Isolation and Characterization of Biocompatible Collagen from the Skin of Puffer Fish (Lagocephalus inermis)

In this present study, acid soluble collagen and pepsin soluble collagen from the skin of marine puffer fish Lagocephalus inermis was successfully isolated and characterized. The collagens extracted from the fish skin showed the high yields of both acid solubilized collagen (ASC) (43.1%) and Pepsin soluble collagen (PSC) (56.6%) on the dry weight basis, respectively. Based on electrophoretic patterns, both ASC and PSC consisted of two α- chains (α1 and α2) and were characterized as type I collagen. Amino acid analysis of both the collagen contained the imino acid of 190 and 198 residues/1000 residues, respectively. The ultraviolet absorption spectrum of collagen showed maximum absorption at 230 nm. Fourier transforms infrared spectra of both ASC, PSC was almost similar, and the acidic or enzymatic extraction had no effect on the triple helical structure of collagen. The denaturation temperature (Td) of the collagen was found to be 31.9 °C for ASC and 32.6 °C for PSC, respectively. Both ASC and PSC had highest solubility at acidic pH. Scanning electron microscopy images revealed the porous structure of collagens and both the collagens showed 100% biocompatible on NIH3T3 cell lines. These characteristic features are essential for wound dressing applications. From this study, a useful product recovery was achieved from the underutilized puffer fish, which may serve as an alternative source for mammalian collagen, as well as the management of natural wastes or ecological problems.