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Purification and Kinetic Characterization of Peroxidase from Tomato Cultivated under Different Salinity Conditions
Author(s) -
RodríguezLópez J.N.,
Espín J.C.,
Tudela J.,
Martínez V.,
Cerdá A.,
GarcíaCánovas F.
Publication year - 2000
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2000.tb15948.x
Subject(s) - peroxidase , salinity , hydrogen peroxide , substrate (aquarium) , chemistry , isozyme , homogeneous , enzyme , chromatography , food science , horticulture , botany , biochemistry , biology , ecology , physics , thermodynamics
By including hydrophobic chromatography in the purification scheme, 2 homogeneous tomato fruit peroxidase isoenzymes were obtained. The expression of these 2 peroxidases, one acid and the other basic, was determined in tomato fruits grown under different salinity conditions. Increased salinity modified the isoenzyme profile of tomato peroxidase. In tomatoes grown under highly saline conditions, there was an increase in the expression of the acid form with respect to the basic, the acid/basic ratio rising from 4.5 in tomatoes grown under normal saline conditions to 70 in those grown in highly saline conditions. Kinetic studies using 2,2′‐azinobis(3‐ethylbenzo‐thiazolinesulfonic acid) as reducing substrate showed that increased salinity in the growth medium did not modify the kinetic parameter of tomato peroxidase over both hydrogen peroxide or reducing substrate.