Study On The Antifreeze Activity Of Collagen From Different Sources
Keywords
Antifreeze Activity, Collagen, Thermal Hysteresis Activity, Recrystallization Inhibitory Effect
Abstract
Collagen from different sources was prepared using enzymatic methods, and its purity and amino acid composition were identified. On this basis, differential scanning calorimeter and cryogenic microscope were used to study its thermal hysteresis activity (THA) and recrystallization inhibition effect (ice recrystallizationinhibition, IRI). The results show that the prepared collagen is typical type I collagen with high purity and a molecular mass of approximately 330 kD. Compared with bovine serum albumin, among collagens from different sources, pig skin collagen has a higher Thermal hysteresis activity, that is, when the retention temperature is -0.2¡ãC and the ice crystal content of the system is ¦Õ¡Ü5%, THA is 0.52¡ãC; the ice crystals formed in the pig skin collagen system are irregular spherical and are not likely to cause damage to cells and tissues. damage, and after one cycle, the ice crystals do not increase significantly
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Original research was done by Yu Jinsong, Xu Fei, Cao Hui, Ruan Gongcheng
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