A Novel Enzymatic Method for Preparation and Characterization of Collagen Film from Swim Bladder of Fish Rohu (<i>Labeo rohita</i>)

Abstract

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/cm 2 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.