Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)
Autor(a) principal: | |
---|---|
Data de Publicação: | 2009 |
Outros Autores: | , |
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. |
id |
TECPAR-1_a0cfb71cf37cb84a6ff7f17d4ae1df76 |
---|---|
oai_identifier_str |
oai:scielo:S1516-89132009000400025 |
network_acronym_str |
TECPAR-1 |
network_name_str |
Brazilian Archives of Biology and Technology |
repository_id_str |
|
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 |
_version_ |
1750318273159757824 |