Abstract
Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were extracted from the swim bladders of yellowfin tuna (Thunnus albacares) with yields of 1.07% and 12.10%, respectively. Based on electrophoretic patterns, both ASC and PSC consisted of two α-chains (α1 and α2) and were characterised to be type I collagen. ASC had higher β-chains than PSC. Imino acid contents of ASC and PSC were 128 and 169residues/1000residues, respectively. Fourier transform infrared (FTIR) spectra of both ASC and PSC were similar and revealed the presence of a triple helix. Both ASC and PSC had the highest solubility at acidic pHs. From zeta potential analysis, a net charge of zero was found at pH 6.05 and 5.93 for ASC and PSC, respectively. Tmax of ASC and PSC were 32.97 and 33.92°C, respectively. The swim bladders of yellowfin tuna could therefore serve as an alternative source of collagen for future applications.
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