Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)

Detalhes bibliográficos
Autor(a) principal: Neves,Valdir Augusto
Data de Publicação: 2009
Outros Autores: Picchi,Douglas Gatte, Silva,Maraiza Aparecida da
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132009000400025
Resumo: Polyphenoloxidase (PPO; EC 1.14.18.1) extracted from Mentha arvensis leaves was isolated by (NH4)2SO4 precipitation and extensive dialysis. Its optimum pH and temperature varied with the substrate. The PPO showed activity with various diphenols. Km values were found 0.825, 0.928 and 7.41mM for caffeic acid, 4-methylcatechol and catechol, respectively. On heat-inactivation, half of the activity was lost after 60 and 15 sec at 70 and 75ºC, respectively. Measuring of residual activity showed a stabilizing effect of sucrose at various temperatures with activation energy (Ea) for inactivation increasing with sucrose concentration from 0 to 40% (w/w). Ea values of 78.13; 80.37; 82.79 and 81.00 kJ/Mol were found for 0, 15; 30 and 40% sucrose, respectively. PPO was inhibited by ascorbic, benzoic, cinnamic, ferulic, p-coumaric, protocatechuich acids, sodium metabisulfite, pyrogallol and resorcinol. The Ki values showed that ascorbic acid was the most effective inhibitor. The type inhibition was determined for each inhibitor.
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spelling Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)polyphenoloxidaseMentha arvensischaracterizationheat inactivationinhibitorsPolyphenoloxidase (PPO; EC 1.14.18.1) extracted from Mentha arvensis leaves was isolated by (NH4)2SO4 precipitation and extensive dialysis. Its optimum pH and temperature varied with the substrate. The PPO showed activity with various diphenols. Km values were found 0.825, 0.928 and 7.41mM for caffeic acid, 4-methylcatechol and catechol, respectively. On heat-inactivation, half of the activity was lost after 60 and 15 sec at 70 and 75ºC, respectively. Measuring of residual activity showed a stabilizing effect of sucrose at various temperatures with activation energy (Ea) for inactivation increasing with sucrose concentration from 0 to 40% (w/w). Ea values of 78.13; 80.37; 82.79 and 81.00 kJ/Mol were found for 0, 15; 30 and 40% sucrose, respectively. PPO was inhibited by ascorbic, benzoic, cinnamic, ferulic, p-coumaric, protocatechuich acids, sodium metabisulfite, pyrogallol and resorcinol. The Ki values showed that ascorbic acid was the most effective inhibitor. The type inhibition was determined for each inhibitor.Instituto de Tecnologia do Paraná - Tecpar2009-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132009000400025Brazilian Archives of Biology and Technology v.52 n.4 2009reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132009000400025info:eu-repo/semantics/openAccessNeves,Valdir AugustoPicchi,Douglas GatteSilva,Maraiza Aparecida daeng2009-09-10T00:00:00Zoai:scielo:S1516-89132009000400025Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2009-09-10T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
title Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
spellingShingle Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
Neves,Valdir Augusto
polyphenoloxidase
Mentha arvensis
characterization
heat inactivation
inhibitors
title_short Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
title_full Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
title_fullStr Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
title_full_unstemmed Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
title_sort Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
author Neves,Valdir Augusto
author_facet Neves,Valdir Augusto
Picchi,Douglas Gatte
Silva,Maraiza Aparecida da
author_role author
author2 Picchi,Douglas Gatte
Silva,Maraiza Aparecida da
author2_role author
author
dc.contributor.author.fl_str_mv Neves,Valdir Augusto
Picchi,Douglas Gatte
Silva,Maraiza Aparecida da
dc.subject.por.fl_str_mv polyphenoloxidase
Mentha arvensis
characterization
heat inactivation
inhibitors
topic polyphenoloxidase
Mentha arvensis
characterization
heat inactivation
inhibitors
description Polyphenoloxidase (PPO; EC 1.14.18.1) extracted from Mentha arvensis leaves was isolated by (NH4)2SO4 precipitation and extensive dialysis. Its optimum pH and temperature varied with the substrate. The PPO showed activity with various diphenols. Km values were found 0.825, 0.928 and 7.41mM for caffeic acid, 4-methylcatechol and catechol, respectively. On heat-inactivation, half of the activity was lost after 60 and 15 sec at 70 and 75ºC, respectively. Measuring of residual activity showed a stabilizing effect of sucrose at various temperatures with activation energy (Ea) for inactivation increasing with sucrose concentration from 0 to 40% (w/w). Ea values of 78.13; 80.37; 82.79 and 81.00 kJ/Mol were found for 0, 15; 30 and 40% sucrose, respectively. PPO was inhibited by ascorbic, benzoic, cinnamic, ferulic, p-coumaric, protocatechuich acids, sodium metabisulfite, pyrogallol and resorcinol. The Ki values showed that ascorbic acid was the most effective inhibitor. The type inhibition was determined for each inhibitor.
publishDate 2009
dc.date.none.fl_str_mv 2009-08-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132009000400025
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132009000400025
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-89132009000400025
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.52 n.4 2009
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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