Evaluating the Physicochemical and Structural Properties of Collagen from Lizardfish (Saurida tumbil Bloch, 1795) Skin Prepared with the Optimal Enzymatic Process: in Comparison with Recent Studies

Marine fish byproducts are quiet potential raw material for protein-based commodities like collagen. Due to their abundant resources, safer from many zoonosis, and great biocompatibility, marine collagens are regarded as an ideal candidate biopolymer for such research and medical applications. Although lizardfish (Saurida tumbil Bloch, 1795) skin collagen had been extracted optimally by our previous research, the characterization of its physicochemical and microstructural properties has been reported yet. Thus, the aim of this article was to evaluate the characteristic of the pepsin soluble collagen (PSC) from lizardfish skin prepared using the optimal extraction process. The obtained PSC was categorized as type I collagen, as evidenced by the existence of two alpha chains following electrophoresis in acrylamide gel, and its imino acid was 187.54 residues/1000 residues. Analysis using ultraviolet-visible (UV-vis) techniques verified that the extracted collagen displayed an absorption peak at 232 nm, consistent with various fish collagens. The triple helical structure of PSC was preserved after being confirmed through X-ray diffraction (XRD) and Fourier transforms infrared spectroscopy (FTIR) tests. In terms of thermostability, the type I PSC exhibited high maximum transition temperature (Tmax = 36.74°C). At low NaCl and acidic conditions, the relative solubility of optimized collagen was high (more than 80%). The PSC showed many multilayered forms with dense sheet-like film. Overall, the type I collagen processed optimally from the skin of lizardfish could be used as a promising source of biomaterials for industrial viewpoint.