89 immunoactive peptides available in the BIOPEP Database were bioinformatically analyzed. It was determined that potentially immunoactive peptide fragments were present in 90 of 150 sequences of the proteins analysed. In the sequences of immunoactive peptides studied, the following was analysed: peptide chain length, percent content of individual amino acids, pI, molar extinction coefficient, hydropathy index, and net charge. Furthermore, it was determined whether it was possible to in silico release those peptides using specific proteolytic enzymes. Based on the results of the computer analysis performed using a ProtParam software, it was confirmed that the immunoactive peptides were, mainly, hydrophilic fragments and in their sequence, the alkaline amino acids prevailed, such as: Arg, Lys, and Pro, with a positive net charge in neutral pH. A computer simulation of in silico proteolysis of 11 selected food proteins showing the highest occurrence frequency of immunoactive peptides (parameter A > 0.02) was performed and based thereon, it was proved that of all the enzymes available in the BIOPEP Database, only three proteolytic enzymes , i.e.: chymase (EC 3.4.21.39), pancreatic elastase (EC 3.4.21.36), and glycyl endopeptidase (EC 3.4.22.25) were able to release immunoactive peptides in one enzyme setup. The 2-3 amino acid peptide fragments were, mainly, produced during the hydrolysis of the analyzed proteins performed using proteolytic enzymes.