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Protein hydrolysates with ACE-I inhibitory activity from amaranth seeds fermented with Enterococcus faecium-LR9:
Dora Elisa Cruz-Casas1, Rodolfo Ramos-González2, Lilia Arely Prado-Barragán3
1School of Chemistry, Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico.
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.
