A simple assay for measuring catalase activity: a visual approach.
A simple assay for measuring catalase activity: a visual approach.
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DOI：
10.1038/srep03081
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发表时间：
2013-10-30
影响因子：
4.6
通讯作者：
Mizunoe, Yoshimitsu
中科院分区：
文献类型：
--
作者：
Iwase, Tadayuki;Tajima, Akiko;Sugimoto, Shinya;Okuda, Ken-ichi;Hironaka, Ippei;Kamata, Yuko;Takada, Koji;Mizunoe, Yoshimitsu
在这项研究中，一种结合了定性方法的简单易行的测定过氧化氢酶活性的方法被开发出来。检测试剂只包含过氧化氢和Triton X-100。Triton X-100捕获的酶产生的氧泡被可视化为泡沫，并估计其高度。使用定义的过氧化氢酶活性单位的校准图在20-300U的范围内产生了最佳的线性拟合(y=0.3794x−2.0909，R2=0.993)。100U时的精密度和重复性分别为4.6%和4.8%。使用实验室菌株、缺乏过氧化氢酶的等基因突变株、临床分离的产志贺毒素的大肠杆菌和人类细胞，评估了该方法在测量不同样品过氧化氢酶活性方面的适用性。该分析产生了重复性好的结果。结论：该方法可用于细菌分离株和人体细胞过氧化氢酶活性的测定。
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, r2 = 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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