Journal
FOODS
Volume 8, Issue 9, Pages -Publisher
MDPI
DOI: 10.3390/foods8090396
Keywords
collagen; self-assembly; grass carp; crucian carp
Categories
Funding
- Sichuan Science and Technology Program [2018RZ0034]
- China Scholarship Council [201806915013]
- Natural Science Fund of Education Department of Sichuan Province [16ZB0044, 035Z1373]
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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 degrees C, respectively. All three were shown to self-assemble into fibrils at 30 degrees 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.
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