin, Olga. Universidad de Granada; EspañaFil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentin

Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry

The isolation and identification of cholesterol esterase (CE) and pancreatic lipase (PL) inhibitory peptides obtained from the protein hydrolysate of brewer's spent grain (BSG) was performed. BSG peptides were fractionated and purified sequentially by anion exchange, gel filtration (FPLC), and reversed phase high-performance liquid chromatography (RP-HPLC). The fractions obtained from each chromatographic step were collected and the in vitro enzyme inhibitory activity was evaluated. The chromatographic purification process increased the in vitro activities. The most active fractions were evaluated using MALDI-TOF tandem mass spectrometry, which identified three peptides: a peptide with the highest CE inhibition capacity (WNIHMEHQDLTTME) and two peptides with PL inhibition capacity (DFGIASF and LAAVEALSTNG). These three peptides showed hydrophobic and acidic amino acid residues (Asp and Glu) and/or their amines (Asn and Gln), which could be a common feature among lipid-lowering peptides related to CE and PL enzyme inhibition. The in silico studies showed that the three peptides had high hydrophobicity and were susceptible to enzymatic hydrolysis performed by trypsin, pepsin, and pancreatin. The BSG byproduct was a good source of CE and PL inhibitory peptides, thus adding value to this byproduct of the beer industry. This is the first report to demonstrate that BSG peptides can inhibit CE and PL enzymes. This journal isFil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Aquino, Marilín Estefanía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentin

Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion

The aim of this work was to evaluate the bio-accessibility of bioactive peptides with ACE I inhibition, antioxidant and antiplatelet aggregation activity obtained by enzymatic hydrolysis of Pyropia columbina proteins. Two hydrolyzates were produced (A and AF). Bio-accesibility was determined using a gastrointestinal digestion (pepsin and pancreatin) and membrane dialysis system. Hydrolyzates had peptides with medium molecular weight (2300 Da), and Asp, Glu and Ala were the most abundant amino acids. Additionally, AF presented small peptides with 287 Da. Peptides from A showed the highest angiotensin-converting enzyme activity (ACE I) inhibition by uncompetitive mechanism (IC50%, 1.2 ± 0.1 g L−1), and β-carotene bleaching inhibition. Peptides from AF presented the lower IC50% value for ABTS+• and DPPH radical inhibition, the highest copper-chelating activity (CCA), and antiplatelet aggregation activity. In vitro gastrointestinal digestion increased ABTS+• and DPPH scavenging and CCA of both hydrolyzates. Antiplatelet aggregation activity of A peptides was increased after simulated digestion process (≈157%). Peptides from both hydrolyzates were potentially bio-accessible, maintaining overall the bioactivity after gastrointestinal digesFil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Betancur, Ancona, David. Universidad Autónoma de Yucatán; MéxicoFil: Chel Guerrero, Luis. Universidad Autónoma de Yucatán; MéxicoFil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentin

Identification and in silico study of a novel dipeptidyl peptidase IV inhibitory peptide derived from green seaweed Ulva spp. hydrolysates

A number of functional foods containing seaweed-derived peptides are currently commercialized. Some seaweed derived peptide-containing products include Wakame peptide® and Nori peptide S®. To develop functional foods with the addition of Ulva spp. peptides, the isolation and identification of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from hydrolysates of this seaweed was performed. Ulva spp. peptides were fractionated and purified sequentially by anion exchange, ultrafiltration, and reversed phase high performance liquid chromatography. The fractions obtained from each analytical step were collected and the in vitro enzyme inhibitory activity was evaluated. The applied purification process increased the in vitro DPP-IV inhibitory activity. The inhibition mechanism of DPP-IV of the most active fraction was evaluated and it was analyzed by MALDI-TOF. A peptide SLAVSVH was identified. It has 57% of hydrophobic residues in their sequence (including Ala and branched chain amino acids), which could be a common feature among inhibitory peptides of DPP-IV. Molecular docking analysis showed that SLAVSVH/DPP-IV complex was stabilized by CH–π interactions between the side chains of Val6 with the indol of Trp629, and between rings of His7 with Trp563. The energy values obtained for the peptide under study indicate that it is a good candidate to inhibit DPP-IV.Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Nardo, Agustina Estefania. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Garzón, Antonela Guadalupe. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentin

Immunomodulatory properties of the protein fraction from Phorphyra columbina

The phycobiliproteins from Rhodophyta, R-phycoerythrin (R-PE) and C-phycocyanin (C-PC), have been shown to exert immunomodulatory effects. This study evaluated the effects of a Phorphyra columbina protein fraction (PF) and R-PE and C-PC on rat primary splenocytes, macrophages, and T-lymphocytes in vitro. PF featured various protein species, including R-PE and C-PC. PF showed mitogenic effects on rat splenocytes and was nontoxic to cells except at 1 g L-1 protein. IL-10 secretion was enhanced by PF in rat splenocytes, macrophages, and especially T-lymphocytes, whereas it was markedly diminished by R-PE and C-PC. The production of pro-inflammatory cytokines by macrophages was inhibited. The effect of PF on IL-10 was evoked by JNK/p38 MAPK and NF-κB-dependent pathways in macrophages and T-lymphocytes. It was concluded that PF has immunomodulatory effects on macrophages and lymphocytes that appear to be predominantly anti-inflammatory via up-regulated IL-10 production and cannot be accounted for by R-PE and C-PC.Fil: Cian, Raúl Esteban. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: López Posadas, Rocío. Universidad de Granada; EspañaFil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Sánchez De Medina, Fermín. Universidad de Granada; EspañaFil: Martínez Augustin, Olga. Universidad de Granada; Españ

Physical, structural and antioxidant properties of brewer's spent grain protein films

The development of brewer's spent grain protein (BSG‐PC) films with potential active packaging properties was investigated. Films were prepared by casting protein dispersions at different pH values (2, 8, 11), plasticizers [polyethylene glycol (PEG) or glycerol] and levels (0–0.25 g g−1) of PEG. Mechanical, water‐barrier and solubility, optical, antioxidant (reducing power, ABTS•+ and lipidic radical scavenging), and antimicrobial properties of films were determined. Also, the structural characteristics of films were evaluated by attenuated total reflectance‐Fourier transform infrared spectroscopy.Fil: Proaño Miniguano, Janina Lissette. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Salgado, Pablo Rodrigo. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Mauri, Adriana Noemi. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentin

Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH

The aims of this study were to assess bioactive properties (ACE inhibition and antioxidant capacity) from wheat gluten hydrolysate peptides fractionated by pH (4.0, 6.0 and 9.0), to determine peptide action mechanism, and to relate it to the secondary structure and functional groups of peptides. Gluten hydrolysate extracts (GHE) were enriched in peptideswith mediumhydrophobicity and molecularweight (≈60%MH and 5.5 kDa, respectively). Gluten peptides inhibited ACE I by uncompetitive mechanism and a direct relationship between α-helix structure and IC50% value was obtained (r = 0.9127). TEAC and cooper chelating activity from GHE 6.5 were the highest and directly correlated with MH peptides. GHE 9.0 had high carotene bleaching inhibition (47.5± 0.3%) and reducing power activity (163.1±2.9 mg S2O3 2 − equivalent g−1 protein), which were directly related to disulfide bonds content of peptides (r=0.9982 and 0.9216, respectively). pHwas a good alternative to select bioactive peptides from wheat gluten hydrolysate.Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Vioque, Javier. Consejo Superior de Investigaciones Cientificas; EspañaFil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentin