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

Authors :: Deepa SS
Arumughan C
Source :: Phytochemistry [Phytochemistry] 2002 Nov; Vol. 61 (5), pp. 503-11.
Publication Year :: 2002
Abstract: Soluble peroxidase (POD) from oil palm leaf was purified by (NH(4))(2)SO(4) 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.

Subjects :: Antibody Specificity
Carbohydrates analysis
Enzyme Stability
Hot Temperature
Hydrogen-Ion Concentration
Immunohistochemistry
Molecular Weight
Peroxidases chemistry
Peroxidases immunology
Plant Leaves enzymology
Solubility
Time Factors
Arecaceae enzymology
Peroxidases isolation & purification
Peroxidases metabolism

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