Comparative proteomics of goat milk during heated processing

Abstract

Milk proteins have shown to be very sensitive to heated processing. This study investigated the heat-dependent changes of goat milk proteins using label-free quantification (LFQ). A total of 843 proteins were identified in all the samples, of which 625 proteins were quantified. There were 527, 543, 537, 533 and 539 proteins quantified in the control group (CG) and heated groups (HGs: HG1, HG2, HG3 and HG4), respectively, and 438 proteins were common to all groups. The effects of high temperature/short time (HTST) treatment on proteins were similar to ultra-pasteurization (UP) and ultra-high temperature (UHT), but the low temperature/long time (LTLT) was different. Proteomics analysis demonstrated that heated processing increases the digestibility of proteins and is beneficial for anti-atherosclerosis therapy. These results expand the knowledge of the protein compositions from different heated processing. And it can further the utilization of the protein component of goat milk for human nutrition and health.

Keywords: Goat milk; LFQ; Pasteurization; Proteomics; UHT.