Proteomic profiling of camel and cow milk proteins under heat treatment

• For camel milk, α-lactalbumin and peptidoglycan recognition protein were the proteins most affected by heat treatment.
• For cow milk, β-lactoglobulin and α-lactalbumin disappeared completely from the gel patterns.
• After heating caseins were kept intact to heat treatment for camel and cow milks.
• Bovine serum albumin disappeared in heated bovine milk while camel serum albumin existed in heated camel milk.

Cow and camel milk proteins before and after heat treatment at 80 °C for 60 min were identified using LC/MS and LC–MS/MS following monodimensional electrophoresis. The database used for the identification of camel and cow proteins was set from http://www.uniprot.org/. The obtained results showed that, after heating, camel milk at 80 °C for 60 min, camel α-lactalbumin (α-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA) was significantly diminished. When heating cow milk at 80 °C for 60 min, α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were not significantly detected. Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins were identified by LC–MS/MS. Casein fractions were kept intact under a heat treatment of 80 °C during 60 min of both camel and cow milks. Camel and bovine whey proteins were affected by a heat treatment of 80 °C for 60 min.