Study on nucleotide, myofibrillar protein biochemical properties and microstructure of freeze-dried scallop striated muscle during storage and rehydration

The biochemical properties and microstructural changes of freeze-dried Japanese scallop (Patinopecten yessoensis) striated muscle during room temperature storage and rehydration were investigated. The results showed that the content of ATP in freeze-dried scallop muscle remained stable with no significant difference (p > 0.05). However, ATP was rapidly decomposed and AMP accumulated within 1.5 min of rehydration, and HxR and Hx were gradually produced from AMP decomposition with the extension of rehydration time. Besides, the results of chymotryptic digestion patterns demonstrated that the rod of myosin was unstable after dehydration, reflecting lower salt solubility than that of frozen-thawed scallop. In contrast, the myosin subfragment-1 (S-1) was stable, as indicated by the constant of Ca2+-ATPase activity of freeze-dried scallops throughout the storage and rehydration (p > 0.05). Furthermore, the microstructural analysis revealed that the Z line of the freeze-dried scallop was broken after dehydration process. This study might be useful for developing high-quality dehydrated scallops in the future.

Automated summary

This study investigated the biochemical properties and microstructural changes of freeze-dried Japanese scallop muscle during room temperature storage and rehydration. The results showed that ATP content remained stable in freeze-dried scallop muscle, but rapidly decomposed during rehydration, leading to the accumulation of other compounds. The stability of myosin rod and myosin subfragment-1 (S-1) differed after dehydration, and microstructural analysis revealed the breakage of the Z line in freeze-dried scallops.