| Title |
Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea |
| Author |
Junli Dong1, Yuzhi Hong2, Zongze Shao3, and Ziduo Liu1* |
| Address |
1State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, P. R. China, 2College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, P. R. China, 3Key Laboratory of Marine Biogenetic Resources, the Third Institute of Oceanography, State of Oceanic Administration, Xiamen 361005, P. R. China |
| Bibliography |
Journal of Microbiology, 48(3),393-398, 2010,
|
| DOI |
|
| Key Words |
M. mediterranea, endoglucanase, sodium carboxymethyl cellulase, pH-stable |
| 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. |
