Abstract
PURIFICATION AND CHARACTERISATION OF KERATINASE FROM BACILLUS SP. KP1
Joshi Swapnil Satish*
ABSTRACT
In this study we purified and characterized a keratinase produced by a newly isolated bacterium Bacillus sp. KP1. The crude enzyme produced was purified by ammonium sulphate precipitation followed by DEAE Cellulose and Sepharose G-75 chromatography. Molecular mass of 30 kDa was determined by SDS-PAGE. Optimum pH and temperature for enzyme activity were found to be 8.0 and 50 °C respectively. Enzyme got inhibited by EDTA while retained its activity in the presence of PMSF and DTT indicating it’s a metallo-enzyme. When effect of surfactants was studied on highest enzyme activity of 131± 3.9% was observed in the presence of triton X-100. Other surfactants also stimulated enzyme activity(triton X-100, tween-20, tween-80). When effect of metal ions (Ca2+, Mg2+, Mn2+, Zn2+, Hg+, K+, Na+, Cu2+, Fe3+, Al3+) was studied highest enzyme activity of 115 115 115 115 ± 2.8% was achieved for Ca2+ ions.
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