College of Food and Pharmaceutical Sciences, Ningbo University, 315211, China; Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China.
Department of Fisheries Technology, Bangabandhu Sheikh Mujibur Rahman Agricultural University, Gazipur 1706, Bangladesh.
Food Res Int. 2022 Aug;158:111461. doi: 10.1016/j.foodres.2022.111461. Epub 2022 Jun 13.
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 Ca-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.
研究了在室温储存和复水过程中冻干日本帆立贝(Patinopecten yessoensis)横纹肌的生化特性和微观结构变化。结果表明,冻干贝肉中的 ATP 含量保持稳定,无显著差异(p>0.05)。然而,在复水的 1.5 分钟内,ATP 迅速分解,AMP 积累,并且随着复水时间的延长,AMP 分解逐渐产生 HxR 和 Hx。此外,糜蛋白酶消化图谱的结果表明,脱水后肌球蛋白的杆不稳定,反映出其盐溶性低于冷冻-解冻的贝肉。相比之下,肌球蛋白亚基-1(S-1)是稳定的,这表明冻干贝的 Ca-ATPase 活性常数在整个储存和复水过程中保持不变(p>0.05)。此外,微观结构分析表明,脱水过程后冻干贝的 Z 线断裂。这项研究可能对未来开发高质量的脱水贝肉有帮助。