Extraction and Purification of Collagen from the Jellyfish Catostylus mosaicus of the Persian Gulf

Background: Collagen is a protein that constitutes a major component of connective tissue and has many applications in the medical and non-medical fields. The increase in the world population and the need for proteins have led to a special focus on seafood. Furthermore, jellyfish is a rich and renewable source of collagen. Therefore, many researchers have shown interest in collagen extraction from jellyfish. This study aims to extract and purify collagen from jellyfish Catostylus mosaicus. Materials and Methods: Acid-soluble and pepsin-soluble collagens were extracted and purified using a membrane with a MWCO of 100,000 from jellyfish Catostylus mosaicus. Protein content, type, denaturation temperature, and functional groups of the extracted collagens were evaluated using spectrophotometer, electrophoresis, viscometry, and Fourier transform infrared (FTIR) spectroscopy, respectively. Results: The results showed that pepsin-soluble collagen extracted from the umbrella and arm of the Catostylus mosaicus jellyfish consisted of chains α and dimer β, and the yields of the pepsin-soluble collagens extracted from the jellyfish umbrella and arm were 14.58% and 12.8% of the dry weight. The results also showed that the denaturation temperature of collagen extracted from the jellyfish arm and umbrella were about 27.32  and 28.72 , respectively. The FTIR spectra of pepsin-soluble collagen from the jellyfish umbrella and arm were almost identical to other types of collagens. Conclusion: The results show that this species of jellyfish can be used as a renewable marine source of collagen instead of other sources of collagens.