Angiotensin-I converting enzyme inhibitory activity of Amaranthus hypochondriacus seed protein hydrolysates produced with lactic bacteria and their peptidomic profiles

Food Chem. 2021 Nov 30;363:130320. doi: 10.1016/j.foodchem.2021.130320. Epub 2021 Jun 6.


The aim of this work was to determine the in vitro antihypertensive activities of lactobacillus (L. plantarum and L. helveticus) prepared amaranth protein hydrolysates, to determine the contribution of zinc, and to identify peptides. Depending on the bacteria species and the duration of the hydrolysis, up to 45.9% inhibition of angiotensin converting enzyme (ACE) was obtained. Size separation of the most active hydrolysates to yield < 1, <3-1, <3, <10-3 and < 10 kDa fractions enhanced ACE inhibition by 2-fold. A mixed mechanism of inhibition is proposed due to low correlation of ACE and zinc chelation. Thirty-six peptides were identified in the fractions using tandem mass spectrometry. A bioinformatic analysis showed the presence of encrypted fragments such as GVSEE or VNVDDPSK with known ACE-inhibitory properties. In conclusion, lactic acid bacteria proteases released peptides from amaranth proteins with ACE-inhibitory properties that were related to the presence of peptides with known or predicted ACE-inhibitor motifs.

Keywords: ACE inhibition; Amaranth seed protein; Bioactive peptides; Hydrolysates; Zinc chelating.

MeSH terms

  • Amaranthus*
  • Angiotensins
  • Hydrolysis
  • Lactobacillus
  • Protein Hydrolysates*
  • Seeds


  • Angiotensins
  • Protein Hydrolysates