Eggs provide various of nutrients for human beings, such as proteins, lipids, and vitamins. Besides of the processing properties from egg white, bioactive peptides obtained by the enzymatic hydrolysis method have diversiform biological functions. In this paper, biological functions such as of anti-oxidation, prevention of cardiovascular diseases, promoting mineral absorption, anti-diabetes, and regulating intestinal health were summarized, and the structure-activity relationships of egg white peptides from duck egg and chicken egg were also reviewed. It was found that egg white-derived angiotensin-converting enzyme (ACE) inhibitory peptides could affect their ACE inhibitory activity when the C-terminal was proline, leucine, and the N-terminal was aromatic or alkaline amino acid. Hydrophobic amino acids in N-terminal, and aromatic amino acids in the primary structure of antioxidant peptides from egg white can greatly improve the antioxidant capacity of the peptides. Glutamic acid in the first C-terminal, and phosphorylation of serine in the sequence of egg white-derived calcium absorption peptides have important contributions to the calcium absorption. However, bioactive peptides obtained by hydrolysis were confirmed to have different bioactivities, low yield and significantly different structures, making it difficult to obtain universal structure-activity relationship conclusions. Thus, the purpose of this paper is to provide a basis for the high-valued utilization of egg white, and a certain application for the production of egg white bioactive peptides as nutritional supplements, functional nutritional health products and therapeutic drugs, as well as to put forward a new prospect for the research of bioactive peptides.