1. Protein hydrolysates with ACE-I inhibitory activity from amaranth seeds fermented with Enterococcus faecium-LR9: Identification of peptides and molecular docking.
- Author
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Cruz-Casas DE, Ramos-González R, Prado-Barragán LA, Iliná A, Aguilar CN, Rodríguez-Herrera R, Tsopmo A, and Flores-Gallegos AC
- Subjects
- Peptidyl-Dipeptidase A chemistry, Peptidyl-Dipeptidase A metabolism, Plant Proteins chemistry, Plant Proteins metabolism, Enterococcus faecium metabolism, Enterococcus faecium chemistry, Angiotensin-Converting Enzyme Inhibitors chemistry, Angiotensin-Converting Enzyme Inhibitors metabolism, Angiotensin-Converting Enzyme Inhibitors pharmacology, Molecular Docking Simulation, Seeds chemistry, Seeds metabolism, Amaranthus chemistry, Peptides chemistry, Peptides metabolism, Peptides pharmacology, Protein Hydrolysates chemistry, Protein Hydrolysates metabolism, Fermentation
- Abstract
One of the causes of hypertension is the activity of angiotensin-I converting enzyme (ACEI), making its inhibition a crucial strategy for controlling the disease. Protein hydrolysates are a known source of bioactive peptides that contribute to ACE-I inhibition. This study aims to evaluate the ACE-I inhibitory activity of amaranth seed hydrolysates after fermentation with Enterococcus faecium-LR9 and to compare it with Leuconostoc mesenteroides-18C6 and enzymatic hydrolysis (Alcalase®). The fermentation strategy with LR9 proved to be more effective in inhibiting ACE-I (79.1 ± 2.6 %) in vitro compared to 18C6 (68.0 ± 9.8 %) and enzymatic hydrolysis (69.4 ± 1.2 %). Consequently, these protein hydrolysates were subjected to in silico analysis, identifying 125 novel peptides. Bioinformatics and molecular docking analyses revealed 10 peptides with high ACE-I inhibitory potential. Among them, the IFQFPKTY and VIKPPSRAW peptides stood out. Therefore, E. faecium-LR9 is a promising strain for the release of bioactive peptides from seed storage proteins., Competing Interests: Declaration of competing interest The authors declare that they have no conflict of interest., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2025
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