Abstract
Collagens (acid-solubilized and pepsin-solubilized collagens) were prepared from ocellate puffer fish skin and partially characterized.With respect to the pepsin-solubilized collagen, it was a heterotrimer with a chain composition of (α1)2α2. The patterns of peptide fragments were different from skin collagens of other species. The denaturation temperature was 28℃, about 9℃ lower than that of porcine skin collagen. On the other hand, the yields of acid-solubilized and pepsin-solubilized collagens were very high, 10.7% and 44.7%, respectively, on a dry weight basis. These results suggest that ocellate puffer fish skin has potential as an alternative source of collagen for use in various fields.2002 Elsevier Science Ltd. All rights reserved.
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