@article { author = {Zare Mirakabadi, A. and Ghorbanpour, M. and Sadeghi, A. and Sarzaeem, A.}, title = {Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis}, journal = {Archives of Razi Institute}, volume = {67}, number = {2}, pages = {155-160}, year = {2012}, publisher = {Razi Vaccine & Serum Research Institute}, issn = {0365-3439}, eissn = {2008-9872}, doi = {10.22092/ari.2016.103900}, abstract = {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.}, keywords = {α,amylase,Bacillus licheniformis,optimal conditions,PURIFICATION}, url = {https://archrazi.areeo.ac.ir/article_103900.html}, eprint = {https://archrazi.areeo.ac.ir/article_103900_20c251f32823f6c382e5c51451486b5a.pdf} }