Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)

Detalhes bibliográficos
Autor(a) principal: Troiani, Estela de Pieri
Data de Publicação: 2003
Outros Autores: Tropiani, Clariza Tomé, Clemente, Edmar
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFLA
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542003000300019
http://repositorio.ufla.br/jspui/handle/1/5719
Resumo: The enzimatic activity of peroxidase (POD) and polyphenoloxidase (PPO) extracted from three grape cultivars (Vitis vinifera L.), cultivated in Marialva city, state of Paraná, was evaluated in this study. The enzymatic extracts were prepared starting from the Rubi, Borbon and Benitaka grape cultivars pulp and peel. The activity of the peroxidase was 53.00 units/100 g in the extract from the Rubi cultivar peel, and 327.00 units/100 g from the Benitaka cultivar, these values being superior to those observed in the same cultivars pulp extracts, which were 7.67 units/100 g and 44.00 units/100 g respectively. However, the result was opposite in the Borbon cultivar, with values of 141.11 units/100 g in the pulp and 11.50 units/100 g in the peel being found. The results of the polyphenoloxidase in the Borbon cultivar activity were 100.18 units/100 g in the pulp and 102.60 units/100 g in the peel, and in the Rubi and Benitaka cultivars were 60.40 units/100 g, 48.62 units/100 g in the pulp and 17.40 units/100 g, and 26.20 units/100 g in the peel, respectively. Protein determination was carried out in each extract, and the results found in the pulp and peel, respectively, were 0.56 and 0.64 mg/100 g for cultivar Benitaka, 1.38 and 6.45 mg/100 g for cultivar Rubi, and 21.38 and 5.68 mg/100 g for Borbon. The extracts were submitted to thermal treatments (60°C, 65°C, 70°C and 75°C for a 1 to 10 minutes period) to observe the behavior of the peroxidase and polyphenoloxidase enzymatic activity, being verified a continuous decrease of the peroxidase and polyphenoloxidase activities as a result of the thermal treatment. The extracts of the Rubi and Benitaka cultivars were more heat stable than the extract from the Borbon cultivar for both enzymes. However, the temperatures used were not enough for a total inactivation of the enzymes.
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spelling Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)Peroxidase (POD) e polifenoloxidase (PPO) em uva (Vitis vinifera L.)PeroxidasePolyphenoloxidaseGrapeVitis viniferaPeroxidasePolifenoloxidaseUvaThe enzimatic activity of peroxidase (POD) and polyphenoloxidase (PPO) extracted from three grape cultivars (Vitis vinifera L.), cultivated in Marialva city, state of Paraná, was evaluated in this study. The enzymatic extracts were prepared starting from the Rubi, Borbon and Benitaka grape cultivars pulp and peel. The activity of the peroxidase was 53.00 units/100 g in the extract from the Rubi cultivar peel, and 327.00 units/100 g from the Benitaka cultivar, these values being superior to those observed in the same cultivars pulp extracts, which were 7.67 units/100 g and 44.00 units/100 g respectively. However, the result was opposite in the Borbon cultivar, with values of 141.11 units/100 g in the pulp and 11.50 units/100 g in the peel being found. The results of the polyphenoloxidase in the Borbon cultivar activity were 100.18 units/100 g in the pulp and 102.60 units/100 g in the peel, and in the Rubi and Benitaka cultivars were 60.40 units/100 g, 48.62 units/100 g in the pulp and 17.40 units/100 g, and 26.20 units/100 g in the peel, respectively. Protein determination was carried out in each extract, and the results found in the pulp and peel, respectively, were 0.56 and 0.64 mg/100 g for cultivar Benitaka, 1.38 and 6.45 mg/100 g for cultivar Rubi, and 21.38 and 5.68 mg/100 g for Borbon. The extracts were submitted to thermal treatments (60°C, 65°C, 70°C and 75°C for a 1 to 10 minutes period) to observe the behavior of the peroxidase and polyphenoloxidase enzymatic activity, being verified a continuous decrease of the peroxidase and polyphenoloxidase activities as a result of the thermal treatment. The extracts of the Rubi and Benitaka cultivars were more heat stable than the extract from the Borbon cultivar for both enzymes. However, the temperatures used were not enough for a total inactivation of the enzymes.Neste trabalho, estudou-se a atividade enzimática da peroxidase (POD) e da polifenoloxidase (PPO) extraídas de três cultivares de uvas (Vitis vinifera L.) cultivadas em Marialva, PR. Os extratos enzimáticos foram preparados a partir da polpa e da casca das cultivares de uvas Rubi, Borbon e Benitaka. A atividade da peroxidase foi de 53,00 unid./100 g no extrato da casca da cultivar Rubi, e da cultivar Benitaka foi de 327,00 unid./100 g, valores esses superiores aos encontrados nos extratos da polpa das mesmas cultivares, que foram de 7,67 unid./100 g e 44,00 unid/100 g, respectivamente. Porém, na cultivar Borbon, o resultado observado foi inverso, mostrando para o extrato da polpa 141,11 unid./100 g e para o extrato da casca, 11,50 unid./100 g. O resultado da atividade da polifenoloxidase na cultivar Borbon foi de 100,18 unid./100 g; na polpa e na casca, 102,60 unid./100 g, e na cultivar Rubi e Benitaka foram 60,40 unid./100 g, 48,62 unid./100 g na polpa e 17,40 unid./100 g, 26,20 unid./100 g na casca, respectivamente. Determinação de proteína foi feita para cada extrato, e os resultados apresentados para as cultivares foram para Benitaka 0,56 e 0,64 mg/100 g, Rubi 1,38 e 6,45 mg/100 g e Borbon 21,38 e 5,68 mg/100 g, respectivamente. Os extratos foram submetidos a tratamentos térmicos (60°C, 65°C, 70°C e 75°C para um período de 1 a 10 minutos), observando o comportamento da atividade enzimática da peroxidase e polifenoloxidase, sendo verificada uma diminuição contínua das atividades de peroxidase e de polifenoloxidase diante do tratamento térmico. Os extratos da cultivar Rubi e Benitaka foram mais termoestáveis que o extrato do cultivar Borbon para ambas as enzimas. Porém, as temperaturas usadas não foram suficientes para inativação total das enzimas.Editora da Universidade Federal de Lavras2003-06-012015-04-30T13:32:43Z2015-04-30T13:32:43Z2015-04-30info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articletext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542003000300019TROIANI, E. de P.; TROPIANI, C. T.; CLEMENTE, E. Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.). Ciência e Agrotecnologia, Lavras, v. 27, n. 3, p. 635-642, maio/jun. 2003.http://repositorio.ufla.br/jspui/handle/1/5719Ciência e Agrotecnologia v.27 n.3 2003reponame:Repositório Institucional da UFLAinstname:Universidade Federal de Lavras (UFLA)instacron:UFLATroiani, Estela de PieriTropiani, Clariza ToméClemente, Edmarenginfo:eu-repo/semantics/openAccess2016-08-02T11:36:06Zoai:localhost:1/5719Repositório InstitucionalPUBhttp://repositorio.ufla.br/oai/requestnivaldo@ufla.br || repositorio.biblioteca@ufla.bropendoar:2016-08-02T11:36:06Repositório Institucional da UFLA - Universidade Federal de Lavras (UFLA)false
dc.title.none.fl_str_mv Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
Peroxidase (POD) e polifenoloxidase (PPO) em uva (Vitis vinifera L.)
title Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
spellingShingle Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
Troiani, Estela de Pieri
Peroxidase
Polyphenoloxidase
Grape
Vitis vinifera
Peroxidase
Polifenoloxidase
Uva
title_short Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
title_full Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
title_fullStr Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
title_full_unstemmed Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
title_sort Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
author Troiani, Estela de Pieri
author_facet Troiani, Estela de Pieri
Tropiani, Clariza Tomé
Clemente, Edmar
author_role author
author2 Tropiani, Clariza Tomé
Clemente, Edmar
author2_role author
author
dc.contributor.author.fl_str_mv Troiani, Estela de Pieri
Tropiani, Clariza Tomé
Clemente, Edmar
dc.subject.por.fl_str_mv Peroxidase
Polyphenoloxidase
Grape
Vitis vinifera
Peroxidase
Polifenoloxidase
Uva
topic Peroxidase
Polyphenoloxidase
Grape
Vitis vinifera
Peroxidase
Polifenoloxidase
Uva
description The enzimatic activity of peroxidase (POD) and polyphenoloxidase (PPO) extracted from three grape cultivars (Vitis vinifera L.), cultivated in Marialva city, state of Paraná, was evaluated in this study. The enzymatic extracts were prepared starting from the Rubi, Borbon and Benitaka grape cultivars pulp and peel. The activity of the peroxidase was 53.00 units/100 g in the extract from the Rubi cultivar peel, and 327.00 units/100 g from the Benitaka cultivar, these values being superior to those observed in the same cultivars pulp extracts, which were 7.67 units/100 g and 44.00 units/100 g respectively. However, the result was opposite in the Borbon cultivar, with values of 141.11 units/100 g in the pulp and 11.50 units/100 g in the peel being found. The results of the polyphenoloxidase in the Borbon cultivar activity were 100.18 units/100 g in the pulp and 102.60 units/100 g in the peel, and in the Rubi and Benitaka cultivars were 60.40 units/100 g, 48.62 units/100 g in the pulp and 17.40 units/100 g, and 26.20 units/100 g in the peel, respectively. Protein determination was carried out in each extract, and the results found in the pulp and peel, respectively, were 0.56 and 0.64 mg/100 g for cultivar Benitaka, 1.38 and 6.45 mg/100 g for cultivar Rubi, and 21.38 and 5.68 mg/100 g for Borbon. The extracts were submitted to thermal treatments (60°C, 65°C, 70°C and 75°C for a 1 to 10 minutes period) to observe the behavior of the peroxidase and polyphenoloxidase enzymatic activity, being verified a continuous decrease of the peroxidase and polyphenoloxidase activities as a result of the thermal treatment. The extracts of the Rubi and Benitaka cultivars were more heat stable than the extract from the Borbon cultivar for both enzymes. However, the temperatures used were not enough for a total inactivation of the enzymes.
publishDate 2003
dc.date.none.fl_str_mv 2003-06-01
2015-04-30T13:32:43Z
2015-04-30T13:32:43Z
2015-04-30
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://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542003000300019
TROIANI, E. de P.; TROPIANI, C. T.; CLEMENTE, E. Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.). Ciência e Agrotecnologia, Lavras, v. 27, n. 3, p. 635-642, maio/jun. 2003.
http://repositorio.ufla.br/jspui/handle/1/5719
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542003000300019
http://repositorio.ufla.br/jspui/handle/1/5719
identifier_str_mv TROIANI, E. de P.; TROPIANI, C. T.; CLEMENTE, E. Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.). Ciência e Agrotecnologia, Lavras, v. 27, n. 3, p. 635-642, maio/jun. 2003.
dc.language.iso.fl_str_mv eng
language eng
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 Editora da Universidade Federal de Lavras
publisher.none.fl_str_mv Editora da Universidade Federal de Lavras
dc.source.none.fl_str_mv Ciência e Agrotecnologia v.27 n.3 2003
reponame:Repositório Institucional da UFLA
instname:Universidade Federal de Lavras (UFLA)
instacron:UFLA
instname_str Universidade Federal de Lavras (UFLA)
instacron_str UFLA
institution UFLA
reponame_str Repositório Institucional da UFLA
collection Repositório Institucional da UFLA
repository.name.fl_str_mv Repositório Institucional da UFLA - Universidade Federal de Lavras (UFLA)
repository.mail.fl_str_mv nivaldo@ufla.br || repositorio.biblioteca@ufla.br
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