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Isolated, identification and molecular docking of bioactive peptides of secondary whey of Oaxaca cheese as inhibitors of the angiotensin-I converted enzyme
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DOI：10.1007/s00217-026-05227-0.png)
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Abstract
En 中文
Because high blood pressure is the leading cause of death in the world, there is currently an interest in studying natural inhibitors of the angiotensin-I converting enzyme for the treatment and/or prevention of high blood pressure. To identify new inhibitors, proteins from the primary and secondary whey of fresh, panela, and Oaxaca cheeses were evaluated. The whey proteins were hydrolyzed with digestive enzymes (trypsin, chymotrypsin, and pepsin). Pepsin hydrolysis of primary whey of fresh cheese and the secondary whey of Oaxaca cheese showed the highest angiotensin-I converting enzyme inhibitory activities (44.8% and 53.8%, respectively), compared to the other treatments, and an IC50 of 84.8 μg/mL for peptides derived from Oaxaca cheese. Molecular docking results revealed that the IYLL peptide from Oaxaca cheese exhibited the best binding energy (− 11.1 kcal/mol) compared to the FDK peptide from fresh cheese (− 10.6 kcal/mol). However, docking scores do not directly correlate with biological activity and require experimental validation. The data show the functionality of the primary and secondary whey hydrolysates of fresh, panela and Oaxaca cheeses as antihypertensive agents.
Keywords:
Cheese
Whey
Enzymatic hydrolysis
Antihypertensive peptides
Molecular docking
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