Abstract
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.
Highlights
Collagen is the main protein in animal connective tissue, and it has been widely used as a food [1]and as an industrial functional material [2]
The results suggested that GCC, grass carp scales (GSC), and crucian carp skin (CCC) were able to assemble spontaneously, which further confirmed that all three maintained their molecular integrity and did not become denatured [42]
Our results suggested that the in vitro self-assembly of fibrils by GCC, GSC, and CCC is possible if the collagen solution is adjusted appropriately
Summary
Collagen is the main protein in animal connective tissue, and it has been widely used as a food [1]. At least 28 types of collagen have been identified [3], each with a different molecular structure, amino acid sequence, and functionality. Type I collagen is the major structural component in human and animal skin, and it is the most extensively-studied collagen type [4]. Type I collagen has been isolated from the skin and bones of terrestrial animals, such as swine, cattle, and poultry. Studies have suggested that type I collagen molecules can self-assemble into novel structures when treated at the correct temperature, pH level, and ionic strength [8]. Fessler et al confirmed that the amino acid composition of collagen alpha chains varied according to the fish species and the tissues selected, forming different microstructures in the self-assembly process [10]. The assembly properties and morphology of collagens from different sources were investigated during self-assembly curves and scanning electron microscopy (SEM)
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