A Highly Active Alpha Amylase from Bacillus licheniformis: Directed Evolution, Enzyme Characterization and Structural Analysis

2014 ◽  
Vol 24 (7) ◽  
pp. 898-904 ◽  
Author(s):  
Yihan Liu ◽  
Shuai Fan ◽  
Xiaoguang Liu ◽  
Zhimeng Zhang ◽  
Jianling Wang ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Directed Evolution ◽  
Bacillus Licheniformis ◽  
Enzyme Characterization ◽  
Alpha Amylase ◽  
Highly Active

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.

scholarly journals Hyperthermostable mutants of Bacillus licheniformis alpha-amylase: thermodynamic studies and structural interpretation

1997 ◽  
Vol 10 (5) ◽  
pp. 541-549 ◽  
Author(s):  
N. Declerck ◽  
M. Machius ◽  
R. Chambert ◽  
G. Wiegand ◽  
R. Huber ◽  
...  
Keyword(s):  
Bacillus Licheniformis ◽  
Alpha Amylase ◽  
Thermodynamic Studies ◽  
Structural Interpretation

Molecular cloning in Bacillus subtilis of a Bacillus licheniformis gene encoding a thermostable alpha amylase

Gene ◽  
1983 ◽  
Vol 23 (3) ◽  
pp. 267-276 ◽  
Author(s):  
Stephen A. Ortlepp ◽  
James F. Ollington ◽  
David J. McConnell
Keyword(s):  
Bacillus Subtilis ◽  
Molecular Cloning ◽  
Bacillus Licheniformis ◽  
Alpha Amylase ◽  
Gene Encoding

Pearl millet, a source of alpha amylase production by Bacillus licheniformis

2005 ◽  
Vol 96 (10) ◽  
pp. 1201-1204 ◽  
Author(s):  
Ikram-ul-Haq ◽  
Hamad Ashraf ◽  
Qadeer M.A. ◽  
Javed Iqbal
Keyword(s):  
Pearl Millet ◽  
Bacillus Licheniformis ◽  
Alpha Amylase ◽  
Amylase Production
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