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A Novel Endoglucanase (Cel9P) From a Marine Bacterium Paenibacillus sp. BME-14

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Abstract

By constructing a genomic library, an endoglucanase gene (cel9P) was cloned from Paenibacillus sp. BME-14 which was isolated from the sea. It had an open-reading frame of 1,629 bp, encoding a peptide of 542-amino acid residue with a calculated molecular mass of 60 kDa. The enzyme showed the highest amino acid identity of 52% with other known endoglucanases and had a C-terminal catalytic domain belonging to the glycosyl hydrolases family 9. The optimum pH and temperature for enzymatic activity was pH 6.5 and 35 °C. The metal ions of Ca2+, Mg2+, and Mn2+ had a positive effect on the activity while Hg2+, Cu2+, and EDTA had a negative effect. Notably, Cel9P had 65% of the maximal activity at 5 °C. Based on the special characteristic of Cel9P, it had a potential significance for study of cold-active mechanism and industry applications.

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Acknowledgments

This work was supported by grants from the National Natural Sciences Foundation of China (30770021 and 30570057) and the 111 project (B07041).

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Authors and Affiliations

  1. State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People’s Republic of China

    Xiaoyu Fu, Pengfu Liu, Ling Lin, Xiaoluo Huang, Xin Meng & Ziduo Liu

  2. College of Plant Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People’s Republic of China

    Yuzhi Hong

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  1. Xiaoyu Fu
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  2. Pengfu Liu
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  3. Ling Lin
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  7. Ziduo Liu
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Correspondence to Ziduo Liu.

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Fu, X., Liu, P., Lin, L. et al. A Novel Endoglucanase (Cel9P) From a Marine Bacterium Paenibacillus sp. BME-14. Appl Biochem Biotechnol 160, 1627–1636 (2010). https://doi.org/10.1007/s12010-009-8648-2

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