Preparation Methods, Inhibitory Activity, and Regulatory Mechanisms of Angiotensin-Converting Enzyme Inhibitory Peptides Derived from Eggs

Hypertension remains a major global health challenge, driving the ongoing search for safer and more effective dietary interventions as alternative therapies to synthetic drugs. Eggs are widely recognised as an excellent source of high-quality protein, and their bioactive peptides exhibit significant antihypertensive potential. This review makes a significant contribution to the field by systematically integrating and analysing egg-derived angiotensin-converting enzyme inhibitory peptides (ACEIPs) discovered over the past decade. We analyzed and compared ACEIPs from different egg components, including albumin, ovalbumin, lysozyme in egg white, as well as egg yolk and shell membrane. The structure-activity relationships between peptide sequences, structural features (such as C-terminal hydrophobic residues) and inhibitory efficacy was elucidated. Furthermore, this review examines the antihypertensive mechanisms of these bioactive peptides from a multidimensional perspective. This encompasses the classical ACE/Ang II/Angiotensin II Type 1 Receptor(AT1R) and ACE2/Ang(1-7)/Mas receptor (MasR) pathways, anti-inflammatory and antioxidant mechanisms, as well as the key signalling pathways such as NF-κB and p38/Mitogen-activated protein kinase (MAPK). A further distinctive contribution lies in comprehensively summarising cutting-edge identification and evaluation strategies, including molecular docking, quantitative structure-activity relationship (QSAR) modelling, and integrated models utilising spontaneously hypertensive rats. In summary, this review provides essential guidance for future applications of egg-derived ACEIPs in functional foods and therapeutic agents.