The acid-soluble collagens (ASC) were isolated from scale of carp (Cyprinus carpio) caught in the winter and summer. Thermal denaturing behaviors of collagens were investigated by the increased pepsin digestibility and by changes in circular dichroism (CD) spectrum upon heating. The denaturation temperature of collagen were estimated from the half decrease of b component upon heating and subsequent pepsin digestion. Collagen from scales in the winter (w-scale ASC) exhibited a transition curve with a midpoint of 31.6C, which was 1.8C below that of scale collagen from the summer fish (s-scale ASC). The CD measurement results showed the melting temperature of s-scale ASC was higher than that of w-scale ASC by 3C. It was concluded s-scale ASC was more stable than the equivalent from the winter season. The research offered the fundamental information on the carp scale collagens that may be utilized in the food, cosmetic and pharmaceutical industries.
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