Project | ComplexiTE :: publications list |
Title | Codfish skins as potential source of collagen for tissue engineering strategies - isolation and characterization |
Publication Type | Comunications - Poster |
Year of Publication | 2016 |
Authors | Carvalho A. M., Marques A. P., Silva T. H., and Reis R. L. |
Abstract | 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], and this 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 asaccessed (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. Moreover, preliminary studies show that codfish collagen promotes cell adhesion. [1] Gelse, Kolja, E. Pöschl, and T. Aigner. "Collagens—structure, function, and biosynthesis." Advanced drug delivery reviews 55.12 (2003): 1531-1546. |
Conference Name | TermStem |
Date Published | 2016-10-27 |
Conference Location | Guimarães, Portugal |
Keywords | ASTM Guidelines, Collagen type I, Industry by-products, physicochemical characterization |
Rights | openAccess |
Peer reviewed | no |
Status | published |