The aim of this study was production and partial purification of α-amylase enzyme by Bacillus licheniformis. B. Licheniformis was allowed to grow in broth culture for purpose of inducing α-amylase enzyme. Optimal conditions for amylase production by B. Licheniformis are incubation period of 120 h, temperature of 37 °C and pH 7.0. The α-amylase enzyme was purified by ion exchange chromatography on DEAE-sepharose CL-6B and sephadex G-100 gel filtration with a 19.1-fold increase in specific activity as compared to the concentrated supernatant and with a specific activity of 926.47 U/mg. The α-amylase had the highest activity at pH 7.0 and 65 °C. According to the data on native polyacrylamide gel electrophoresis, the molecular weight of the purified enzyme was 72 kDa.
Zare Mirakabadi, A., Ghorbanpour, M., Sadeghi, A., & Sarzaeem, A. (2012). Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis. Archives of Razi Institute, 67(2), 155-160. doi: 10.22092/ari.2016.103900
MLA
A. Zare Mirakabadi; M. Ghorbanpour; A. Sadeghi; A. Sarzaeem. "Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis". Archives of Razi Institute, 67, 2, 2012, 155-160. doi: 10.22092/ari.2016.103900
HARVARD
Zare Mirakabadi, A., Ghorbanpour, M., Sadeghi, A., Sarzaeem, A. (2012). 'Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis', Archives of Razi Institute, 67(2), pp. 155-160. doi: 10.22092/ari.2016.103900
VANCOUVER
Zare Mirakabadi, A., Ghorbanpour, M., Sadeghi, A., Sarzaeem, A. Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis. Archives of Razi Institute, 2012; 67(2): 155-160. doi: 10.22092/ari.2016.103900
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