Eggs are rich in proteins which are well balanced in terms of essential amino acids. In addition to the nutritional benefit, egg consumption might also help maintaining the good health of the nervous, endocrine, cardiovascular or immune systems, because of the biological properties of the peptides encrypted in the main egg proteins. The aim of this study was to simulate the complete hydrolysis of the major proteins found in the egg yolk and white, and to identify the peptides with promising bioactivity. The primary amino acid sequences of the proteins were selected from the UniProt database and hydrolysis was carried out using the Peptide cutter tool. The individual and cumulative action of the following proteases were considered in the study: pepsin, trypsin and chymotrypsin. The peptides released by the main digestive proteases were identified and their bioactivity was further evaluated through in silico approach using the BIOPEP-UWM database. 

The results indicated that small molecular weight hydrophobic peptides with 2 to 4 residues might exhibit antioxidant activity. Moreover, the peptides obtained from the egg white and yolk proteins might also exert antihypertensive activity, antimicrobial activity, anticancer activity or anti-inflammatory activity. 

The impact of the enzyme assisted hydrolysis on the antigenic properties of main allergens found in egg white was also checked. The results indicated that both pepsin and trypsin recognize various peptide bonds from the linear epitopes of ovomucoid and ovalbumin, therefore triggering the decrease of the antigenic properties of these allergens. In conclusion, egg proteins are valuable sources of biologically active peptides, which can be efficiently released thorough hydrolysis with pepsin, trypsin and chymotrypsin.