Journal
FOOD CHEMISTRY
Volume 301, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2019.125278
Keywords
Grass carp; Myofibrillar structural proteins; Muscle ultrastructure; Myofibril fragmentation; Texture softening
Funding
- National Natural Science Foundation of China [NSFC 31701677]
- Postdoctoral Science Foundation of Jiangsu Province [1701098B]
- National Postdoctoral Science Foundation [2017M621634]
- China Agriculture Research System [CARS-45-26]
- National first-class discipline program of Food Science and Technology [JUFSTR20180201]
- Yi Tong-Jiangsu Postdoctoral Program
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Softening is always a problem in fish preservation. This study was aimed to investigate the role of myofibrillar structural proteins degradation in fish softening. The changes of myofibrillar structural proteins, muscle ultrastructure, myofibril fragmentation, and shear force were studied. The results indicated that during the superchilled preservation of grass carp (Ctenopharyngodon idella), small (low-molecular-weight) myofibrillar structural proteins like desmin and troponin-T initiated textural deterioration, leading to Z-disk weakening and actin loosening. In contrast, giant (high-molecular-weight) myofibrillar structural proteins like thin and nebulin were degraded in more amount in the later storage, contributing to Z-disk and M-band disassembly and vague of light and dark regions (I and A bands). Compared to each other, desmin and thin played more important part in softening. All these changes were involved in the increase of muscle fibril segments and the sharp decrease of shear force.
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