Maira Rubí Segura CamposCarlos Paul Espadas-AlcocerLuis Chel‐GuerreroDavid Betancur‐Ancona2026-03-222026-03-22201310.4236/as.2013.412105https://doi.org/10.4236/as.2013.412105https://andeanlibrary.org/handle/123456789/49246Citaciones: 6The hydrolysis of velvet bean (Mucuna pruriens) protein in the presence of Alcalase?-Flavourzyme? and Pepsin-Pancreatin was investigated. The results showed that Alcalase?-Flavourzyme? (29.08%) sequential system catalyzed the hydrolysis most efficiently that Pepsin-Pancreatin (24.78%). In addition, the higher ACE-I inhibitory activity was achieved with the sequential system Alcalase?-Flavourzyme? (33.13%). Furthermore, the concentration of peptides employing an ultrafiltration (UF) system or their purification by gel filtration chromatography showed that the oligomeric peptides with lower molecular weight registered the highest ACE-I inhibitory activity. It has been demonstrated that Mucuna pruriens protein hydrolysates could serve as a source of peptides with ACE inhibitory activity and this activity can be attributed mainly to the mixture of short peptides in the hydrolysate.enMucuna pruriensHydrolysateChemistryHydrolysisUltrafiltration (renal)Size-exclusion chromatographyChromatographyPeptidePepsinMucunaarticle