Identification of the Bioavailable Peptidome of Chia Protein Hydrolysate and the In Silico Evaluation of Its Antioxidant and ACE Inhibitory Potential

J Agric Food Chem. 2024 Feb 14;72(6):3189-3199. doi: 10.1021/acs.jafc.3c05331. Epub 2024 Feb 2.

Abstract

The incorporation of novel, functional, and sustainable foods in human diets is increasing because of their beneficial effects and environmental-friendly nature. Chia (Salvia hispanica L.) has proved to be a suitable source of bioactive peptides via enzymatic hydrolysis. These peptides could be responsible for modulating several physiological processes if able to reach the target organ. The bioavailable peptides contained in a hydrolysate obtained with Alcalase, as functional foods, were identified using a transwell system with Caco-2 cell culture as the absorption model. Furthermore, 20 unique peptides with a molecular weight lower than 1000 Da and the higher statistical significance of the peptide-precursor spectrum match (-10 log P) were assessed by in silico tools to suggest which peptides could be those exerting the demonstrated bioactivity. From the characterized peptides, considering the molecular features and the results obtained, the peptides AGDAHWTY, VDAHPIKAM, PNYHPNPR, and ALPPGAVHW are anticipated to be contributing to the antioxidant and/or ACE inhibitor activity of the chia protein hydrolysates.

Keywords: ACE; DPPH; bioactive peptides; identification; protease; subtilisin.

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry
  • Antioxidants* / chemistry
  • Antioxidants* / pharmacology
  • Caco-2 Cells
  • Humans
  • Hydrolysis
  • Peptides / chemistry
  • Protein Hydrolysates* / chemistry

Substances

  • Protein Hydrolysates
  • Antioxidants
  • Angiotensin-Converting Enzyme Inhibitors
  • Peptides