The acid and pepsin-solubilized collagens from the skin of
balloon fish, D. holocanthus, were extracted and characterized. The
results showed that pepsin can act as a tool for obtaining a greater
yield without having a noticeable effect on the triple-helical
structure. The skin collagens of the balloon fish consisted of two
a chains (a1 and a2) and were classified as type _ without a disulfide
bond. The denaturation temperatures of the ASC and PSC were
about 29 C and 30 C, respectively. The ASC and PSC showed high
solubility at acidic pH and lost solubility when the NaCl concentrations
were increased. These results suggest that the skin of
balloon fish has potential as an alternative source of collagen for
use in various fields.