Thermal stability of sea cucumber collagen and effects of gallic acid crosslinking

The thermal processing characteristics of sea cucumber collagen (SCC) are closely related to its triple helix structure, self-assembly and aggregation ability. The effect of heat treatment on SCC was studied by apparent viscosity, circular dichroism spectra and so on. As heating time increased from 10 to 160 min, apparent viscosity decreased from 400 to 300 mPa center dot s at 80 degrees C, indicating the structure of SCC changed. The decrease in SCC self-assembly and aggregation ability showed the structural change. Positive peak at 220 nm was decreased from 24 to 0 mdeg at 60 degrees C for 10-160 min, which revealed that SCC triple helix structure was uncoiled and disappeared. Fluorescence intensity was increased and the absorption peak showed a red shift during thermal treatment. Gallic acid crosslinking could improve thermal stability and inhibit the degradation of collagen. It could provide theoretical guidance for sea cucumber processing.

Automated summary

The thermal processing of sea cucumber collagen (SCC) affects its triple helix structure, self-assembly, and aggregation ability. Heat treatment resulted in changes in viscosity and circular dichroism spectra, indicating structural changes in SCC. The uncoiling and disappearance of the triple helix structure of SCC were observed, along with increased fluorescence intensity and a red shift in absorption peak during thermal treatment. Crosslinking with gallic acid improved the thermal stability and inhibited collagen degradation. This study provides theoretical guidance for sea cucumber processing.