Purification Properties of Bacillus thuringiensis TS2 Keratinase Enzyme

This study was focused on purification and characterization of keratinase from Bacillus thuringiensis TS2, isolated from feather dumping soil site. Zymogram of crude enzyme on native-PAGE presented bands with keratinase activity of molecular weights is 41 kDa. In purification steps 2.69 fold purification was achieved after 80% ammonium precipitation of the with 34.42% recovery. In further purification steps a 5.69 fold purified keratinase was recovered by Sephadex G-75 chromatography with 21.23% of recovery. The specific activity of purified enzyme was 970.15.54 U/mg. Kinetic studies indicated that substrate specificity of TS2 keratinase was towards various natural and synthetic proteolytic substrates but inactive against collagen and keratin. These findings suggested that the keratinase may have much industrial application.