%0 Journal Article
%T Two-step purification and partial characterization of an extra cellular ¦Á-amylase from Bacillus licheniformis
%A Zare Mirakabadi
%A A.
%A Ghorbanpour
%A M.
%A Sadeghi
%A A.
%A Sarzaeem
%A A.
%J Archives of Razi Institute
%D 2012
%I Razi Vaccine and Serum Research Institute, Karaj
%X The aim of this study was production and partial purification of ¦Á-amylase enzyme by Bacillus licheniformis. B. Licheniformis was allowed to grow in broth culture for purpose of inducing ¦Á-amylase enzyme. Optimal conditions for amylase production by B. Licheniformis are incubation period of 120 h, temperature of 37 ¡ãC and pH 7.0. The ¦Á-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 ¦Á-amylase had the highest activity at pH 7.0 and 65 ¡ãC. According to the data on native polyacrylamide gel electrophoresis, the molecular weight of the purified enzyme was 72 kDa.
%K ¦Á -Amylase
%K Bacillus licheniformis
%K optimal conditions
%K purification
%U http://www.archrazi.com/browse.php?a_id=323&sid=1&slc_lang=en