4.7 Article

A Simple Assay for Measuring Catalase Activity: A Visual Approach

Journal

SCIENTIFIC REPORTS
Volume 3, Issue -, Pages -

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/srep03081

Keywords

TECHNIQUES AND APPLICATIONS; BIOCHEMICAL ASSAYS

Funding

  1. Jikei University
  2. Jikei University Graduate Research Fund
  3. Uehara Memorial Foundation
  4. MEXT
  5. Science Research Promotion Fund of The Promotion and Mutual Aid Corporation for Private Schools of Japan (non-profit organization)
  6. Grants-in-Aid for Scientific Research [23590521] Funding Source: KAKEN

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In this study, an assay that combines the ease and simplicity of the qualitative approach for measuring catalase activity was developed. The assay reagents comprised only hydrogen peroxide and Triton X-100. The enzyme-generated oxygen bubbles trapped by Triton X-100 were visualized as foam, whose height was estimated. A calibration plot using the defined unit of catalase activity yielded the best linear fit over a range of 20-300 units (U) (y = 0.3794x - 2.0909, r(2) = 0.993). The assay precision and reproducibility at 100 U were 4.6% and 4.8%, respectively. The applicability of the assay for measuring the catalase activity of various samples was assessed using laboratory strains of Escherichia coli, catalase-deficient isogenic mutants, clinically isolated Shiga toxin-producing E. coli, and human cells. The assay generated reproducible results. In conclusion, this new assay can be used to measure the catalase activity of bacterial isolates and human cells.

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