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A thermostable manganese-containing superoxide dismutase from the thermophilic fungus Thermomyces lanuginosus

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Abstract

A thermostable superoxide dismutase (SOD) from a Thermomyces lanuginosus strain (P134) was purified to homogeneity by fractional ammonium sulfate precipitation, ion-exchange chromatography on DEAE-Sepharose, Phenyl-Sepharose hydrophobic interaction chromatography, and gel filtration on Sephacryl S-100. The molecular mass of a single band of the enzyme was estimated to be 22.4 kDa, using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Using gel filtration on Sephacryl S-100, the molecular mass was estimated to be 89.1 kDa, indicating that this enzyme was composed of four identical subunits of 22.4 kDa each. The SOD was found to be inhibited by NaN3, but not by KCN or H2O2, suggesting that the SOD in T. lanuginosus was of the manganese superoxide dismutase type. The SOD exhibited maximal activity at pH 7.5. The optimum temperature for the activity was 55°C. It was thermostable at 50 and 60°C and retained 55% activity after 60 min at 70°C. The half-life of the SOD at 80°C was approximately 28 min and even retained 20% activity after 20 min at 90°C.

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Acknowledgements

This work was supported by grants from IFS (Sweden), 863 (China), and NFSC (China).

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Authors and Affiliations

  1. Department of Environmental Biology, Shandong Agricultural University, Taian, Shandong, 271018, China

    Duo-Chuan Li, Jing Gao, Ya-Ling Li & Jing Lu

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  1. Duo-Chuan Li
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  2. Jing Gao
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  3. Ya-Ling Li
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  4. Jing Lu
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Correspondence to Duo-Chuan Li.

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Communicated by K. Horikoshi

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Li, DC., Gao, J., Li, YL. et al. A thermostable manganese-containing superoxide dismutase from the thermophilic fungus Thermomyces lanuginosus. Extremophiles 9, 1–6 (2005). https://doi.org/10.1007/s00792-004-0413-4

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  • DOI: https://doi.org/10.1007/s00792-004-0413-4

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