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KMID : 0880220100480030393
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Journal of Microbiology
2010 Volume.48 No. 3 p.393 ~ p.398
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Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea
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Dong Jun-Il
Hong Yu-Zhi
Shao Zong-Ze
Liu Zi-Duo
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Abstract
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A novel gene encoding an endoglucanase designated Cel5D was cloned from a marine bacterium Martelella mediterranea by genomic library. The gene had a 1,113 bp opening reading frame encoding a 371-amino-acid protein with a molecular mass of 40,508 Da and containing a putative signal peptide (41 amino acids). Cel5D had low similarity (48-51% identity) with other known endoglucanases and consisted of one single catalytic domain, which belonged to the glycosyl hydrolase family 5. The maximum activity of Cel5D was observed at 60°C and pH 5.0. Cel5D displayed broad pH stability within the range of pH 3.0-11.0 and retained hydrolytic activity in the presence of a wide variety of metal ions and some chemical reagents. These characteristics suggest that the enzyme has considerable potential in industrial applications.
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KEYWORD
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M. mediterranea, endoglucanase, sodium carboxymethyl cellulase, pH-stable
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