Investigating the migration hypothesis: Effects of trypsin-like protease on the quality of muscle proteins of red shrimp (Solenocera crassicornis) during cold storage.

This study aimed to investigate the effect of trypsin-like protease (TLP) on the quality of muscle proteins in red shrimp (Solenocera crassicornis) during cold storage. The results indicated that the activity of TLP decreased significantly in the head of shrimp but increased significantly in the muscle tissues during the cold storage. The myofibril fragmentation index (MFI) value of intact shrimp was significantly higher than that of beheaded shrimp, while the Ca2+-ATPase activity of intact shrimp was significantly lower than that of beheaded shrimp. SDS-PAGE analysis showed that the molecular weight of purified TLP from the shrimp head was about 24 kDa, and the TLP showed high activity at 50 °C and pH 8, indicating that the TLP belongs to the trypsin family. Results from in vitro simulation experiments indicated that the process of TLP incubation significantly reduced the particle size and enlarged the distribution of myofibrillar proteins (MPs) in shrimp muscle tissues. The comparisons were made with respect to the control samples. It can be inferred that TLP migrated from the shrimp head to the muscle tissues during storage and thus promoted the degradation of MPs in red shrimp. The beheading treatment could be an effective mean to maintain better quality and extend the commercialization of shrimp products.