alexa Cel8H, a novel endoglucanase from the halophilic bacterium Halomonas sp. S66-4: molecular cloning, heterogonous expression, and biochemical characterization.
Environmental Sciences

Environmental Sciences

Journal of Bioremediation & Biodegradation

Author(s): Huang X, Shao Z, Hong Y, Lin L, Li C,

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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 degrees 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 degrees C. Various substrate tests indicated that the enzyme hydrolyzes beta-1,4-glucosidic bonds specifically. This article was published in J Microbiol and referenced in Journal of Bioremediation & Biodegradation

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