< 0.05). The addition of 30% ice was conducive to the increase of protein β-sheet proportion during heat treatment, exposing more reactive sulfhydryl groups. These promoted the combination of protein-protein through disulfide bonds and hydrophobic-hydrophobic interactions, forming an ordered three-dimensional gel network structure. Meanwhile, the increase in hydrogen bonds promoted the protein-water interaction. Low-field nuclear magnetic resonance analysis showed that more bound water was locked in the gel system, reducing the migration of immobile water to free water and finally showing better gel properties. When the amount of ice added was insufficient (20%), the gel structure lacked the support of immobile water, resulting in deterioration of gel strength. However, excessive addition of ice (>30%) was not conducive to the combination of protein-protein and protein-water, forming a large and rough gel structure, resulting in the migration of immobile water to free water and ultimately exhibited weak gel properties.
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Chen et al. (2021) studied this question.
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