Characterization of α- Amylase Produced from a Local Isolate of Bacillus licheniformis R5

2016 ◽  
Vol 6 (2) ◽  
pp. 34-48
Author(s):  
Rana Abdullah Hussein ◽  
Mohammed O.Muhyaddin
Keyword(s):  
Bacillus Licheniformis ◽  
Local Isolate

Characterization of Xyn30A and Axh43A of Bacillus licheniformis SVD1 identified by its genomic analysis

2012 ◽  
Vol 51 (4) ◽  
pp. 193-199 ◽  
Author(s):  
Makiko Sakka ◽  
Satoshi Tachino ◽  
Hirotaka Katsuzaki ◽  
J. Susan van Dyk ◽  
Brett I. Pletschke ◽  
...  
Keyword(s):  
Bacillus Licheniformis ◽  
Genomic Analysis

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

2009 ◽  
Vol 3 (2) ◽  
pp. 41-52
Author(s):  
Rasha T. Abdullah ◽  
Abdulkareem J. Hashim ◽  
JASIM M. Karhout
Keyword(s):  
Enzyme Activity ◽  
Bovine Serum Albumin ◽  
Ion Exchange ◽  
Bacillus Licheniformis ◽  
Enzyme Characterization ◽  
Optimal Temperature ◽  
Chicken Feathers ◽  
Local Isolate ◽  
Cellulose Column ◽  
Optimal Ph

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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