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KMID : 0364820160520020230
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Korean Journal of Microbiology
2016 Volume.52 No. 2 p.230 ~ p.235
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Comparison of enzyme activities of the native and N-terminal 6xHis tagged Fe supreoxide dismutase from Streptomyces subrutilus P5
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Park Joong-Ho
Kim Jae-Heon
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Abstract
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This study was carried out to analyze the differences in enzyme activity and stability between the native Fe superoxide
dismutase (FeSOD) and the 6xHis-tagged superoxide dismutase (6xHis-FeSOD) of Streptomyces subrutilus P5. The optimum pHs for both native FeSOD and 6xHis-FeSOD were 7, while the pH range of the activity was narrower for the 6xHis-FeSOD. The native FeSOD was stable at pH 4?9, but the 6xHis-FeSOD lost its stability at pH > 9. The temperatures of the optimum activities were same for both types of enzymes. However, the heat stability of the 6xHis-FeSOD was clearly decreased; even at 20°C the enzyme lost the activity after 360 min.
In contrast, the native FeSOD was stable after 720 min at below 40°C. H2O2 inhibition was occurred already at 0.5 mM for the 6xHis-tagged enzyme. Therefore, from the results that the 6xHis-FeSOD retained the enzyme activity at pH 6?7 and 20?40°C, it can be assumed that the protein structure became destabilized under different storage conditions and sensitive to the enzyme inhibitor.
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KEYWORD
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Streptomyces subrutilus P5, 6xHis tag, Fe superoxide dismutase, heat, pH, stability
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