2024-03-28T10:16:39Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/181972019-02-27T10:45:38Zcom_10261_72com_10261_6col_10261_325
Neptuno-Rodríguez, José
Espín de Gea, Juan Carlos
Amor, Francisco del
Tudela, José
Martínez, Vicente
Cerdá, Antonio
García-Cánovas, Francisco
2009-10-30T09:32:18Z
2009-10-30T09:32:18Z
2000-04-18
Journal of Agricultural and Food Chemistry 48(5): 1537-1541 (2000)
0021-8561
http://hdl.handle.net/10261/18197
10.1021/jf9905774
1520-5118
http://dx.doi.org/10.13039/501100007273
The 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.
eng
closedAccess
Melon
Peroxidase
Salinity
Peroxidase isoenzyme
Enzyme kinetics
Purification and kinetic characterization of an anionic peroxidase from melon (Cucumis melo L.) cultivated under different salinity conditions
artículo