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ABSTRACT
The acid soluble collagens (ASC) and pepsin soluble col-lagens (PSC) of albacore tuna and silver-line grunt skin, by-products from frozen fish fillet industry, had been extracted, purified and characterized. Analysis of the collagens by SDS-PAGE indicated the absence of a disulfide bond, which is a characteristic of type I collagen. They also contained different subunits, a, β and ?. At least two different a chains, a1 and a2, were presented. The proportion of ? trimer in ASC was higher than in PSC. This caused reduced solubility of ASC, whereas, PSC were lower molecular weight and had fewer crosslinks, which resulted in increased solubility. Collagen water solubility was lower than in 0.5 M acetic acid, but the solubility increased as the temperature increased. Denaturation temperature (Td) of silver-line grunt collagen was slightly higher than albacore tuna collagen, but about 7–9°C lower than calfskin collagen.