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Characterization of peroxidase-mediated chlorophyll bleaching in strawberry fruit


Characterization of peroxidase-mediated chlorophyll bleaching in strawberry fruit



Phytochemistry 58(3): 379-387



ISSN/ISBN: 0031-9422

PMID: 11557069

DOI: 10.1016/s0031-9422(01)00266-7

Peroxidase (POX) from strawberry fruits was analyzed for its capacity to bleach chlorophyll. The partially purified enzyme preperation catalyzed the bleaching of chlorophylls and their derivatives in the presence of H2O2 and phenolic compounds. The optimal reaction conditions were 35 degrees C, pH 5.2 and ionic strength equal to 0.2. The maximum activity was observed at 1 mM of H2O2, while higher concentrations inhibited enzyme activity. Compounds with a high affinity to the heme group, radical scavengers and reducing agents, showed an inhibitory effect. Phenolic compounds such as umbelliferone, naringenin and p-substituted monophenols acted as cofactors. Instead, other phenolic compounds tested such as caffeic acid, catechin, ellagic acid, esculin and quercetin inhibited the activity of POX on chlorophylls. Phenolic compounds extracted from strawberry fruits showed an inhibitory effect on POX-chlorophyll bleaching activity, although this effect decreased markedly during ripening. POX showed higher affinity for compounds derived from chlorophyll a than from chlorophyll b, and the enzyme preferentially degraded chlorophyll derivatives with the Mg(2+) ion present and the phytol group removed. The POX-chlorophyll bleaching activity was found in all ripening stages from small green to ripe, the highest activity corresponding to large green fruits.

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Accession: 003380582

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