| Autor: |
Borges-Contreras B; 1 National Technology of Mexico/Technological Institute of Tuxtepec, Tuxtepec, Mexico., Martínez-Sánchez CE; 1 National Technology of Mexico/Technological Institute of Tuxtepec, Tuxtepec, Mexico., Herman-Lara E; 1 National Technology of Mexico/Technological Institute of Tuxtepec, Tuxtepec, Mexico., Rodríguez-Miranda J; 1 National Technology of Mexico/Technological Institute of Tuxtepec, Tuxtepec, Mexico., Hernández-Santos B; 1 National Technology of Mexico/Technological Institute of Tuxtepec, Tuxtepec, Mexico., Juárez-Barrientos JM; 2 National Technology of Mexico/Higher Technological Institute of Tierra Blanca, Tierra Blanca, Mexico., Guerra-Almonacid CM; 3 Department of Chemistry, Research Group in Natural Products, Faculty of Sciences, University of Tolima, Ibague, Colombia., Betancur-Ancona DA; 4 Department of Food Science, Faculty of Chemical Engineering, Autonomous University of Yucatan, Merida, Mexico., Torruco-Uco JG; 1 National Technology of Mexico/Technological Institute of Tuxtepec, Tuxtepec, Mexico. |
| Abstrakt: |
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 IC 50 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 IC 50 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 IC 50 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. |
