Chrysosporium sp. strain isolated from soil using hair baiting technique was tested for its abilities to hydrolyze the hair keratin. It was able to produce highest keratinase i.e. 336 U/ml after 9 days of incubation with a total protein content of 1.19 mg/ml and 16.7 mg/ml of cystein. The enzyme was partially purified by ammonium sulphate fractionation and DEAE-cellulose column chromatography. A purification fold about 7.13 with a recovery of 14.92% was obtained. Specific activity of this partially purified enzyme was 1415.73 U/ml. The optimal pH and temperature for keratinolytic activity was approximately 9 and 50°C respectively. This keratinase was inhibited by addition of PMSF whereas the enzyme activity was enhanced in presence of EDTA and 1,10 phenanthroline at a concentration of 5 mM and 1 mM concentration. Strain Chrysosporium sp., therefore, shows great promise of finding potential applications in keratin hydrolysis and keratinase production.
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