Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea

Junli Dong; Yuzhi Hong; Zongze Shao; Ziduo Liu

doi:10.1007/s12275-010-9361-0

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Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea: Junli Dong ¹, Yuzhi Hong ², Zongze Shao ³, Ziduo Liu ¹; Journal of Microbiology 2010;48(3):393-398.
DOI: https://doi.org/10.1007/s12275-010-9361-0
Published online: June 23, 2010

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. China¹State 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

Corresponding author: Ziduo Liu , Tel: +86-27-8728-1429,

Received: 23 November 2009 • Accepted: 3 March 2010

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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.

Keywords: M. mediterranea;endoglucanase;sodium carboxymethyl cellulase;pH-stable

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Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea

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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