Role of the intestines on the muscle quality of Pacific white shrimp (Litopenaeus vannamei) during chilled storage: Physicochemical and label-free-based peptidomics analyses.

The effect of shrimp deveining on the quality of Pacific white shrimp muscle was investigated by analyzing the protein degradation during chilled storage via physicochemical and label-free peptidomics analyses. In this study, shrimp with intact intestines were in the control group (CS), while deveined shrimp (DS) were in the treatment group. The total viability count (TVC), total volatile base nitrogen (TVB-N) content, and trichloroacetic acid (TCA)-soluble peptide content in all of the shrimp groups gradually increased with prolonged chilled storage. However, in the later stages of chilled storage, the DS samples exhibited significantly lower TVB-N, total bacterial, and TCA-soluble peptide contents than the CS samples, indicating that deveining treatment effectively prolonged shrimp quality. The peptidomics analysis revealed varying degrees of protein hydrolysis in the DS and CS samples during chilled storage. A total of 396 differentially abundant peptides (DAPs) were identified in the DS compared with the CS, comprising 98 upregulated and 298 downregulated segments. This suggests that the removal of the intestine effectively inhibits protein hydrolysis. Gene ontology (GO) analysis suggested that the DAPs were mainly involved in catalytic activity, binding, and metabolic processes. The cluster of orthologous groups of protein (COG) analysis showed that the cytoskeleton dynamics of the muscle proteins underwent considerable alterations influenced by the shrimp's intestines during chilled storage.