Angiotensin-Converting Enzyme Inhibition In Vitro by Protein Hydrolysates and Peptide Fractions from Mojarra of Nile Tilapia (Oreochromis niloticus) Skeleton.

Mojarra of Nile tilapia (Oreochromis niloticus) skeleton was used as protein source for the preparation of protein hydrolysates and peptide fractions with angiotensin-converting enzyme (ACE) inhibitory activity. The flour presented a content of 34.92% protein and a brightness (luminosity, L*) of 82.29. Protein hydrolysates were obtained from the protein-rich flour with the enzymes Flavourzyme® and Alcalase® reaching degree of hydrolysis (%DH) of 52% and 67% at 100 min of reaction, respectively. Both hydrolysates showed low-molecular-weight (MW) peptides estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The hydrolysates obtained with Flavourzyme at 60 min and at 80 min with Alcalase showed greater ACE inhibitory activity with IC50 values of 0.238 and 0.344 mg/mL, respectively. The peptide fraction A (MW >10 kDa) with Flavourzyme and fraction B (MW = 10-5 kDa) with Alcalase obtained by ultrafiltration of hydrolysates with higher DH presented IC50 of 0.728 and 0.354 mg/mL, respectively, whereas peptide fraction C (MW = 5-3 kDa) with both enzymes hydrolysates with greater ACE inhibitory activity showed IC50 values of 0.470 and 0.634 mg/mL. The components obtained in this study could be used as functional ingredients in the design and development of functional foods.

Antioxidant Activity of Collagen Extracts Obtained from the Skin and Gills of Oreochromis sp.

Efforts aimed at reduction of fishing waste generated during the evisceration and filleting are scarce. The fishing waste is used in the production of low value-added products, such as flours or silages. It is important to visualize an alternative and profitable use of this waste, as it constitutes a serious environmental problem. This research determined the antioxidant properties of collagenous extracts of skin and galls of Oreochromis sp. The raw materials were characterized by proximal chemical analysis. Three treatments were applied to extract the collagen: salt-soluble collagen, acid-soluble collagen (ASC), and pepsin-hydrolyzed collagen (PHC). The collagenous fractions were hydrolyzed (0.1% pepsin). The recovered collagen yield and antioxidant activity were determined to hydrolyzed collagen (HC) and nonhydrolyzed collagen (NHC). The ASC skin showed the highest extraction yield (3.02%). For galls, only the PHC extraction was feasible (0.16%). Antioxidant analysis of NHC did not reveal radical scavenging activities. HC displayed a 2,2-diphenyl-1-picrylhydrazyl %RSA of 22.58 (ASC skin) and 10.34% (PHC galls), and a 2,2'-azino-bis[3-ethylbenzothiazoline-6-sulfonic acid] %RSA of 30.40% (PHC skin) and 29.43% (PHC galls), respectively. The ASC skin and PHC gall extracts exhibited 94.40% and 81.54% in ferric-reducing antioxidant power, and 43.63 and 38.08 µg ascorbic acid equivalents per milli liter for total antioxidant capacity, respectively. The collagen extracts showed %RSA and chelation of pro-oxidant metal ions. Different mechanism of antioxidant action was identified for the extracts: radical scavengers for HC and metal ion chelators for NHC. In conclusion, red tilapia skin collagen is recommended as an active ingredient of nutraceuticals, pharmaceuticals, or functional foods, for the identified bioactive properties.

ACE-I Inhibitory Activity from Phaseolus lunatus and Phaseolus vulgaris Peptide Fractions Obtained by Ultrafiltration.

The involvement of angiotensin-I-converting enzyme (ACE-I) as one of the mechanisms controlling blood pressure is being studied to find alternative means of control of hypertension on human beings. On the market there are synthetic drugs that can control it, but these can cause undesirable health side effects. In this work was assessed the fractionation by ultrafiltration of the Lima bean (Phaseolus lunatus) and Jamapa bean (Phaseolus vulgaris), protein hydrolysates obtained with Alcalase(®) and Flavourzyme(®) on ACE-I inhibitory activity. Four membranes of different molecular cutoffs (10, 5, 3, and 1 kDa) were used. Fractions that had a higher inhibitory activity in both legumes were denominated as E (<1 kDa) with IC50 of 30.3 and 51.8 µg/mL values for the P. lunatus with Alcalase and Flavourzyme, respectively, and for the Phaseolus vulgaris with Alcalase and Flavourzyme with about 63.8 and 65.8 µg/mL values, respectively. The amino acid composition of these fractions showed residues in essential amino acids, which make a good source of energy and amino acids. On the other hand, the presence of hydrophobic amino acids such as V and P is a determining factor in the ACE-I inhibitor effect. The results suggest the possibility of obtaining and utilizing these peptide fractions in the development and innovation of a functional product that helps with treatment and/or prevention of hypertension.