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

  • Segura-Campos M
  • Espadas-Alcocer C
  • Chel-Guerrero L
  • et al.
N/ACitations
Citations of this article
13Readers
Mendeley users who have this article in their library.

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.

Cite

CITATION STYLE

APA

Segura-Campos, M. R., Espadas-Alcocer, C. P., Chel-Guerrero, L., & Betancur-Ancona, D. (2013). ACE-I inhibitory peptide fractions from enzymatic hydrolysates of velvet bean (<i>Mucuna pruriens</i>). Agricultural Sciences, 04(12), 767–773. https://doi.org/10.4236/as.2013.412105

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free