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- Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea
- Junli Dong , Yuzhi Hong , Zongze Shao , Ziduo Liu
- J. Microbiol. 2010;48(3):393-398. Published online June 23, 2010
- DOI: https://doi.org/10.1007/s12275-010-9361-0
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- 31 Scopus
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Abstract
- 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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