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Chemical interactions and protein conformations changes during the formation of silver carp surimi gel were studied by textural analysis, chemical methods, laser Raman spectroscopy, and circular dichrosim. The optimum setting time at 40°C was 60 min. During surimi gel formation, ionic bonds and hydrogen bonds decreased significantly (P ≤ 0.05), while hydrophobic interactions, disulfide bonds, and non-disulfide covalent bonds increased significantly (P ≤ 0.05). Hydrophobic interactions, disulfide bonds, and non-disulfide covalent bonds were the main chemical interactions maintaining the stable structure of surimi gel. Secondary structural analysis of surimi protein showed that 94.11% α-helix existed in native myosin and it partly changed into β-turn and random coil during heating. Myosin gel was made up of 33.70% α-helix, 12.40% β-turn and 53.90% random coil. These three kinds of secondary structures were the main protein conformations in surimi gel.
Liu et al. (2013) studied this question.