title: Purification and characterization of soluble peroxidase from oil palm (Elaeis guineensis Jacq) leaf.
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.
authors.affiliation: Agro Processing Division, Industrial Estate P O, Trivandrum 695 019, Kerala, India.
authors.forename: S S
authors.initials: SS
authors.lastname: Deepa
authors.forename: C
authors.initials: C
authors.lastname: Arumughan
mesh_terms: D000918:Antibody Specificity; D028023:Arecaceae / Q000201:enzymology*; D002241:Carbohydrates / Q000032:analysis; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007150:Immunohistochemistry; D008970:Molecular Weight; D010544:Peroxidases / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism*; D018515:Plant Leaves / Q000201:enzymology; D012995:Solubility; D013997:Time Factors
chemical_list: D002241:Carbohydrates; D010544:Peroxidases