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

AuthorsNeptuno-Rodríguez, José; Espín de Gea, Juan Carlos ; Amor, Francisco del; Tudela, José ; Martínez, Vicente ; Cerdá, Antonio; García-Cánovas, Francisco
Peroxidase isoenzyme
Enzyme kinetics
Issue Date18-Apr-2000
PublisherAmerican Chemical Society
CitationJournal of Agricultural and Food Chemistry 48(5): 1537-1541 (2000)
AbstractThe 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.
Description5 pages, 6 figures, 1 table.
Publisher version (URL)http://dx.doi.org/10.1021/jf9905774
Appears in Collections:(CEBAS) Artículos
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