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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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 Title & Authors
Comparison of enzyme activities of the native and N-terminal 6xHis-tagged Fe supreoxide dismutase from Streptomyces subrutilus P5
Park, Joong-ho; Kim, Jae-heon;
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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 the enzyme lost the activity after 360 min. In contrast, the native FeSOD was stable after 720 min at below . 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 , it can be assumed that the protein structure became destabilized under different storage conditions and sensitive to the enzyme inhibitor.
Streptomyces subrutilus P5;6xHis tag;Fe superoxide dismutase;heat;pH;stability;
 Cited by
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