Investigating changes of proteome in the bovine milk serum after retort processing using proteomics techniques.

The objective of this study was to investigate the changes of the proteins in bovine milk serum after retort processing by label-free quantification proteomics techniques. A total of 96 and 106 proteins were quantified in control group (CG) and retort group (RG), respectively. Hierarchical clustering analysis of the identified milk serum proteins showed a decrease in the abundance of most proteins, such as serum albumin, lactoperoxidase, lactotransferrin, and complement C3, and an increase in the abundance of other proteins such as κ-casein, lipocalin 2, and Perilipin. Student's -test showed 21 proteins significantly differential abundance between CG and RG ( < .05), of which intensity-based absolute quantification (iBAQ) of five proteins decreased and iBAQ of 16 proteins increased. Bioinformatics analysis demonstrated that retort processing increased the digestibility of proteins, but this improvement was offset by a decrease in the digestibility of proteins caused by protein modification. Our results provide insight into the proteome of retort sterilized milk for the first time. Given the extremely high security of retort sterilized milk, the proteome of bovine milk serum changes after retort sterilization exposed in this study will contribute to the formula design of retort sterilized milk products.