Proteomics and microstructure profiling of goat milk protein after homogenization.

ABSTRACT

This study investigated the protein changes in goat milk during the homogenization process using label-free quantification. We quantified 310 and 315 proteins in the control group (CG) and homogenized group (HG), respectively, and 16 proteins were significantly different between the 2 groups. For HG, the goat milk protein particle sizes were smaller and more evenly distributed and exhibited an increase in the regular arrangement of the secondary structures. Proteomics analysis verified that xanthine dehydrogenase and asparaginase-like 1 expression in CG were higher than in HG, whereas the opposite was observed for fructose-bisphosphate aldolase, κ-casein, and ß-casein. Significant changes were found in the homogenization-treated goat milk proteome that were related to goat milk glycolysis/gluconeogenesis metabolism. This work provides updated information on the current proteome characteristics of homogenized goat milk, which may be important for applying the protein component of goat milk to human nutrition and health.