Isolation and characterization of collagen from the skin of sepia pharaonis (ehrenberg, 1831)

In the present study an attempt has been made to isolate and characterize the type I collagen from outer skin of Sepia pharaonis. The total protein content and molecular weight of acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were determined. The structure of ASC and PSC from S. pharaonis was persistent by using Fourier transform infrared spectroscopy (FT-IR) and UV vis spectrum. The soluble collagen was extracted by treating the skin with 0.5 M CH3COOH and centrifuged (ASC). Then residue was resuspended in 0.5 M CH3COOH and was digested with 10% (w/v) pepsin (PSC). On the basis of dry weight the ASC and PSC content was observed as 1.70% and 3.61% and the total protein content of both ASC and PSC was found to be 16.4% and 44.6% respectively. The molecular weight of ASC and PSC was calculated as 107 kDa and 73 to 117 kDa respectively. Both ASC and PSC consisted of two different α chains (α 1 and α 2), and were characterized to be type I with no disulfide bond. PSC had a higher content with high molecular weight cross-links, than did ASC. The results of this study suggest that the skin of S. pharaonis could be used as another potent source for the exploration of collagen.