AS  Vol.4 No.12 , December 2013
ACE-I inhibitory peptide fractions from enzymatic hydrolysates of velvet bean (Mucuna pruriens)

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.

Cite this paper: Segura-Campos, M. , Espadas-Alcocer, C. , Chel-Guerrero, L. and Betancur-Ancona, D. (2013) ACE-I inhibitory peptide fractions from enzymatic hydrolysates of velvet bean (Mucuna pruriens). Agricultural Sciences, 4, 767-773. doi: 10.4236/as.2013.412105.

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