In the present study, porcine and bovine collagen were mixed respectively with the matrix composed of fish scale type I collagen, and then the properties of the reconstructed collagen sponge were tested. The fourier transform infrared spectroscopy (FTIR) analysis showed intact retention of the classical triple-helix structure after reconstruction with perfect water absorption capacity. The micro-fibril structure of the fish scale type I collagen in the mixture was observed more compact by scanning electron microscope(SEM), and significant improves in thermostability and enzymatic hydrolysis stability were also detected by tests of enzymatic hydrolysis, differential scanning calorimetry (DSC), and thermogravimetry (TG).
