Abstract
Acid-soluble and pepsin-soluble collagens (ASC and PSC) were extracted from the skin of channel catfish ( Ictalurus punctaus) and partially characterized . The collagen obtained in the experiment contained more than 23% glycine as the most abundant amino acid. The denaturation temperature of acid-soluble collagen was 32.5 °C, about 5 °C lower than that of the porcine skin collagen. SDS–PAGE showed that the collagens were composed of two distinct alpha chains, which is similar to the porcine type I collagen. The contents of the skin ASC and PSC, on a dry weight basis, were 25.8% and 38.4%, respectively. These results suggest that channel catfish skin has potential as a supplement to the sources of vertebrate collagens.
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