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Molecular cloning, characterization, and heterologous expression of a new κ-carrageenase gene from marine bacterium Zobellia sp. ZM-2

  • Applied genetics and molecular biotechnology
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Abstract

κ-Carrageenases exhibit apparent distinctions in gene sequence, molecular weight, enzyme properties, and posttranslational processes. In this study, a new κ-carrageenase gene named cgkZ was cloned from the marine bacterium Zobellia sp. ZM-2. The gene comprised an open reading frame of 1,638 bp and encoded 545 amino acids. The natural signal peptide of κ-carrageenase was used successfully for the secretory production of the recombinant enzyme in Escherichia coli. A posttranslational process that removes an amino acid sequence of about 20 kDa from the C-terminal end of κ-carrageenase was first discovered in E. coli. An increase in enzyme activity by 167.3 % in the presence of 5 mM DTT was discovered, and Na+ at a certain concentration range was positively correlated with enzyme activity. The κ-carrageenase production of E. coli was 9.0 times higher than that of ZM-2. These results indicate the potential use of the enzyme in the biotechnological industry.

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Acknowledgments

This work was supported by the National Natural Science Foundation of China (no. 41076087), Program for New Century Excellent Talents in University (NCET-10-0719), and Program for Changjiang Scholars and Innovative Research Team in University.

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Authors and Affiliations

  1. College of Food Science and Engineering, Ocean University of China, Qingdao, 266003, China

    Zhemin Liu & Haijin Mou

  2. Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, 266071, China

    Guiyang Li & Zhaolan Mo

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  1. Zhemin Liu
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  2. Guiyang Li
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  3. Zhaolan Mo
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  4. Haijin Mou
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Correspondence to Haijin Mou.

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Liu, Z., Li, G., Mo, Z. et al. Molecular cloning, characterization, and heterologous expression of a new κ-carrageenase gene from marine bacterium Zobellia sp. ZM-2. Appl Microbiol Biotechnol 97, 10057–10067 (2013). https://doi.org/10.1007/s00253-013-5215-0

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  • DOI: https://doi.org/10.1007/s00253-013-5215-0

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