Study on the thermal stability of channel catfish skin collagen based on ultrafine grinding

Through the method of acid- pepsin, the collagen was extracted from the skin of channel catfish which was grinded, and its thermal stability was studied.The denaturation temperature and shrinkage temperature of skin collagenwere analyzed through differential scanning calorimetric measurements, and the renaturation of collagen was investigated through circular dichroic, FT- IR spectra and SDS- PAGE after it was treated in denaturation temperature and shrinkage temperature for 1h and placed at 4℃ for 24h.The result indicated that the denaturation temperature and shrinkage temperature were respectively 36℃ and 65℃, and the collagen was characterized as type I by SDS-PAGE spectra.The structure of collagen treated in 36℃ and 65℃ was damaged to a certain extent compared with the untreated collagen, and it could't revert to the original structure.What's more, the collagen of 36℃ treatment had a better denaturation than that of 65℃ treatment.The research can provide theoretical basis for the use of channel catfish skin collagen ( CCSC) .