Loading...
6 results
Search Results
Now showing 1 - 6 of 6
- Enzymatic soy protein hydrolysis: a tool for biofunctional food ingredient productionPublication . Coscueta, Ezequiel R.; Campos, Débora A.; Osório, Hugo; Nerli, Bibiana B.; Pintado, ManuelaThis work aimed to evaluate the digestive stability of the peptides previously identified from a Corolase PP soy protein hydrolysate (SPH) and to respond to the uncertainty about the merit of controlled hydrolysis. For this purpose, we applied an empirical and theoretical analysis, determining peptide sequences, oxygen radical scavenging (ORAC) and ACE inhibitory (iACE) activities, and the effect of hydrolysis on solubility. Results showed that during digestion most of SPH peptides were degraded as smaller ones. However, both SPH bioactivities improved significantly after digestion (3.9 ± 0.1 μmol TE/mg protein for ORAC and IC50 = 52 ± 4μg protein/mL for iACE) with similar values for soy protein isolate (SPI). With respect to solubility, the controlled hydrolysis considerably increased this functional property. In conclusion, the results indicated that controlled enzymatic hydrolysis of SPI with Corolase PP produced an ingredient more apt to be incorporated in certain nutritional or nutraceutical formulations.
- Bioactive properties of peptides obtained from Argentinian defatted soy flour protein by Corolase PP hydrolysisPublication . Coscueta, Ezequiel R.; Amorim, Maria M.; Voss, Glenise B.; Nerli, Bibiana B.; Picó, Guillermo A.; Pintado, M. E.Enzymatic hydrolysis of soybean meal protein isolate (SPI) obtained under two temperature conditions with Corolase PP was studied, assessing the impact of hydrolysis on potential antioxidant and antihypertensive activities. The protein was isolated from soybean meal under controlled conditions of time and temperature (70 C, 1 h; 90 C, 30 min). Degree of hydrolysis assessed the progress of hydrolysis at different sampling times. For hydrolysates the antioxidant and angiotensin-converting-enzyme (ACE) inhibitory activities were measured. As observed, the DH was increasing until reaching 20% at 10 h with disappearance of globular proteins and generation of low molecular weight peptides (less than 3 kDa). A significant increase in antioxidant and ACE inhibitory capacities was observed. Five main peptides were identified, which may explain through their sequences the bioactive properties analyzed. Through this study was possible to obtain for the first time with Corolase PP soy hydrolysates with potential antioxidant and ACE inhibitory activities, which can be used to obtain new added value functional ingredients from soy meal.
- Optimization of bromelain isolation from pineapple byproducts by polysaccharide complex formationPublication . Campos, Débora A.; Coscueta, Ezequiel R.; Valetti, Nadia Woitovich; Pastrana-Castro, Lorenzo M.; Teixeira, José A.; Picó, Guillermo A.; Pintado, Maria ManuelaA simple method for bromelain extraction from industrial pineapple residues (stems and peels) was developed and optimized through factorial experimental design. The developed methodology, based on precipitation with carrageenan, represents an alternative to the use of organic solvents and inorganic salts (common industrial precipitation) and allows achieving extracts with high bromelain purity. High recovery yield – 80–90% - of active bromelain was obtained for both crude juices (stems and peels) making possible to obtain ca. 0.3 g of bromelain from 100 g of pineapple byproducts using a low polysaccharide concentration (0.2–0.3% w/v).
- Continuous method to determine the trypsin inhibitor activity in soybean flourPublication . Coscueta, Ezequiel R.; Pintado, Manuela E.; Picó, Guillermo A.; Knobel, Gastón; Boschetti, Carlos E.; Malpiedi, Luciana Pellegrini; Nerli, Bibiana B.The determination of trypsin inhibitor (TI) activity is of importance to evaluate the nutritional value of soybean flours. An analytical method, which involves a continuous spectrophotometric rate determination for trypsin activity against the substrate N-benzoyl-DL-arginine p-nitroanilide, is proposed as an alternative to the standard discontinuous assay. Stopping the reaction with acetic acid and a centrifugation/filtration step to decrease turbidity are not required, thus reducing costs and sample preparation time. The TI activity of different flour samples, determined by both assays, demonstrated to be statistically comparable, irrespective of the TI concentration level. The coefficients of variation of the novel method did not exceed 8% at any concentration level. The curves of progress reaction showed a non-linear behavior in samples without TI. A reduction of incubation time from 10min to 2min increased the method sensitivity and extended its linear range. A more economical, faster and simpler assay was developed.
- Cod skin collagen extraction and characterizationPublication . Coscueta, Ezequiel; Brassesco, María; Pintado, Manuela
- The Health-Promoting Potential of Salix spp. Bark Polar Extracts: Key Insights on Phenolic Composition and In Vitro Bioactivity and BiocompatibilityPublication . Ramos, Patrícia A. B.; Moreirinha, Catarina; Silva, Sara; Costa, Eduardo M.; Veiga, Mariana; Coscueta, Ezequiel R.; Santos, Sónia A. O.; Almeida, Adelaide; Pintado, M. Manuela; Freire, Carmen S. R.; Silva, Artur M. S.; Silvestre, Armano J. D.Salix spp. have been exploited for energy generation, along with folk medicine use of bark extracts for antipyretic and analgesic benefits. Bark phenolic components, rather than salicin, have demonstrated interesting bioactivities, which may ensure the sustainable bioprospection of Salix bark. Therefore, this study highlights the detailed phenolic characterization, as well as the in vitro antioxidant, anti-hypertensive, Staphylococcus aureus growth inhibitory effects, and biocompatibility of Salix atrocinerea Brot., Salix fragilis L., and Salix viminalis L. bark polar extracts. Fifteen phenolic compounds were characterized by ultra-high-performance liquid chromatography-ultraviolet detection-mass spectrometry analysis, from which two flavan-3-ols, an acetophenone, five flavanones, and a flavonol were detected, for the first time, as their bark components. Salix bark extracts demonstrated strong free radical scavenging activity (5.58–23.62 µg mL−1 IC50 range), effective inhibition on angiotensin-I converting enzyme (58–84%), and S. aureus bactericidal action at 1250–2500 µg mL−1 (6–8 log CFU mL−1 reduction range). All tested Salix bark extracts did not show cytotoxic potential against Caco-2 cells, as well as S. atrocinerea Brot. and S. fragilis L. extracts at 625 and 1250 µg mL−1 against HaCaT and L929 cells. These valuable findings can pave innovative and safer food, nutraceutical, and/or cosmetic applications of Salix bark phenolic-containing fractions.