Isolation and characterization of collagen type I from codfish: a potential source of collagen for tissue engineering strategies

Collagen is the most abundant structural protein in the extracellular matrix. Besides providing biomechanical
features, collagen also defines cell adhesion, differentiation, growth, cellular activities and survival [1]. This
features makes collagen a primary material in tissue engineering strategies. Among collagen alternatives, fish
provides the best source of raw material due to its high availability, no risk of disease transmission and the
absence of religious barriers [2]. Moreover, it contributes to a more sustainable exploitation of marine natural
resources, and the development off added-value biomedical products. In this work, acid soluble collagen was
isolated from codfish skins, an industry by-product, and characterized according to ASTM F 2212-08e1 guideline
[3]. Extract purity was determined as (74.63 ± 19.72) % and (87.70 ± 3.58) % for using SIRCOL and micro BCA
assays respectively. The SDS-PAGE extract profile is coherent with collagen type I, as well as amino acid
content. FTIR analysis and CD shows that the extracted collagen presents triple-helix conformation in some
extent. The denaturing temperature was determined as (16.26 ± 0.05) oC.

[1] Gelse, Kolja, E. Pöschl, and T. Aigner. "Collagens—structure, function, and biosynthesis." Advanced drug
delivery reviews 55.12 (2003): 1531-1546.
[2] Berillis, Panagiotis, “Marine Collagen: Extraction and Applications.” Research Trends in Biochemistry,
Molecular Biology and Microbiology (2015): 1-13
[3] F 2212 - 08e1 “Standard guide for characterization of type I collagen as starting material for surgical
implants and substrates for tissue engineered medical products (TEMPs)” ASTM International