Cel8H, a Novel Endoglucanase from the Halophilic Bacterium Halomonas sp. S66-4: Molecular Cloning, Heterogonous Expression, and Biochemical Characterization

Xiaoluo Huang; Zongze Shao; Yuzhi Hong; Ling Lin; Chanjuan Li; Fei Huang; Hui Wang; Ziduo Liu

doi:10.1007/s12275-009-0188-5

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Cel8H, a Novel Endoglucanase from the Halophilic Bacterium Halomonas sp. S66-4: Molecular Cloning, Heterogonous Expression, and Biochemical Characterization: Xiaoluo Huang ¹, Zongze Shao ², Yuzhi Hong ³, Ling Lin ¹, Chanjuan Li ¹, Fei Huang ¹, Hui Wang ¹, Ziduo Liu ¹; Journal of Microbiology 2010;48(3):318-324.
DOI: https://doi.org/10.1007/s12275-009-0188-5
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, ²Key Laboratory of Marine Biogenetic Resources, The Third Institute of Oceanography, State of Oceanic Administration, Xiamen 361005, P. R. China, ³College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, P. R. China¹State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, P. R. China, ²Key Laboratory of Marine Biogenetic Resources, The Third Institute of Oceanography, State of Oceanic Administration, Xiamen 361005, P. R. China, ³College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, P. R. China

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

Received: 16 June 2009 • Accepted: 20 August 2009

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Abstract

A recombinant Escherichia coli clone expressing an endoglucanase was identified from a genomic library of the halophilic bacterium Halomonas sp. S66-4, and the enzyme was designated Cel8H. The cel8H gene consisted of 1,053 bp and encoded 350 amino acids sharing the highest identity of 48% to other known endoglucanases. The protein was expressed in E. coli BL21 (DE3) and purified to homogeneity. The purified recombinant enzyme had an optimal activity of 4.9 U/mg at pH 5 and 45°C toward the substrate carboxymethylcellulose. It exhibited extraordinary properties which differed from endoglucanases reported previously at the point of high salt tolerance above 5 M, simultaneously with high pH stability at pH 4-12 and high temperature stability at 40-60°C. Various substrate tests indicated that the enzyme hydrolyzes β-1,4-glucosidic bonds specifically.

Keywords: endoglucanase;salt tolerance;pH stability;temperature stability;Halomonas sp.

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Cel8H, a Novel Endoglucanase from the Halophilic Bacterium Halomonas sp. S66-4: Molecular Cloning, Heterogonous Expression, and Biochemical Characterization

J. Microbiol. 2010;48(3):318-324. Published online June 23, 2010

DOI: https://doi.org/10.1007/s12275-009-0188-5

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