Objective: Dromedary milk has a good nutritive value and is free of b-lactoglobulin (b-Lg), which is considered one of the major antigens of cow's milk proteins responsible for the incidence of allergy in infancy. In this work, we try to assess the in vitro gastrointestinal digestion of dromedary's whey proteins.Methods: The dromedary and bovine whey proteins were subjected to two successive hydrolysis: pepsic followed by the mixture of trypsin/chymotrypsin. The kinetics of degradation was determined, then the degree of hydrolysis (DH) and the peptide chains length (PCL) was calculated. SDS-PAGE was carried out to evaluate the specific protein composition before and after degradation.Results: The determination of α-NH2 free functions and DH shows that the dromedary's whey proteins are more susceptible to pepsin digestion (***p<0.001, *p<0.05/ **p<0.01, *p<0.05), and combined trypsin/chymotrypsin digestion (***p<0.001, **p<0.01/ **p<0.01, **p<0.01) compared to bovine whey proteins digestibility. In the other hand, the PCL of the dromedary hydrolysates obtained are shorter than those of the bovine hydrolysates. The electrophoretic profile of native dromedary's whey proteins shows the absence of the b-Lg and the presence of specific proteins (CWBP: Camel Whey Basic Protein, PGRP: Peptidoglycan Recognition Protein and WAP: Whey Acidic Protein), Also, we observed in the electrophoretic gels that a new band was present and could correspond to new peptide generated after the peptic hydrolysis of dromedary's whey proteins.Conclusion: The gastrointestinal digestion of the two whey is important with higher DH of dromedary's whey proteins and PCL almost identical at the end of digestion.Â
