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

Autor: Cruz-Casas DE; School of Chemistry, Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico., Ramos-González R; CONAHCYT-Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico., Prado-Barragán LA; Biotechnology Department, Biological. Health Sciences Division, Universidad Autónoma Metropolitana, Iztapalapa Campus, 09340 Ciudad de México, Mexico., Iliná A; 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., Aguilar CN; School of Chemistry, Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico., Rodríguez-Herrera R; School of Chemistry, Universidad Autónoma de Coahuila, Boulevard Venustiano Carranza e Ing. José Cárdenas Valdés s/n Col. República, 25280 Saltillo, Coahuila, Mexico., Tsopmo A; Food Science Program, Department of Chemistry, Carleton University, 1125 Colonel By Drive, Ottawa, ON K1S 5B6, Canada.. Electronic address: apollinaire.tsopmo@carleton.ca., Flores-Gallegos AC; 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: carolinaflores@uadec.edu.mx.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2024 Oct 09; Vol. 464 (Pt 1), pp. 141598. Date of Electronic Publication: 2024 Oct 09.
DOI: 10.1016/j.foodchem.2024.141598
Abstrakt: 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.)
Databáze: MEDLINE
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