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Segura-Campos, M.R., Chel-Guerrero, L.A. and BetancurAncona, D.A. (2011) Purification of angiotensin I-converting enzyme inhibitory peptides from a cowpea (Vigna unguiculata) enzymatic hydrolysate. Process Biochemistry, 46, 864-872.
http://dx.doi.org/10.1016/j.procbio.2010.12.008

has been cited by the following article:

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

  AUTHORS: Maira Rubi Segura-Campos, Carlos Paul Espadas-Alcocer, Luis Chel-Guerrero, David Betancur-Ancona

  KEYWORDS: Velvet Bean; Mucuna pruriens; ACE-I Inhibition; Peptide Fractions; Enzymatic Hydrolysis

  JOURNAL NAME: Agricultural Sciences, Vol.4 No.12, December 25, 2013

  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.