To explore the damage mechanisms of freeze-thaw cycles on cooked crayfish in frozen storage, changes in the phys-icochemical properties and structure of cooked crayfish during the freeze-thaw cycles were investigated....To explore the damage mechanisms of freeze-thaw cycles on cooked crayfish in frozen storage, changes in the phys-icochemical properties and structure of cooked crayfish during the freeze-thaw cycles were investigated. The phys-icochemical properties of cooked crayfish changed significantly after five freeze-thaw cycles. The moisture content, water holding capacity, pH, and textural properties were decreased, while the total color difference, drip loss, and pro-tein and lipid oxidation were significantly increased (P < 0.05). LF-NMR and MRI verified the water loss, and SDS-PAGE showed denaturation/degradation of myofibrillar proteins (MPs). Multiple freeze-thaw cycles promoted the transition from α-helix to β-turn in the secondary structure, the unfolding of tertiary structure, and a significant change in the chemical forces of MPs. SEM results revealed a disruption in the microstructure of muscle fibers. Repeated freeze-thaw cycles reduced the moisture content and distorted the structure of MPs in cooked crayfish, resulting in the disruption of physicochemical properties and its structure.展开更多
基金support from the Jiangsu Agricultural Science and Technology Innovation Fund[CX(21)2030]Basic Scientific Research Project of Jiangsu Academy of Agricultural Sciences[ZX(22)5004].
文摘To explore the damage mechanisms of freeze-thaw cycles on cooked crayfish in frozen storage, changes in the phys-icochemical properties and structure of cooked crayfish during the freeze-thaw cycles were investigated. The phys-icochemical properties of cooked crayfish changed significantly after five freeze-thaw cycles. The moisture content, water holding capacity, pH, and textural properties were decreased, while the total color difference, drip loss, and pro-tein and lipid oxidation were significantly increased (P < 0.05). LF-NMR and MRI verified the water loss, and SDS-PAGE showed denaturation/degradation of myofibrillar proteins (MPs). Multiple freeze-thaw cycles promoted the transition from α-helix to β-turn in the secondary structure, the unfolding of tertiary structure, and a significant change in the chemical forces of MPs. SEM results revealed a disruption in the microstructure of muscle fibers. Repeated freeze-thaw cycles reduced the moisture content and distorted the structure of MPs in cooked crayfish, resulting in the disruption of physicochemical properties and its structure.
