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Peroxidase from peach fruit: thermal Stability BABT
Neves,Valdir Augusto; Lourenço,E. J..
Peroxidase from peach fruit was purified 28.9-fold by DEAE-cellulose, Sephadex G-100 and hydroxylapatite chromatography. The purified enzyme showed only one peak of activity with an optimum pH of 5.0 and temperature of 40ºC. The calculated activation energy (Ea) for the reaction was 7.97 kcal/mol. The enzyme was heat-labile in the temperature range of 60 to 80ºC with a fast inactivation at 80ºC. PAGE of the inactivation course at 70ºC showed only one band of activity. Different sugars increased the heat stability of the activity in the following order: sucrose>lactose>glucose>fructose. Measurement of residual activity showed a stabilizing effect of sucrose at various temperature/sugar concentrations (10 to 40%, w/w) with the Ea for inactivation...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Peach peroxidase; Purification; Heat stability; Regeneration.
Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131998000200002
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