Study on nucleotide, myofibrillar protein biochemical properties and microstructure of freeze-dried scallop striated muscle during storage and rehydration
[Display omitted] •The ATP content of dried scallops kept unchanged during storage at room temperature.•ATP decomposed rapidly during rehydration.•Ca2+-ATPase activity of dried scallop kept unchanged during rehydration process.•Rod of myosin was not stable during rehydration resulted in low salt sol...
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| Vydané v: | Food research international Ročník 158; s. 111461 |
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| Hlavní autori: | , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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Elsevier Ltd
01.08.2022
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| ISSN: | 0963-9969, 1873-7145, 1873-7145 |
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| Abstract | [Display omitted]
•The ATP content of dried scallops kept unchanged during storage at room temperature.•ATP decomposed rapidly during rehydration.•Ca2+-ATPase activity of dried scallop kept unchanged during rehydration process.•Rod of myosin was not stable during rehydration resulted in low salt solubility.
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. |
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| AbstractList | 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. [Display omitted] •The ATP content of dried scallops kept unchanged during storage at room temperature.•ATP decomposed rapidly during rehydration.•Ca2+-ATPase activity of dried scallop kept unchanged during rehydration process.•Rod of myosin was not stable during rehydration resulted in low salt solubility. 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. 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.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. |
| ArticleNumber | 111461 |
| Author | Yuan, Chunhong Yang, Wenge Golam Rasul, Md Wei, Huamao Sun, Zhongqi Huang, Tao Yamashita, Tetsuro Takaki, Koichi |
| Author_xml | – sequence: 1 givenname: Huamao surname: Wei fullname: Wei, Huamao organization: College of Food and Pharmaceutical Sciences, Ningbo University, 315211, China – sequence: 2 givenname: Md surname: Golam Rasul fullname: Golam Rasul, Md organization: Department of Fisheries Technology, Bangabandhu Sheikh Mujibur Rahman Agricultural University, Gazipur 1706, Bangladesh – sequence: 3 givenname: Zhongqi surname: Sun fullname: Sun, Zhongqi organization: College of Food and Pharmaceutical Sciences, Ningbo University, 315211, China – sequence: 4 givenname: Wenge surname: Yang fullname: Yang, Wenge organization: College of Food and Pharmaceutical Sciences, Ningbo University, 315211, China – sequence: 5 givenname: Tao surname: Huang fullname: Huang, Tao organization: College of Food and Pharmaceutical Sciences, Ningbo University, 315211, China – sequence: 6 givenname: Tetsuro surname: Yamashita fullname: Yamashita, Tetsuro organization: Faculty of Agriculture, Iwate University, Ueda 3-18-8, Morioka, Iwate 020-8550, Japan – sequence: 7 givenname: Koichi surname: Takaki fullname: Takaki, Koichi organization: Faculty of Science and Engineering, Iwate University, Ueda 4-3-5, Morioka, Iwate 020-8551, Japan – sequence: 8 givenname: Chunhong surname: Yuan fullname: Yuan, Chunhong email: chyuan@iwate-u.ac.jp organization: Faculty of Agriculture, Iwate University, Ueda 3-18-8, Morioka, Iwate 020-8550, Japan |
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•The ATP content of dried scallops kept unchanged during storage at room temperature.•ATP decomposed rapidly during rehydration.•Ca2+-ATPase... The biochemical properties and microstructural changes of freeze-dried Japanese scallop (Patinopecten yessoensis) striated muscle during room temperature... |
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| SubjectTerms | ambient temperature Ca2+-ATPase activity Chymotryptic digestion patterns digestion food research freeze drying freeze-thaw cycles Microstructure Mizuhopecten yessoensis muscles myosin rehydration Salt solubility scallops SDS-PAGE solubility striated muscle |
| Title | Study on nucleotide, myofibrillar protein biochemical properties and microstructure of freeze-dried scallop striated muscle during storage and rehydration |
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