Abstract

Among 26 sous-vide cooking conditions of scallop adductor muscle (SAM), 65 °C-5.5 h, 70 °C-1.5 h and 100 °C-5 min were selected by the differential scanning calorimetry analysis. After sous-vide cooking, the shear force, hardness, springiness, cohesiveness, chewiness and recoverability of SAM increased significantly compared to fresh sample. The cooking also changed the secondary structures of the proteins in SAM with the rising β-sheet and descending α-helix, and the chemical interactions with the rising hydrophobic interactions and disulfide bonds but the descending ionic bonds and hydrogen bonds. These caused the longitudinal shrinkage and transverse aggregation of muscle fibers, and the aggregation and cross-linking between myofibrils which led to the squeeze of immobile water from myofibril network structure. This indicated that the denaturation, oxidation, aggregation and cross-linking of proteins caused by heat treatment changed the microstructure and water distribution, which contributed to the increased textural indicators of sous-vide cooked SAM.

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