Protein hydrolysates with ACE-I inhibitory activity from amaranth seeds fermented with Enterococcus faecium-LR9: Identification of peptides and molecular docking

Dora Elisa Cruz-Casas; Rodolfo Ramos-González; Lilia Arely Prado-Barragán; Anna Iliná; Cristóbal N Aguilar; Raúl Rodríguez-Herrera; Apollinaire Tsopmo; Adriana Carolina Flores-Gallegos

doi:10.1016/j.foodchem.2024.141598

Protein hydrolysates with ACE-I inhibitory activity from amaranth seeds fermented with Enterococcus faecium-LR9: Identification of peptides and molecular docking

Food Chem. 2025 Feb 1;464(Pt 1):141598. doi: 10.1016/j.foodchem.2024.141598. Epub 2024 Oct 9.

Authors

Dora Elisa Cruz-Casas¹, Rodolfo Ramos-González², Lilia Arely Prado-Barragán³, Anna Iliná⁴, Cristóbal N Aguilar¹, Raúl Rodríguez-Herrera¹, Apollinaire Tsopmo⁵, Adriana Carolina Flores-Gallegos⁶

Affiliations

¹ School of Chemistry, Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico.
² CONAHCYT-Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico.
³ Biotechnology Department, Biological. Health Sciences Division, Universidad Autónoma Metropolitana, Iztapalapa Campus, 09340 Ciudad de México, Mexico.
⁴ Nanobioscience Group, School of Chemistry, Universidad Autónoma de Coahuila. Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico.
⁵ Food Science Program, Department of Chemistry, Carleton University, 1125 Colonel By Drive, Ottawa, ON K1S 5B6, Canada.. Electronic address: [email protected].
⁶ School of Chemistry, Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico. Electronic address: [email protected].

PMID: 39413603
DOI: 10.1016/j.foodchem.2024.141598

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.

Keywords: Amaranth; Antihypertensive peptides; Enterococcus faecium; Protein hydrolysates.

MeSH terms

Amaranthus* / chemistry
Angiotensin-Converting Enzyme Inhibitors* / chemistry
Angiotensin-Converting Enzyme Inhibitors* / metabolism
Angiotensin-Converting Enzyme Inhibitors* / pharmacology
Enterococcus faecium* / chemistry
Enterococcus faecium* / metabolism
Fermentation*
Molecular Docking Simulation*
Peptides* / chemistry
Peptides* / metabolism
Peptides* / pharmacology
Peptidyl-Dipeptidase A / chemistry
Peptidyl-Dipeptidase A / metabolism
Plant Proteins / chemistry
Plant Proteins / metabolism
Protein Hydrolysates* / chemistry
Protein Hydrolysates* / metabolism
Seeds* / chemistry
Seeds* / metabolism

Substances

Angiotensin-Converting Enzyme Inhibitors
Peptides
Protein Hydrolysates
Peptidyl-Dipeptidase A
Plant Proteins