ACE-inhibitory activity of enzymatic protein hydrolysates from lupin and other legumes

Giovanna Boschin, Graziana Maria Scigliuolo, Donatella Resta, Anna Arnoldi

Research output: Contribution to journalArticle


The objective of this investigation was to compare the angiotensin converting enzyme (ACE)-inhibitory activity of the hydrolysates obtained by pepsin digestion of proteins of some legumes, such as chickpea, common bean, lentil, lupin, pea, and soybean, by using the same experimental procedure. The ACE-inhibitory activity was measured by using the tripeptide hippuryl-histidyl-leucine (HHL), as model peptide, and HPLC-DAD, as analytical method. The peptide mixtures of all legumes were active, with soybean and lupin the most efficient, with IC50 values of 224 and 226 μg/ml, respectively. Considering the promising results obtained with lupin, and aiming to identify the protein(s) that release(s) the peptides responsible for the activity, the peptides obtained from the pepsin digestion of some industrial lupin protein isolates and purified protein fractions were tested. The most active mixture, showing an IC50 value of 138 μg/ml, was obtained hydrolysing a mixture of lupin α + β conglutin.

Original languageEnglish
Pages (from-to)34-40
Number of pages7
JournalFood Chemistry
Publication statusPublished - 2014


  • Angiotensin converting enzyme (ACE)
  • Enzymatic protein hydrolysates
  • Hippuric acid
  • Hypertension
  • inhibitors
  • Legumes
  • Lupin
  • Pepsin
  • Protein isolates

ASJC Scopus subject areas

  • Food Science
  • Analytical Chemistry
  • Medicine(all)

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