Fish Scale Collagen Preparation, Characterization and Its Application in Wound Healing

A series of fish collagen proteins were prepared for wound healing application. The physicochemical properties such as molecular weight, solubility, thermal stability of the products was studied. Fourier transform infrared spectroscopy (FTIR) was employed to identify the chemical bonds of fish collagen and its resemblance to type 1 collagen. The surface morphology of the prepared collagen was also studied by scanning electron microscopy (SEM). Results obtained showed that Tilapia and Grey mullet collagen consists of identical four subunits including β chains, γ chains and two α chains (α1 and α2). Due to strong fibrillar nature of collagen, it greatly enhances the cell adhesion capacities of the prepared products. Moreover, the antibacterial activity of collagen was investigated. It was found that all the extracted collagen products have inhibitory activity against all of the tested bacteria. Wound healing efficiency of the prepared collagen was also investigated through assessing the rate of wound contraction, histological evaluations demonstrated that collagen treatment resulted in better resolution and closure of the wound. The above analysis suggested that the isolated fish collagen can be a potential candidate for wound healing application.