Studies on Collagen in Aquatic Animals-II

On the Solubilization of the Dolphin Insoluble Hide Collagen

Abstract

For the purification of the dolphin collagen the fiber formation processing after the solubilization of pretreated dolphin hide was applied. First, the effect of the pretreatment on the component of the dolphin hide and some methods of the solubilization were examined.
The dolphin hide was pretreated with acetone and ethyl ether, then 0.5M sodium acetate and 0.1%, acetic acid. From the analyses of amino acids (Hypro, Pro, Tyr, Try), sugars (hexose and pentose) and amino sugar (hexosamine), the dolphin hide seemed to be considerably purified by the pretreatment (Table 1).
The amount of acid soluble collagen extracted by citrate buffer (pH 3.6) was as low as 0.1%.
It was confirmed to be better to solubilize the dolphin hide with the treatment of pepsin (crystallized twice-PU 366000) than with that of the Hiirotake enzyme product (PU 16600) after pretreating under the following condition as a method of the solubilization; Preheating treatment was done at 70°C, for 10min. After preheating, the dolphin hide was cooled slowly to room temperature for 2-3hr. Pepsin treatment was done with 1%, pepsin on dried hide weight at pH 1.5 (HCl-CH₃COONa buffer), and 25°C.