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

Summary 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·s at 80 °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 °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.