Alkaline crude enzymes from the viscera of the Tunisian barbel (Barbus callensis) were extracted and characterized. Proteolytic crude extract from barbel viscera was active and stable in alkaline solution. The optimum pH and temperature were 11.0 and 55 °C, respectively, using casein as a substrate. The crude alkaline protease was extremely stable in the pH range of 5.0-12.0. Zymography activity staining using casein as a substrate showed the presence of at least five distinct proteases. The crude alkaline proteases showed stability towards various surfactants, bleach agents and compatibility with some commercial detergents. Alkaline proteases from the viscera of the barbel were tested in chicken feather-degradation and showed important feather degrading activity. Complete solubilisation of whole feathers was observed after 24h of incubation at 50°C. Additionally, crude alkaline protease demonstrated powerful capabilities of hair removal from skin and the collagen, the major leather-forming protein, was not significantly degraded. Considering its promising properties, alkaline crude enzyme from the viscera of the Tunisian barbel may be considered as a potential candidate for future use in several biotechnological processes.