Rheological properties, thermal stability and conformational changes of collagen from sea cucumber (Apostichopus japonicas).

Sea cucumber collagen (SCC) properties affected the thermal processing of sea cucumber. SCC showed the shear-thinning and pseudo-plastic properties, and the viscosity and frequency of viscoelastic crossover were decreased gradually with the temperature from 15 to 30 °C. Differential scanning calorimetry of SCC confirmed that it was thermolabile with the increase of temperatures, acid or NaCl concentrations. As the temperature increasing, the triple helix of SCC disappeared with the decrease of the relative proportion of P2 structures by circular dichroism spectrometry and Fourier transform infrared spectroscopy, and shearing could accelerate the change. Intramolecular changes investigated by molecular dynamics simulation showed the average number of hydrogen bonds decreased from 47 (20 °C) to 42 (80 °C), indicating triple helix of SCC was triggered to uncoil within 250 ns. These results could provide a scientific basis for processing of sea cucumbers.