At present alkaline proteases are widely used in leather processing, detergent formulations,rnsilver recovery process, and in the production of protein hydrolysates. All alkaline proteasesrnare dervied from microbial sources that grow on expensive growth substrate. Many studiesrnshowed that nearly 40% of the production cost of alkaline proteases is accounted for by therngrowth substrate. To reduce the production cost it is important to search for microorganismsrncapable of growing and producing suffiecient amount of the enzyme using cheap substartes.rnIn this regard keratinacious wastes released by poultry and leather tanning industries has anrnenourmous potential to serve as growth substartes for protease production. In this study, arnprotease producing Vibrio sp. capable of growing on bovine and sheep hair was isolated fromrnLake Arenguade. The organism produced appreciable level of keratinolytic protease usingrnhair as the sole source of carbon and nitrogen. The enzyme was active in the pH range of 7.0-rn11.5 and 40-70Â°C with an optimum pH of 11.0 and 50oC. The enzyme showed good stabilityrnin the presence of oxidizing agents and detergents. Application of the enzyme at the innerrnside sheep skin at a dosage of 58U/ml, pH 10.0 brought about complete removal of hairrnwithin 24 h at room temperature and 12 h at 37oC. Protease R-11 was also tested for thernrecovery of silver from used x-ray films. At enzyme dose of 11.6 U/ml and at 55oC completernremoval of the gelatin layer of used x-ray films was achieved within 3 min at pH 10.00.rnThese results indicate the potential of protease R-11 for multipurpose industrial application.rnBecause the organism produces the enzyme using cheap substrates, hair, its production cost isrnexpected to be very low.rnKey words: Dehairing; Gelatin hydrolysis. Hair degrading; Keratinolytic protease; Keratinousrnwastes; Used x-ray film; Vibrio sp. strain R11