[Cloning and DNA sequencing of Bacillus pumilus endo-1,4-beta-glucanase gene].
Zhi‐gang Yang, R Chen, Fengtang Yang, Xiaojing Xu
Abstract
Zhi‐gang Yang, R Chen, Fengtang Yang, Xiaojing Xu
Abstract
Bacillus pumilus S-27 screened from marine environment produces an extracellular endo-1,4-beta-glucanase. The enzyme has its optimal activity at pH 5.0-7.0 and 55 degrees C and still retained 79.0% of it at pH 9.0. The gene encoded this endo-1,4-beta-glucanase was cloned and sequenced. The structural gene contained an open reading frame of 1980 bp, corresponding to 660 amino acids, the amino acid sequence of this enzyme is very close to that of an EG of C. cellulovorans and an EG of Bacillus sp. KSM-522, all belong to the cellulase family E2.
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Bacillus pumilus S-27 screened from marine environment produces an extracellular endo-1,4-beta-glucanase. The enzyme has its optimal activity at pH 5.0-7.0 and 55 degrees C and still retained 79.0% of it at pH 9.0. The gene encoded this endo-1,4-beta-glucanase was cloned and sequenced. The structural gene contained an open reading frame of 1980 bp, corresponding to 660 amino acids, the amino acid sequence of this enzyme is very close to that of an EG of C. cellulovorans and an EG of Bacillus sp. KSM-522, all belong to the cellulase family E2.
Key concepts: Bacillus pumilus, Glucanase, Cellulase, Gene, Open reading frame, Molecular cloning, Cloning (programming), Biology