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首页> 外文期刊>Journal of Advances in Biology & Biotechnology >Extraction, Partial Purification and Characterization of Peroxidase from Calotropis procera Leaves
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Extraction, Partial Purification and Characterization of Peroxidase from Calotropis procera Leaves

机译：东方菜叶中过氧化物酶的提取，部分纯化和鉴定

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Aim: This study was aimed at the isolation, partial purification and characterization of peroxidase from low cost material, Calotropis procera leaves. Materials and Methods: Partial purification of crude enzyme extract was done by ammonium sulfate precipitation followed by dialysis against Tris-HCl buffer. Peroxidase activity was measured spectrophotometrically. Results: It was observed that after partial purification, the enzyme specific activity was increased as compared to crude enzyme extract. Peroxidase from Calotropis procera leaves was purified up to 2.04 fold with specific activity of 2.68 U/mg after dialysis. The partially purified peroxidase displayed optimum activity at temperature 50°C and pH 6.0. The kinetic data shows that guaiacol is a better substrate than ABTS. All the tested metal ions (Fe3+, Co2+, Ni2+, Mg2+, Zn2+) and EDTA exhibited strong inhibitory effects on the Calotropis procera leaves peroxidase. Conclusion: It is more evident that Calotropis procera leaves are a good source of peroxidase. It is therefore, concluded that further purification and full biochemical characterization of this enzyme may serve as a promising option to be explored for industrial purposes.
机译：目的：本研究旨在从低成本材料Calotropis procera叶子中分离，部分纯化和表征过氧化物酶。材料和方法：粗酶提取物的部分纯化是通过硫酸铵沉淀，然后用Tris-HCl缓冲液进行透析来进行的。分光光度法测量过氧化物酶活性。结果：观察到部分纯化后，酶比活性与粗酶提取物相比增加。透析后，纯化后的原花菜叶片的过氧化物酶被纯化至2.04倍，比活性为2.68 U / mg。部分纯化的过氧化物酶在温度50°C和pH 6.0时显示最佳活性。动力学数据表明，愈创木酚是比ABTS更好的底物。所有测试的金属离子（Fe 3 + ，Co 2 + ，Ni 2 + ，Mg 2 + ， Zn 2 + ）和EDTA对Calotropis procera叶片的过氧化物酶具有较强的抑制作用。结论：更明显的是，斜纹夜蛾叶片是过氧化物酶的良好来源。因此，得出的结论是，对该酶的进一步纯化和完整的生化特性可作为工业用途探索的有前途的选择。

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