Functional Properties of Faba Bean Protein and Effect of Enzymatic Hydrolysis on Its Antioxidant Activity

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