Research Article
Isolation and Characterization of Acid Soluble Collagen from the Skin of African Catfish (Clarias gariepinus), Salmon (Salmo salar) and Baltic Cod (Gadus morhua)
Robert Tylingo1*, Szymon Mania1, Anna Panek2, Rafał Piątek3and Roman Pawłowicz4
1Department of Chemistry, Technology and Biotechnology of Food, Gdansk University of Technology, Gabriela Narutowicza Street 11/12, Gdansk 80-233, Poland
2Department of Biology and Biochemistry, University of Bath, Bath BA2 7AX, United Kingdom
3Department of Molecular Biotechnology and Microbiology, Gdansk University of Technology, Gabriela Narutowicza Street 11/12, Gdansk 80-233, Poland
4Department of Chemical and Process Engineering, Gdansk University of Technology, Gabriela Narutowicza Street 11/12, Gdansk 80-233, Poland
- *Corresponding Author:
- Robert Tylingo
Department of Chemistry, Technology and Biotechnology of Food
Faculty of Chemistry, Gdansk University of Technology
ul. Gabriela Narutowicza 11/12
80-233 Gdańsk, Poland
Tel: (48-58) 347-1595
Fax: (48- 58) 347-1246
E-mail: robertt@pg.gda.pl
Received date June 07, 2016; Accepted date June 21, 2016; Published date June 28, 2016
Citation: Tylingo R, Mania S, Panek A, Piątek R, Pawłowicz R (2016) Isolation and Characterization of Acid Soluble Collagen from the Skin of African Catfish (Clarias gariepinus), Salmon (Salmo salar) and Baltic Cod (Gadus morhua). J Biotechnol Biomater 6:234. doi:10.4172/2155-952X.1000234
Copyright: © 2016 Tylingo R, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Acid-soluble collagen (ASC) from the fish skin of African catfish (Clarias gariepinus), Salmon (Salmo salar) and Baltic cod (Gadus morhua) was extracted and characterized. The ASC extraction yield was 75%, 73% and 68%, respectively. The denaturation and melting temperatures of African catfish ASC (29.3°C and 100.0°C) were significantly higher than ASC of Salmon and Baltic cod (20.6°C and 90.5°C; 15.2°C and 86.7°C, respectively), assessed by differential scanning calorimetry. The SDS-PAGE profile showed that each of tested ASC was the type I collagen and consisted of two different α chains, α1 and α2, as well as a β component. The FTIR spectra of all collagens indicate that the overall their chemical compositions are quite similar. The fish skin collagen is easy to prepare and represents a possible resource for use on industrial scale.