Protein play an important role in determining structure and texture of various food
products. Therefore, the goals of this research were to study the functional properties of faba bean
protein cultivar, Giza3, compared to ß-Lactoglobulin (ß-Lg) and to hydrolyze this protein using pepsin
at different pH values (1.5 and 3) and different incubation periods (0, 5, 10, 60, and 180 min) to
characterize the resultant hydrolysates and evaluate their antioxidant activities. The solubility at
different pH, emulsifying properties, stability against creaming and oil droplets size, of faba bean
protein were tested compared to ß-Lg protein. The findings cleared that the solubility and emulsifying
properties of faba protein were very low compared to ß-Lg. Concerning to hydrolysis process, the
degree of hydrolysis at pH 1.5 was higher than that at pH 3. The molecular weight distribution bands
of faba protein hydrolysates were in the range of 9–98 kDa using SDS-PAGE method while, peptides
were in the range of 500 – 4000 Da using MALDI-TOF MS method. The results of both methods
confirmed that the hydrolysis at pH 1.5 was higher than pH 3. Moreover, the enzymatic hydrolysis
significantly improved the antioxidant activity of faba bean protein. Hydrolysates produced at pH 3
had a slight high antioxidant activity than at pH 1.5 at all incubation periods. Finally, these results
suggest that faba bean hydrolysates could be used in preparing functional foods and as natural
antioxidants to prevent oxidation process in food products.