4.7 Article

Purification and characterization of soluble peroxidase from oil palm (Elaeis guineensis Jacq.) leaf

Journal

PHYTOCHEMISTRY
Volume 61, Issue 5, Pages 503-511

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0031-9422(02)00167-X

Keywords

Elaeis guineensis Jacq.; oil palm; leaflet; enzyme purification; peroxidase; vascular bundle; xylem; phloem

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Soluble peroxidase (POD) from oil palm leaf was purified by (NH4)(2)SO4 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. (C) 2002 Elsevier Science Ltd. All rights reserved.

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