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|Type:||Artigo de periódico|
|Title:||Extraction and partial characterization of peroxidase from Copaifera langsdorffii Desf. leaves|
|Abstract:||In the literature, several processes have been described to obtain peroxidases. The purpose of this work was to obtain peroxidase from Copaifera langsdorffii leaves and characterize it partially using a factorial design of experiments and univaried tests, to confirm the results obtained by the factorial design of experiments. Peroxidase activity was measured using the guaiacol: hydrogen peroxide system. The isolated peroxidase presented 81.6% of horseradish peroxidase activity and was easy to obtain from leaves of an abundant tree distributed all over the country. Semi-purified peroxidase (COP) was precipitated with acetone 65% (v.v(-1)) of the crude extract, obtaining the acetone powder. The COP optimum reaction pH values were between 5.0-7.0 and the temperatures between 5 and 45 degrees C, with a maximum activity at pH 6.0 and 35 degrees C. The enzyme was stable in temperatures below 50 degrees C and pH from 4.5 to 9.0 for up to 24 hours. The peroxidase was inactivated after 4 hours at 80 degrees C and after 3 minutes at 96 degrees C. This enzyme can possibly be used as a diagnostic reagent, biosensor and for other analytical methods in several fields of Sciences.|
|Editor:||Soc Brasileira Ciencia Tecnologia Alimentos|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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