Effect of water change on quality deterioration of Pacific white shrimp (Litopenaeus vannamei) during partial freezing storage.

The correlation between water changes and quality deterioration of Litopenaeus vannamei during partial freezing storage was evaluated in this study. Significant increases in cross-sectional area and equivalent diameter are detected, but the roundness and longiness of the ice crystals show irregular growth. Within the extension of storage, the bound water (T2b) and immobilized water (T21) decreased significantly. However, the free water (T22) increased significantly. Quality determination showed significant decrease in total sulfhydryl and Ca2+-ATPase, but significant increase in disulfide bonds during storage. Correlation analysis revealed that cross-sectional area showed significant negative correlation with total sulfhydryl and Ca2+-ATPase, while significant positive correlation with disulfide bonds, respectively. The correlation between water distribution index and Ca2+-ATPase, disulfide bonds was significant, respectively. Predicted models for the growth of ice crystals with respect to cross-sectional area and equivalent diameter size have been developed with the help of the Arrhenius model.

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.