Thermal stable characteristics of acid- and pepsin-soluble collagens from the carapace tissue of Chinese soft-shelled turtle (Pelodiscus sinensis)

[Display omitted] •Characterization of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from carapace.•Glycine as the major amino acid for both ASC and PSC of Chinese soft-shelled turtle.•The high denaturation temperature (Td); minimum solubility at pH 8; maximum solubility at a salt concentration of 3%.•Both ASC and PSC appeared to be spongy like microstructure with fibrillar pores.•Potential uses as new substitute for mammalian collagen in medicinal, food or biomaterial fields. The carapace from the Chinese soft-shelled turtle (Pelodiscus sinensis) is used as a traditional Chinese medicine. Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from turtle carapace were isolated and characterized to screen novel collagen material in this study. Yields of 1.0% and 2.8% were obtained for ASC and PSC which contained glycine as the major amino acid and had high imino acid content. Both collagens had maximum ultraviolet absorption peaks of 220 nm. SDS-PAGE revealed that the structure of both collagens was similar, belonging to type I collagen. Relative viscosities of collagens were decreased as the temperature increased. Collagens showed minimum solubility at pH 8 and maximum solubility at a salt concentration of 3%. The denaturation temperature (Td) of PSC was higher whereas the melting temperature was lower than that of ASC. Both ASC and PSC appeared to be spongy like microstructure with fibrillar pores shown by scanning electron microscopy. The results suggest that collagens isolated from turtle carapace has high thermal stability with potential uses as new substitute for mammalian collagen in medicinal, food or biomaterial fields. However, their biological or pharmacological activities are needed to be further studied.