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首页> 外文期刊>Química Nova >Extraction, purification and biochemical characterization of a peroxidase from Copaifera langsdorffii leaves
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Extraction, purification and biochemical characterization of a peroxidase from Copaifera langsdorffii leaves

机译：兰番石榴叶中过氧化物酶的提取，纯化和生化特性

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The aim of this work is to obtain, purify and characterize biochemically a peroxidase from Copaifera langsdorffii leaves (COP). COP was obtained by acetone precipitation followed by ion-exchange chromatography. Purification yielded 3.5% of peroxidase with the purification factor of 46.86. The COP optimum pH is 6.0 and the temperature is 35 oC. COP was stable in the pH range of 4.5 to 9.3 and at temperatures below 50.0 oC. The apparent Michaelis-Menten constants (Km) for guaiacol and H2O2 were 0.04 mM and 0.39 mM respectively. Enzyme turnover was 0.075 s-1 for guaiacol and 0.28 s-1 for hydrogen peroxide. Copaifera langsdorffii leaves showed to be a rich source of active peroxidase (COP) during the whole year. COP could replace HRP, the most used peroxidase, in analytical determinations and treatment of industrial effluents at low cost.
机译：这项工作的目的是获得，纯化和化学表征兰卡多菲叶（COP）的过氧化物酶。通过丙酮沉淀，然后进行离子交换色谱法获得COP。纯化产生3.5％的过氧化物酶，纯化因子为46.86。 COP的最佳pH为6.0，温度为35 oC。 COP在4.5至9.3的pH范围和低于50.0 oC的温度下稳定。愈创木酚和过氧化氢的表观Michaelis-Menten常数（Km）分别为0.04 mM和0.39 mM。愈创木酚的酶转化率为0.075 s-1，过氧化氢的酶转化为0.28 s-1。在整个一年中，Copaifera langsdorffii叶片是活性过氧化物酶（COP）的丰富来源。在分析测定和工业废水处理中，COP可以低成本替代最常用的过氧化物酶HRP。

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