Isolation and purification of alkaline keratinase from Bacillus sp. 50-3
AbstractA new alkaline keratinase extracted from Bacillus sp. 50-3 was isolated and purified in this study. Solid ammonium sulfate was selected to precipitate the enzyme. Its proper adding mass was also determined.
Through solid ammonium sulfate precipitation and liquid chromatography via the DEAE-Sephadex-A50 column using with azokeratin as a substrate, 17.7-fold purification with a yield of 46.5% was obtained. The purification effect was determined through SDS-PAGE, and the molecular weight of the enzyme was found at 27 423 Da by the MALDI-TOF-MS. Its simple purification step and high yield using a cheap medium attest to the great biotechnological potential of keratinase, especially in environment
protection and in recycling valuable materials from wastes.