Peroxidase (POD) and polyphenoloxidase (PPO) in grape (Vitis vinifera L.)
Autor(a) principal: | |
---|---|
Data de Publicação: | 2003 |
Outros Autores: | , |
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. |
id |
UFLA_6343adcd26ea7bdeb91fec179bb965b7 |
---|---|
oai_identifier_str |
oai:localhost:1/5719 |
network_acronym_str |
UFLA |
network_name_str |
Repositório Institucional da UFLA |
repository_id_str |
|
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 |
_version_ |
1815439070114873344 |