Purification and characterization of soluble peroxidase from oil palm (Elaeis guineensis Jacq.) leaf
2002
Deepa, S.S. | Arumughan, C.
Soluble peroxidase (POD) from oil palm leaf was purified by (NH4)2SO4 precipitation, anion exchange chromatography and molecular exclusion chromatography. The purification grade obtained was 429 yielding 54% of the enzyme activity. Electrophoresis of purified enzyme under denatured conditions revealed M(r) of 48 +/- 2 kDa. It has an optimum pH of 5 and it exhibited very high pH and thermal stabilities. K(m) for guaiacol, ABTS and pyrogallol were 3.96, 1 and 0.84 mM, respectively. Immunocytochemical localization studies showed that soluble POD was mainly located in the vascular bundles and epidermis of leaf.
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