Peroxidase from peach fruit: Thermal stability

Detalhes bibliográficos
Autor(a) principal: Neves, V. A.
Data de Publicação: 1998
Outros Autores: Lourenco, E. J.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1590/S1516-89131998000200002
http://hdl.handle.net/11449/36856
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.
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spelling Peroxidase from peach fruit: Thermal stabilitypeach peroxidasepurificationheat stabilityregenerationPeroxidase 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.UNESP, Univ Paulista Julio de Mesquita Filho, Fac Pharmaceut Sci, Dept Food Nutr, São Paulo, BrazilUNESP, Univ Paulista Julio de Mesquita Filho, Fac Pharmaceut Sci, Dept Food Nutr, São Paulo, BrazilInst Tecnologia ParanaUniversidade Estadual Paulista (Unesp)Neves, V. A.Lourenco, E. J.2014-05-20T15:26:46Z2014-05-20T15:26:46Z1998-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article179-186application/pdfhttp://dx.doi.org/10.1590/S1516-89131998000200002Brazilian Archives of Biology and Technology. Curitiba-Paraná: Inst Tecnologia Parana, v. 41, n. 2, p. 179-186, 1998.0365-0979http://hdl.handle.net/11449/3685610.1590/S1516-89131998000200002S1516-89131998000200002WOS:000165534400002WOS000165534400002.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBrazilian Archives of Biology and Technologyinfo:eu-repo/semantics/openAccess2023-11-01T06:09:14Zoai:repositorio.unesp.br:11449/36856Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:35:30.524534Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Peroxidase from peach fruit: Thermal stability
title Peroxidase from peach fruit: Thermal stability
spellingShingle Peroxidase from peach fruit: Thermal stability
Neves, V. A.
peach peroxidase
purification
heat stability
regeneration
title_short Peroxidase from peach fruit: Thermal stability
title_full Peroxidase from peach fruit: Thermal stability
title_fullStr Peroxidase from peach fruit: Thermal stability
title_full_unstemmed Peroxidase from peach fruit: Thermal stability
title_sort Peroxidase from peach fruit: Thermal stability
author Neves, V. A.
author_facet Neves, V. A.
Lourenco, E. J.
author_role author
author2 Lourenco, E. J.
author2_role author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Neves, V. A.
Lourenco, E. J.
dc.subject.por.fl_str_mv peach peroxidase
purification
heat stability
regeneration
topic peach peroxidase
purification
heat stability
regeneration
description 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.
publishDate 1998
dc.date.none.fl_str_mv 1998-01-01
2014-05-20T15:26:46Z
2014-05-20T15:26:46Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1590/S1516-89131998000200002
Brazilian Archives of Biology and Technology. Curitiba-Paraná: Inst Tecnologia Parana, v. 41, n. 2, p. 179-186, 1998.
0365-0979
http://hdl.handle.net/11449/36856
10.1590/S1516-89131998000200002
S1516-89131998000200002
WOS:000165534400002
WOS000165534400002.pdf
url http://dx.doi.org/10.1590/S1516-89131998000200002
http://hdl.handle.net/11449/36856
identifier_str_mv Brazilian Archives of Biology and Technology. Curitiba-Paraná: Inst Tecnologia Parana, v. 41, n. 2, p. 179-186, 1998.
0365-0979
10.1590/S1516-89131998000200002
S1516-89131998000200002
WOS:000165534400002
WOS000165534400002.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Brazilian Archives of Biology and Technology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 179-186
application/pdf
dc.publisher.none.fl_str_mv Inst Tecnologia Parana
publisher.none.fl_str_mv Inst Tecnologia Parana
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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