Extraction, purification and biochemical characterization of a peroxidase from Copaifera langsdorffii leaves

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Abstract

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°C. COP was stable in the pH range of 4.5 to 9.3 and at temperatures below 50.0°C. 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 p eroxidase, in analytical determinations and treatment of industrial effluents at low cost.

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Maciel, H. P. F., Gouvêa, C. M. C. P., Toyama, M., Smolka, M., Marangoni, S., & Pastore, G. M. (2007). Extraction, purification and biochemical characterization of a peroxidase from Copaifera langsdorffii leaves. Quimica Nova, 30(5), 1067–1071. https://doi.org/10.1590/S0100-40422007000500003

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