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Information Journal Paper

Title

PURIFICATION OF α-AMYLASE FROM BACILLUS SP. GHA1 AND ITS PARTIAL CHARACTERIZATION

Pages

  432-440

Abstract

 Bacillus sp. GHA1 was isolated from water samples and screened for the production of a-amylase. Maximum production of amylase by this strain occurs at 42oC, pH 6.5 and 72 h after cultivation in production medium. The enzyme was purified through successive applications of ammonium sulfate precipitation, ion exchange and hydrophobic interaction chromatography, resulting in a single band with an apparent molecular weight of 66 kDa, as judged by SDS-PAGE. Calcium analysis of the purified enzyme revealed that it contained three metal ions per molecule. The new extracellular a-amylase is active in a wide range of pH with its maximum activity at pH values 5.5-8.0. The optimum temperature for enzyme activity is 57oC and the presence of calcium has relatively low influence on its activity and thermostability. The BACILLUS SP. GHA1 a-amylase with these properties may be suitable for use in detergent and food industries.

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  • Cite

    APA: Copy

    AHMADI, A., GHOBADI, S., KHAJEH, K., NOUMANPOUR, B., & BADOUEI DALFARD, A.. (2010). PURIFICATION OF α-AMYLASE FROM BACILLUS SP. GHA1 AND ITS PARTIAL CHARACTERIZATION. JOURNAL OF THE IRANIAN CHEMICAL SOCIETY(JICS), 7(2), 432-440. SID. https://sid.ir/paper/282370/en

    Vancouver: Copy

    AHMADI A., GHOBADI S., KHAJEH K., NOUMANPOUR B., BADOUEI DALFARD A.. PURIFICATION OF α-AMYLASE FROM BACILLUS SP. GHA1 AND ITS PARTIAL CHARACTERIZATION. JOURNAL OF THE IRANIAN CHEMICAL SOCIETY(JICS)[Internet]. 2010;7(2):432-440. Available from: https://sid.ir/paper/282370/en

    IEEE: Copy

    A. AHMADI, S. GHOBADI, K. KHAJEH, B. NOUMANPOUR, and A. BADOUEI DALFARD, “PURIFICATION OF α-AMYLASE FROM BACILLUS SP. GHA1 AND ITS PARTIAL CHARACTERIZATION,” JOURNAL OF THE IRANIAN CHEMICAL SOCIETY(JICS), vol. 7, no. 2, pp. 432–440, 2010, [Online]. Available: https://sid.ir/paper/282370/en

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