Identification of ACE-inhibitory peptides from Phaseolus vulgaris after in vitro gastrointestinal digestion

Int J Food Sci Nutr. 2015;66(7):774-82. doi: 10.3109/09637486.2015.1088940. Epub 2015 Sep 23.


The objective of this study was to identify the angiotensin I-converting enzyme (ACE)-inhibitory peptides released from thermally treated Phaseolus vulgaris (pinto) whole beans after in vitro gastrointestinal digestion. The degree of hydrolysis increased during digestion reaching a value of 50% at the end of the pancreatic digestion. The <3 kDa fraction of the postpancreatic sample showed high ACE-inhibitory activity (IC50 = 105.6 ± 2.1 μg of peptides/mL). Peptides responsible for the ACE-inhibitory activity were isolated by reverse-phase high-performance liquid chromatography (HPLC). Three fractions, showing the highest inhibitory activity, were selected for tandem mass spectrometry (MS/MS) experiments. Eleven of the identified sequences have previously been described as ACE-inhibitors. Most of the identified bioactive peptides have a hydrophobic amino acid, (iso)leucine or phenylalanine, or proline at the C-terminal position, which is crucial for their ACE-inhibitory activity. The sequence of some peptides allowed us to anticipate the presence of ACE-inhibitory activity.

Keywords: Common bean; hypertension; mass spectrometry; peptides; proteolysis.

MeSH terms

  • Amino Acid Sequence
  • Angiotensin-Converting Enzyme Inhibitors / metabolism*
  • Animals
  • Blood Pressure
  • Chromatography, High Pressure Liquid
  • Digestion
  • Hydrolysis
  • Hydrophobic and Hydrophilic Interactions
  • Hypertension / prevention & control
  • In Vitro Techniques
  • Molecular Structure
  • Pancreas
  • Peptides / metabolism
  • Peptides / pharmacology*
  • Peptides / therapeutic use
  • Peptidyl-Dipeptidase A / metabolism*
  • Phaseolus / chemistry*
  • Plant Proteins / metabolism*
  • Proteolysis
  • Rabbits
  • Swine
  • Tandem Mass Spectrometry


  • Angiotensin-Converting Enzyme Inhibitors
  • Peptides
  • Plant Proteins
  • Peptidyl-Dipeptidase A