ABSTRACT
Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) from golden pompano skins were extracted and characterized. The molecular weight of ASC was about 130 kDa for α1 and 115 kDa for α2, which were slightly higher than those of PSC. Similar amino acid composition and Fourier transform infrared (FTIR) spectra were observed in both collagens, but slight differences were found in the peptide maps of collagen digested by V8 protease and trypsin. The denaturation temperatures (Tds) of ASC and PSC calculated from the reduced viscosity were 31.8 and 30.0°C, while the transition temperature (Tm) of ASC and PSC analyzed by DSC were 33.0 and 32.0°C, respectively. ASC has a lag phase, a growth phase, and a plateau phase in the turbidity–time curve, while PSC does not have similar phenomenon. It was found that the fibril gel of ASC could be formed at 25°C, leading to improved thermal stability.
Funding
This work is sponsored by National Natural Science Fund (31271984), Fujian Natural Science Fund for Distinguished Young Scholar (2014J06013), Special Foundation for Development of Marine Economy of Xiamen (14CZP031HJ05), Quanzhou Science and Technology Project (2016Z003), and Regional Development Project of Fujian Province (2017N3004).