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


Autoria(s): Maciel,Hermelinda Penha Freire; Gouvêa,Cibele Marli Cação Paiva; Toyama,Marcos; Smolka,Marcus; Marangoni,Sergio; Pastore,Gláucia Maria
Data(s)

01/10/2007

Resumo

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.

Formato

text/html

Identificador

http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422007000500003

Idioma(s)

en

Publicador

Sociedade Brasileira de Química

Fonte

Química Nova v.30 n.5 2007

Palavras-Chave #Copaifera langsdorffii #peroxidase #vegetal extract
Tipo

journal article