ACE-I inhibitory peptide fractions from enzymatic hydrolysates of velvet bean ( Mucuna pruriens)

Abstract

The 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.