Effect of ultra-high pressure on molecular structure and properties of bullfrog skin collagen

Ultra-high pressure technology has attracted a great deal of attention in recent years, and has been widely used in food science, medicine, and other fields. This study aimed to determine the effect of ultra-high pressure on the structure and properties of collagen. Native collagen extracted from bullfrog skin was processed under different ultra-high pressure treatment conditions (300, 400, and 500 MPa). Then systematic analysis of the molecular structures and properties of the samples after ultra-high pressure treatment were performed. It was found that the conformation of collagen molecules could be adjusted by ultra-high pressure treatment, and this regulation was closely related to the level of treatment pressure. A possible mechanism of the impact of ultra-high pressure on the collagen molecular structures was speculated according to the experimental results. At low pressure levels (300–400 MPa), the pressure perpendicular to collagen axis dominates and leads to a tightening of the triple helix structure of collagen, while the pressure parallel to collagen axis is dominant and the triple helix tends to dissociate like a zipper at high pressure levels (> 400 MPa). These structural changes would simultaneously result in various changes to thermal stability, self-assembly properties, and antigenicity of collagen.