Abstract
A novel dimeric 58kDa keratinase is reported from Bacillus licheniformis ER-15. The bacterium produced 244U/ml keratinase in 48h which was increased by eight fold (1962U/ml) after medium optimization by one-variable-at-a-time and response surface methodology. Enzyme was concentrated by ultrafiltration followed by acetone precipitation and purified by gel filtration chromatography. It had subunit of 30 and 28kDa and pI of 8.4. Enzyme was maximally active at pH 11 and 70°C. It hydrolyzed various complex proteins viz. haemoglobin, feather, hooves, fibrin and meat protein. It was a thiol activated serine protease and 6.25-fold enhancement in activity was observed in presence of 5mM mercaptoethanol. Nearly 1200U keratinase degraded 1.5g feather in 12h at pH 8, 50°C in redox free environment. This enzyme also dehaired buffalo hide within 16h in presence of 3% Ca (OH)2.
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