Characteristics of acid- and pepsin-soluble collagens from scale of seabass (Lates calcarifer)

- Scales of seabass could serve as the source of collagen.
- Pepsin was able to increase the extraction yield of scale collagens.
- Acid and pepsin soluble collagens showed similar molecular properties.

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from seabass (Lates calcarifer) scale were characterised. Yields of ASC and PSC were 0.38 and 1.06% (based on dry weight), respectively. Both ASC and PSC were identified to be type I collagen, which consisted of α1 and α2 chains. β component was also found in both collagens. ASC and PSC contained glycine as the major amino acid and had high imino acid content (193-198 residues/1000 residues). Tmax of ASC and PSC from seabass scale were 38.17 °C and 39.32 °C, respectively. FTIR spectra indicated that triple helical structure of resulting PSC was not disrupted by pepsin digestion. ASC and PSC from seabass scale exhibited high solubility in very acidic pH range (pH 2-4). Therefore, seabass scale could be an alternative source of collagen and the characteristics of collagens were slightly affected by extraction process used.