Peroxidase from peach fruit: Thermal stability
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Data
1998-01-01
Autores
Neves, V. A.
Lourenco, E. J.
Título da Revista
ISSN da Revista
Título de Volume
Editor
Inst Tecnologia Parana
Resumo
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 40 degreesC. 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 80 degreesC with a fast inactivation at 80 degreesC. PAGE of the inactivation course at 70 degreesC 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 increasing with sucrose concentration from 0 to 20% (w/w). After inactivation at 70 degreesC and 75 degreesC the enzyme was able to be reactivated by up to 40% of the initial activity when stared at 30 degreesC.
Descrição
Palavras-chave
peach peroxidase, purification, heat stability, regeneration
Como citar
Brazilian Archives of Biology and Technology. Curitiba-Paraná: Inst Tecnologia Parana, v. 41, n. 2, p. 179-186, 1998.