Quality changes and indicator proteins of Litopenaeus vannamei based on label-free proteomics analysis during partial freezing storage

Litopenaeus vannamei are known to deteriorate in quality during low-temperature storage. This study demonstrated the potential protein indicators of partial freezing of stored shrimp by traditional quality parameters and label-free based proteomic techniques. The carbonyl content and myofibril fragmentation index (MFI) of shrimp increased from 0.56 +/- 0.03 to 2.14 +/- 0.03 nmol/mg and 13.09 +/- 0.14 to 54.93 +/- 0.96, respectively. Within the extension of storage, the trichloroacetic acid (TCA), cooking loss and whiteness significantly increased. A total of 240 proteins changed in abundance at 10, 20, and 30 days compared to fresh samples. Projectin, ribosomal protein and histone were potential biomarkers for protein denaturation and oxidation in shrimp muscle. Myosin heavy chain and glyceraldehyde-3-phosphate dehydrogenase corresponded with the degradation of muscle proteins. Myosin light chain, tubulin alpha chain, and heat shock protein correlated with tenderness and water holding capacity; meantime, malate dehydrogenase and hemocyanin can serve as color indicators. Further study of the properties of these indicator proteins can inform their exploitation as quality indicator proteins during partial freezing storage.

Automated summary

This study demonstrated the potential protein indicators of partial freezing of stored shrimp by traditional quality parameters and label-free based proteomic techniques. The carbonyl content and myofibril fragmentation index (MFI) of shrimp increased significantly during storage. A total of 240 proteins changed in abundance at different time points compared to fresh samples. Projectin, ribosomal protein and histone were potential biomarkers for protein denaturation and oxidation in shrimp muscle. Myosin heavy chain and glyceraldehyde-3-phosphate dehydrogenase corresponded with the degradation of muscle proteins. Myosin light chain, tubulin alpha chain, and heat shock protein correlated with tenderness and water holding capacity, while malate dehydrogenase and hemocyanin can serve as color indicators.