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Information Journal Paper

Title

TWO-STEP PURIFICATION AND PARTIAL CHARACTERIZATION OF AN EXTRA CELLULAR α-AMYLASE FROM BACILLUS LICHENIFORMIS

Pages

  155-160

Abstract

 The aim of this study was production and partial PURIFICATION of a-amylase enzyme by BACILLUS LICHENIFORMIS. B. Licheniformis was allowed to grow in broth culture for purpose of inducing a-amylase enzyme. OPTIMAL CONDITIONS for amylase production by B. Licheniformis are incubation period of 120 h, temperature of 37oC and pH 7.0. The a-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 65oC. According to the data on native polyacrylamide gel electrophoresis, the molecular weight of the purified enzyme was 72 kDa.

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  • Cite

    APA: Copy

    ZARE MIRAKABADI, A., GHORBANPOUR, M., SADEGHI, M., & SARZAIEM, 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. SID. https://sid.ir/paper/120112/en

    Vancouver: Copy

    ZARE MIRAKABADI A., GHORBANPOUR M., SADEGHI M., SARZAIEM A.. TWO-STEP PURIFICATION AND PARTIAL CHARACTERIZATION OF AN EXTRA CELLULAR α-AMYLASE FROM BACILLUS LICHENIFORMIS. ARCHIVES OF RAZI INSTITUTE[Internet]. 2012;67(2):155-160. Available from: https://sid.ir/paper/120112/en

    IEEE: Copy

    A. ZARE MIRAKABADI, M. GHORBANPOUR, M. SADEGHI, and A. SARZAIEM, “TWO-STEP PURIFICATION AND PARTIAL CHARACTERIZATION OF AN EXTRA CELLULAR α-AMYLASE FROM BACILLUS LICHENIFORMIS,” ARCHIVES OF RAZI INSTITUTE, vol. 67, no. 2, pp. 155–160, 2012, [Online]. Available: https://sid.ir/paper/120112/en

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