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Título

Purification and kinetic characterization of an anionic peroxidase from melon (Cucumis melo L.) cultivated under different salinity conditions

AutorNeptuno-Rodríguez, José; Espín de Gea, Juan Carlos ; Amor, Francisco del; Tudela, José ; Martínez, Vicente ; Cerdá, Antonio; García-Cánovas, Francisco
Palabras claveMelon
Peroxidase
Salinity
Peroxidase isoenzyme
Enzyme kinetics
Fecha de publicación18-abr-2000
EditorAmerican Chemical Society
CitaciónJournal of Agricultural and Food Chemistry 48(5): 1537-1541 (2000)
ResumenThe partial characterization of an anionic peroxidase in melon fruit is described. Four melon peroxidase (MPX) isoenzymes were detected in crude extracts after isoelectric focusing. The major MPX isoenzyme (pI = 3.7) was partially purified by including hydrophobic and anion-exchange chromatography in the purification scheme. The sample obtained was used to characterize MPX. This peroxidase did not show activity on ascorbic acid but oxidized guaiacol at a high rate, showing an optimum pH of 5.5 when acting on this last reducing substrate. Melon fruits grown under highly saline conditions showed slightly increased levels of this anionic isoenzyme. Kinetic studies using 2,2‘-azinobis(3-ethylbenzothiazolinesulfonic acid) (ABTS) as reducing substrate showed that increased salinity in the growth medium did not modify the kinetic parameters of melon peroxidase on both hydrogen peroxide and reducing substrate.
Descripción5 pages, 6 figures, 1 table.
Versión del editorhttp://dx.doi.org/10.1021/jf9905774
URIhttp://hdl.handle.net/10261/18197
DOI10.1021/jf9905774
ISSN1520-5118 (Online)
0021-8561 (Print)
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