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Characterization of novel thermostable dextranase from Thermotoga lettingae TMO

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Abstract

Biochemical properties of a putative thermostable dextranase gene from Thermotoga lettingae TMO were determined in a recombinant protein (TLDex) expressed in Escherichia coli and purified to sevenfold apparent homogeneity. The 64-kDa protein displayed maximum activity at pH 4.3, and enzyme activity was stable from pH 4.3–10. The optimal temperature was 55–60°C during 15 min incubation, and the half-life of the enzyme was 1.5 h at 65°C. The enzyme showed higher activity against α-(1 → 6) glucan and released isomaltose and isomaltotriose as main products from dextran T2000. An unusual kinetic feature of TLDex was the negative cooperative behavior on the reaction of dextran T2000 cleavage. Enzyme activity was not significantly affected by the presence of metal ions, except for the strong inhibited by 1 mM Fe2+ and Ag2+. TLDex may prove useful as an enzyme for high temperature sugar milling processes.

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Acknowledgements

This work was partially supported by grant No. RTI05-01-01 from the Regional Technology Innovation Program of the Ministry of Knowledge Economy (MKE), South Korea. We are also thankful to Korea Basic Science Institute Gwangju Branch for the DNA sequencing.

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Authors and Affiliations

  1. School of Biological Sciences and Technology, Chonnam National University, Gwangju, 500-757, Republic of Korea

    Young-Min Kim

  2. School of Biological Sciences and Technology & Research Institute for Catalysis, Chonnam National University, Gwangju, 500-757, Republic of Korea

    Doman Kim

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  1. Young-Min Kim
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  2. Doman Kim
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Correspondence to Doman Kim.

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Kim, YM., Kim, D. Characterization of novel thermostable dextranase from Thermotoga lettingae TMO. Appl Microbiol Biotechnol 85, 581–587 (2010). https://doi.org/10.1007/s00253-009-2121-6

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  • DOI: https://doi.org/10.1007/s00253-009-2121-6

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