Isolation and characterisation of collagen from the ribbon jellyfish (Chrysaorasp.)

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Pepsin-solubilised collagen from the ribbon jellyfish (Chrysaora sp., morphotype 1) umbrella (JPSC) was isolated and characterised. The yield of collagen varied (9–19%, based on ash-free dry weight) depending on the amount of pepsin used. Type II collagen was the major component of extracted collagen. The peptide map of JPSC differed from that of standard collagen type II, which indicates their different primary structures. FTIR spectra of JPSC, however, did not differ significantly from those of type II collagen. The Tmax of JPSC was 37.38 °C, which is higher than that of other marine collagens. Glycine was the main amino acid in JPSC (320 residues per 1000 residues), followed by glutamic acid, alanine, proline, aspartic acid and hydroxyproline. The isoelectric point of JPSC was 6.64. These results indicate that this jellyfish species has the potential to be a marine source of type II collagen that can be used in place of land-based sources.

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