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Ionically Bound Peroxidase from Peach Fruit BABT
Neves,Valdir Augusto.
Soluble, ionically bound peroxidase (POD) and polyphenoloxidase (PPO) were extracted from the pulp of peach fruit during ripening at 20°C. Ionically bound form was purified 6.1-fold by DEAE-cellulose and Sephadex G-100 chromatography. The purified enzyme showed only one peak of activity on Sephadex G-100 and PAGE revealed that the enzyme was purified by the procedures adopted. The purified enzyme showed a molecular weight of 29000 Da, maximum activity at pH 5.0 and at 40ºC. The calculated apparent activation energy (Ea) for the reaction was10.04 kcal/mol. The enzyme was heat-labile in the temperature range of 60 to 75ºC with a fast inactivation at 75ºC. Measurement of residual activity showed a stabilizing effect of sucrose at various temperature/sugar...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Peach peroxidases; Ripening; Purification; Kinetics; Heat stability.
Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132002000100002
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