T. Abdullah, R., J. Hashim, A., M. Karhout, J. (2009). Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized. , 3(2), 41-52.
Rasha T. Abdullah; Abdulkareem J. Hashim; JASIM M. Karhout. "Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized". , 3, 2, 2009, 41-52.
T. Abdullah, R., J. Hashim, A., M. Karhout, J. (2009). 'Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized', , 3(2), pp. 41-52.
T. Abdullah, R., J. Hashim, A., M. Karhout, J. Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized. , 2009; 3(2): 41-52.

Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized

Jornal of Biotechnology Research Center
Article 1, Volume 3, Issue 2, 2009, Pages 41-52
Authors
Rasha T. Abdullah; Abdulkareem J. Hashim; JASIM M. Karhout
Abstract
The keratinase produced from local isolate Bacillus licheniformis was purified by two steps included precipitation by ammonium sulphate with 40% saturation; followed by ion exchange using CM-Cellulose column. The enzyme was purified to 12.6 times in the last step with an enzyme yield of 17%. Enzyme characterization results indicated that: The optimal pH for enzyme activity was 7.5 and it was stable at 7-9.5. The optimal temperature for enzyme activity was 50°C and it was stable for 30 min at 25-45 °C. Substrate specifity was tested using casein, Bovine serum albumin, gelatin, hooves, human hair, chicken feathers and wool; higher specifity was recorded using casein gave 0.6 unit /ml. The enzyme was inhibited by PMSF and metal ions like Hg+2, Fe+2, Cu+2 and Mn+2, and activated by Ca+2, Mg+2, Zn+2and Al+3.
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