Whey-Derived ACE-I Inhibitory Peptides, Advances in LAB Fermentation and Structural Insights: A Mini-Review

Hypertension is a major global risk factor for cardiovascular disease, and inhibiting angiotensin-converting enzyme I (ACE-I) is a key therapeutic strategy. Natural ACE-I inhibitors, particularly bioactive peptides from dietary proteins, offer a promising alternative to synthetic drugs. Whey proteins are valuable precursors due to their unique amino acid composition, and fermentation with lactic acid bacteria (LAB) facilitates the release of peptides through proteolytic activity. Over the past 15 years, approximately 102 ACE-I inhibitory peptides have been identified from LAB-fermented whey. Studies have shown that the inhibitory activity of these peptides shows good bioavailability, structural stability, and low toxicity. This review analyzed ACE-I inhibitory peptides derived from LAB-fermented whey, focusing on fermentation conditions, peptide characteristics, and the molecular mechanisms of ACE-I inhibition. Emphasizing the integration of in vitro and in vivo studies and molecular docking simulations. Our analysis confirms that fermentation-based products represents a sustainable biotechnological approach to manage hypertension.