Data/hora: 10/06/2024 14:11:51

Provedor de dados: | 52
País: | Brazil
Título: | Peroxidase from peach fruit: thermal Stability
Autores: | Neves,Valdir Augusto; Lourenço,E. J.
Data: | 1998-01-01
Ano: | 1998
Palavras-chave: | Peach peroxidase; Purification; Heat stability; Regeneration.
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 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&gt;lactose&gt;glucose&gt;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 70ºC and 75ºC the enzyme was able to be reactivated by up to 40% of the initial activity when stored at 30ºC.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131998000200002
Editor: | Instituto de Tecnologia do Paraná - Tecpar
Relação: | 10.1590/S1516-89131998000200002
Formato: | text/html
Fonte: | Brazilian Archives of Biology and Technology  v.41 n.2 1998
Fonte: | info:eu-repo/semantics/openAccess