Collagens were extracted from grass carp skin (GCC), grass carp scales (GSC), and crucian carp skin (CCC) using an acid-enzyme combination method, and their characteristics and self-assembly properties were analyzed. Electrophoretic patterns characterized all three as type I collagens. An ultraviolet analysis identified the optimal wavelengths for collagen detection, while a Fourier transform infrared spectroscopy analysis confirmed the triple-helical structure of the collagens. The GCC, GSC, and CCC had denaturation temperatures of 39.75, 34.49, and 39.05 °C, respectively. All three were shown to self-assemble into fibrils at 30 °C in the presence of NaCl, but the fibril formation rate of CCC (40%) was slightly higher than those of GCC (28%) and GSC (27%). The GSC were shown to form a more strongly intertwined fibril network with a characteristic D-periodicity. The fish collagens extracted in this study have potential applications in the development of functionalized materials.
Keywords: collagen; crucian carp; grass carp; self-assembly.