Journal
SCIENTIFIC REPORTS
Volume 3, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep03081
Keywords
TECHNIQUES AND APPLICATIONS; BIOCHEMICAL ASSAYS
Categories
Funding
- Jikei University
- Jikei University Graduate Research Fund
- Uehara Memorial Foundation
- MEXT
- Science Research Promotion Fund of The Promotion and Mutual Aid Corporation for Private Schools of Japan (non-profit organization)
- 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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