Proteomics and microstructure profiling of Bactrian camel milk protein after homogenization

Abstract

In the present study, label-free quantification was used to study the protein changes in camel milk during homogenization. In the control and homogenization groups, we quantified 280 and 264 proteins, respectively between two groups. For the homogenization group, camel milk protein particles were smaller and more evenly distributed, and the ratio of each secondary structure of camel milk proteins changed compared with those in the control group. Proteomic analysis verified higher levels of FABP domain-containing protein, lactoperoxidase isoform 1 preproprotein, and lactoferrin in the control group than in the homogenization. For κ-casein, peptidoglycan-recognition protein, and Alpha-1-acid glycoprotein, the opposite result was observed. These proteins are associated with biological processes such as single organism process and cellular process. In the homogenized camel milk, significant changes were found in the proteome related to glycolysis/gluconeogenesis metabolism. The findings of the present study provide detailed information regarding the proteomic characteristics of homogenized camel milk.