Identification and Physicochemical Properties of Collagen from Sika Antler Base

The structure and physicochemical properties of ASC and PSC extracted from the antler plate of plum blossom deer were studied, which provided a theoretical basis for developing new collagen resources and improving the added value of deer products. The results showed that ASC and PSC were consistent with the characteristic distribution of amino acids of type Ⅰ collagen. The methionine content was the lowest and the hydroxylation degree was higher (45.69% and 46.30%, respectively). ASC and PSC consisted of at least two α chains (α1 and α2), a high amount of β chain, and a small amount of γ chain. The secondary structures of ASC and PSC were similar, with the characteristic absorption peaks of amide A, B, Ⅰ, Ⅱ and Ⅲ, preserving the triple helix structure. ASC and PSC had almost no absorption at 280 nm. The maximum absorption peaks of ASC and PSC were at 219.0 nm and 224.0 nm. The closer the pH values of ASC and PSC solutions was to pI values, the worse the solubility, emulsifying capacity, and emulsifying stability. The solubility, foaming of ASC and PSC could be enhanced by increasing NaCl concentration in the range of 0~2 mol/L. In the range of 0~0.4 mol/L, the emulsifying capacity and emulsifying stability of ASC and PSC could be improved. The emulsifying stability of the them was at the maximum level when the protein concentration was 0.5%, and the emulsifying stability of them was at the minimum level when the protein concentration was 4%.