Characterization and evaluation of immunotherapeutic potential of ovotransferrin PC2 (OTf PC2) were performed in this study. The ovoprotein was obtained from egg white from hens immunized with bacterial antigens, pathogenic for humans. For the negative control samples, OTf was extracted from eggs collected from Specific Pathogen-Free (SPF) hens and purified by affinity chromatography on Protein G-agarose column with two eluting peaks: I, representing ovalbumin, and II, ovotransferrin. The final apo-OTf form was reached by successive precipitation with ammonium sulfate and citric acid and the holo-OTf form by saturating the apo-form with FeCl3. Multiple OTf PC2 samples were analyzed through Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) and, based on the molecular marker migration model, the ovotransferrin (76.5 kDa) and ovalbumin (45 kDa) were detected. The agglutination reaction exhibited statistically significant high specificity of the multiple OTf PC2, by reacting with the antigens used for hens' immunization. Following ELISA, it was established that OTf PC2 from hyperimmune eggs has specificity for all antigens; the antibody titer was high, indicating that OTf PC2 possesses immunological properties similar to immunoglobulin Y (Ig Y). This study suggests that OTf PC2 immunological activity may play a crucial role in the prevention and treatment of infections resistant to antibiotics and OTf PC2 can also act as a valuable nutraceutical.