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- W4220794356 abstract "This study investigated the relationship of secondary protein structures with textural attributes of chicken breast subjected to 6 freeze (-20 °C) thaw (4 °C for 12 h) cycles. 2DE identified 78 distinct protein spots. Moreover, WB indicated a remarkable increase in the degree of desmin degradation during multiple freeze-thaw (MFT). In addition, the TEM micrographs revealed that MFT remarkably increased the spacing between the muscle fibers, especially from cycles 3 to 5, slightly decreased H-zone, but a remarkable shrinkage of Z-lines, as well as degradation of myofibril structures (Z-line, I-bands, and M-lines). DSC showed shifts in first and second endothermic transition peaks during the 3rd and 5th cycles. Viscoelastic graphs revealed a cycle-dependent decrease in gel-forming ability (G') during MFT. Finally, the MFT chicken breast samples exhibited significantly decreased shear force in a cycle-dependent manner. This study highlighted the critical role of desmin in regulating myofibrillar degradation through various routes and mechanisms." @default.
- W4220794356 created "2022-04-03" @default.
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- W4220794356 date "2022-08-01" @default.
- W4220794356 modified "2023-09-26" @default.
- W4220794356 title "Desmin as molecular chaperone for myofibrillar degradation during freeze-thaw cycles" @default.
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- W4220794356 doi "https://doi.org/10.1016/j.foodchem.2022.132691" @default.
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