Abstract
This study aims to elucidate the mechanism behind the deterioration in the gel properties of collagen gel resulting from high-temperature treatment. The results show that the high level of triple-helix junction zones and related lateral stacking contribute to the dense and orderly collagen gel network with high gel strength and storage modulus. The analysis of the molecular properties of heated collagen shows that high-temperature treatment leads to serious denaturation and degradation of collagen, resulting in the formation of gel precursor solutions composed of low-molecular-weight peptides. The short chains in the precursor solution are not easy to nucleation and can limit the growth of triple-helix cores. To conclude, the decrease in triple-helix renaturation and crystallization abilities of peptide components is the reason for the deterioration in the gel properties of collagen gel induced by high temperature. The findings presented in this study add the understanding of texture deterioration in high-temperature processed collagen-based meat products and related products, and provide a theoretical basis for establishing methods to overcome the production dilemma faced by these products.
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