Purification and characterization of a novel pullulanase enzyme from Bacillus thuringiensis for detergent industry

In the present study purification and characterization of a novel extracellular pullulanase enzyme from Bacillus thuringiensis was carried out for use in detergents. Maximum production (5.71 U/ml) obtained medium containing tryptone as carbon energy source having pH 6.0 when it inoculated with 3% overnight grown inoculum incubated at 37°C 24 hrs.  Optimal conditions pullalanse activity were also determined maximum (8.584 found 4% pullulan substrate phosphate buffer 7.0 50°C after 20 minutes incubation. Purification achieved to homogeneity by ammonium sulphate precipitation well ion exchange chromatography distinct band 97 kDa analyzed SDS-PAGE. fold purified calculated 16.83 37% yield 45.45 U/mg specific activity. The stable up 90°C 4.0-8.0. presence Ca+2 ions, increased, whereas EDTA reduce activity.  Addition 1% Tween 80 do not showed considerable effects but SDS DMSO inhibit No significant effect organic solvents (ethanol, methanol, acetone, isopropanol, n-butanol) detected on residual Purified great stability laundry detergents wash performance increased along amylase against starchy stain.