Structure Restoration of Thermally Denatured Collagen by Ultrahigh Pressure Treatment
Man Sun, Xu Wei, Haibo Wang, Chengzhi Xu, Benmei Wei, Juntao Zhang, Lang He, Yuling Xu, Sheng Li
Food and Bioprocess Technology
Thermal denaturation is the primary reason for the loss of excellent performance for collagen-based materials. It is particularly urgent to explore an effective structure restoration strategy for thermally denatured collagen. In this study, three different degrees of collagen thermal denaturation models were constructed; the effects of ultrahigh pressure treatments of varying intensities on the structure and properties of partially thermal denatured collagen were investigated. Those results showed that ultrahigh pressure partially restores the triple helix conformation and the α helix of low thermally denatured collagen molecules and moderately restores collagen thermal stability. However, this recovery is not a “perfect” structural restoration; it cannot effectively restore the fibrotic ability of collagen which leads to a decrease in the fiber diameter of the product and an increase in the storage modulus of the product gel. As the degree of thermal denaturation of collagen increases, the ultrahigh pressure recovery effect is gradually lost. For moderate thermally denatured collagen, ultrahigh pressure treatments only recover a small amount of its triple helical conformation. For high thermally denatured collagen, ultrahigh pressure treatments exacerbate the destruction of the three-dimensional structure of collagen molecules, thereby losing the order of molecular structure and the capability of fibrosis self-assembly.
Circular dichroism, Collagen, Thermal stability, Secondary structure, Biochemistry, Food science