The aim of this study was to compare the physicochemical parameters of milk samples of five different species: cow, goat, donkey, camel and human. Also the analysis of whey protein profile in different milk samples was performed by anion-exchange fast protein liquid chromatography (FPLC) while polyacrylamide gel electrophoresis was used to identify a single fraction. Camel milk was the most acid (pH 6.460±0.005) and the richest in total proteins (3.41±0.31 %) and ash (0.750±0.102 %), whereas donkey milk had a neutral pH (7.03±0.02) and characterised by low proteins (1.12±0.40 %) and fat (0.97±0.03 %) content, being very close to human milk. Proteomic analysis of cow, goat, donkey, camel and human milk highlighted significant interspecies differences. Camel milk was similar to human milk in lacking of β-lactoglobulin and richness of α-lactalbumin. The knowledge gained from the proteomic comparison of the milk samples analysed within this study might be of relevance, both, in terms of identifying sources of hypoallergenic alternatives to bovine milk and detection of adulteration of milk samples and products.

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The effect of a successive in vitro hydrolysis by pepsin and pancreatin on the free radical scavenging activity of camel milk casein was investigated in order to assess the effect of gastro-intestinal digestion. Hydrolysis of camel casein was controlled by reversed-phase high performance liquid chromatography. Anti-oxidant activity was measured by the 2,2'-azino-bis-(3-ethylbensothiazoline-6sulfonic acid) (ABTS) method. The Trolox equivalent antioxidant capacity (TEAC) values of camel casein and its hydrolysate were 1.6±0.12 µmol TE/mg protein and 0.25 µmol TE/µmol eq. NH 2 , respectively. After digestion, the scavenging activity of the casein peptides was more efficient than those reported in the literature regarding digestive hydrolysates of camel milk, colostrum and whey proteins.

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