Soluble egg shell membrane protein as a regulating material for collagen matrix reconstruction.

Soluble egg shell membrane protein (SEP) was prepared from egg shell membrane by the combined treatment of performic acid oxidation (4 or 25 degrees C for 24 h) and pepsin digestion (25 degrees C for 24-72 h) before dialyzing against water and lyophilizing. The yield of SEP was about 16-39%. SEP had high contents of acidic amino acids (320-340 residues/1000 residues) containing cysteic acid (101-108 residues) converted from cystine, a small amount of saccharides, a main molecular weight of 12,000-22,000 and pI 4.2-4.8. SEP accelerated the reconstruction of collagen matrix with ordered molecular rearrangement and reduced redissolution of the collagen matrix under several solvent conditions. SEP elevated the denaturation temperature of the matrix.