Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-50356
Food Chem September 30, 2022; 389 133033.
Show Gene links Show Anatomy links

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

Song X , Si L , Sun X , Zhu X , Li Z , Li Y , Wang Y , Hou H .


Abstract
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.

PubMed ID: 35490516
Article link: Food Chem