A novel enzymatic method for extraction and preparation of fish collagen from swim bladder revealed the occurrence of α, β and γ bands with approximately 12.1 g/100g collagen corresponding to 89% of collagen and thus confirmed the nativity and purity of the fish collagen. FT-IR studies confirmed the retention of all three amide bands of I, II and III, and triple helixcity. UN-crosslinked and UV-crosslinked fish collagen membrane records a very high temperature of helix denaturation at 197℃ and 215℃, shrinkage temperature at 50℃ ± 3.2℃ and 62℃ ± 2.7℃ and tensile strength at 16.89 ± 2.5 and 120.02 ± 1.0 Kg/cm2 respectively. Fish collagen matrix promoted NIH 3T3 and L6 cellular growth and proliferation. The study indicates that availability of pure fish collagen could replace bovine collagen in tissue engineering applications.
展开▼
