Abstract
Present study is the first report on production and purification of β-keratinase enzyme from a bacterium belongs to the genus Brevibacillus. The response surface optimized alkaline β-keratinase production by this strain was achieved as 923.0 × 10 3 U l −1 post 48 h of incubation. An alkaline β-keratinase (Brevicarnase) having molecular mass of 83.2 kDa purified from this strain showed optimum activity at 45 °C and pH 12.5, respectively. The K m and V max values of β-keratinase towards keratin were determined as 0.3 mg ml −1 and 4.5 μmol min −1 mg −1, respectively. The Brevicarnase demonstrated appreciable thermo-stability and stability in the presence of anionic and non-ionic surfactants, oxidizing and bleaching agents, EDTA, and compatibility with the tested commercial laundry detergents at a concentration of 0.1%. The purified β-keratinase did not show collagen-degrading activity however, demonstrated dehairing property when tested on goat skin. These properties reinforce the feasibility of inclusion of Brevicarnase in laundry detergent formulations and in leather-industry.
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