Proteolytic Bacillus strains isolated from tannery effluent were screened on saline skim milk agar plates (pH-9) for their potency to secrete alkaline protease. Bacillus licheniformis exhibited highest extracellular alkaline protease activity of 360 Units/ml at 72hrs of incubation. Among the proteolytic isolates, Bacillus licheniformis degraded chicken feathers to the maximum extent (58%), followed by Bacillus cereus M-1 (40%) and Bacillus subtilis (37%). Dehairing activity of alkaline protease revealed that they were efficient when employed in dip method, than spray and paint method. Complete destaining was observed within 20mins by the crude enzyme produced from Bacillus licheniformis. Crude enzymes were partially purified by acetone precipitation and SDS-PAGE results revealed that the molecular weight of the alkaline protease enzyme was 28kDa.