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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/36856
Title: 
Peroxidase from peach fruit: Thermal stability
Author(s): 
Institution: 
Universidade Estadual Paulista (UNESP)
ISSN: 
0365-0979
Abstract: 
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.
Issue Date: 
1-Jan-1998
Citation: 
Brazilian Archives of Biology and Technology. Curitiba-Paraná: Inst Tecnologia Parana, v. 41, n. 2, p. 179-186, 1998.
Time Duration: 
179-186
Publisher: 
Inst Tecnologia Parana
Keywords: 
  • peach peroxidase
  • purification
  • heat stability
  • regeneration
Source: 
http://dx.doi.org/10.1590/S1516-89131998000200002
URI: 
Access Rights: 
Acesso aberto
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/36856
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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