Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale)
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2006 |
| Outros Autores: | , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
| Texto Completo: | http://hdl.handle.net/10400.14/2854 |
Resumo: | The effect of heat and the combined heat/ultrasound (thermosonication) treatment on the inactivation kinetics of peroxidase in watercress (Nasturtium officinale) was studied in the temperature range of 40-92.5 degrees C. In the heat blanching processes, the enzyme kinetics showed a first-order biphasic inactivation model. The activation energies and the rates of the reaction at a reference temperature for both the heat-labile and heat-resistant fractions were, respectively, E-a1 = 421 +/- 115 kJmol(-1) and E-a2 = 352 +/- 81 kJmol(-1), k(184.6 degrees C) = 18 +/- 14min(-1) and k(284.6 degrees C) = 0.24 +/- 0.14min(-1). The initial relative specific activity for both isoenzyme fractions were also estimated, being C-01 = 0.5 +/- 0.08 mu mol min(-1)mg protein(-1) and C-02 = 0.5 +/- 0.06 mu mol min(-1)mg protein(-1), respectively. The application of thermosonication was studied to enable less severe thermal treatments and, therefore, improving the quality of the blanched product. In this treatment the enzyme kinetics showed a first-order model. The activation energy, the rate of reaction at a reference temperature and the initial relative specific activity were, respectively, E-a3 = 496 +/- 65 kJmol(-1), k(387.5 degrees C) = 10 +/- 2min(-1) and C-03 = 1 +/- 0.05 mu mol min(-1)mg protein(-1), proving that the enzyme became more heat labile. The present findings will help to design the blanching conditions for the production of a new and healthy frozen product, watercress (Nasturtium officinale), with minimized colour or flavour changes along its shelf life. |
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Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale)Watercress (Nasturtium officinale)HeatUltrasoundInactivationPeroxidaseKineticsModellingThe effect of heat and the combined heat/ultrasound (thermosonication) treatment on the inactivation kinetics of peroxidase in watercress (Nasturtium officinale) was studied in the temperature range of 40-92.5 degrees C. In the heat blanching processes, the enzyme kinetics showed a first-order biphasic inactivation model. The activation energies and the rates of the reaction at a reference temperature for both the heat-labile and heat-resistant fractions were, respectively, E-a1 = 421 +/- 115 kJmol(-1) and E-a2 = 352 +/- 81 kJmol(-1), k(184.6 degrees C) = 18 +/- 14min(-1) and k(284.6 degrees C) = 0.24 +/- 0.14min(-1). The initial relative specific activity for both isoenzyme fractions were also estimated, being C-01 = 0.5 +/- 0.08 mu mol min(-1)mg protein(-1) and C-02 = 0.5 +/- 0.06 mu mol min(-1)mg protein(-1), respectively. The application of thermosonication was studied to enable less severe thermal treatments and, therefore, improving the quality of the blanched product. In this treatment the enzyme kinetics showed a first-order model. The activation energy, the rate of reaction at a reference temperature and the initial relative specific activity were, respectively, E-a3 = 496 +/- 65 kJmol(-1), k(387.5 degrees C) = 10 +/- 2min(-1) and C-03 = 1 +/- 0.05 mu mol min(-1)mg protein(-1), proving that the enzyme became more heat labile. The present findings will help to design the blanching conditions for the production of a new and healthy frozen product, watercress (Nasturtium officinale), with minimized colour or flavour changes along its shelf life.ElsevierVeritatiCruz, Rui M. S.Vieira, Margarida C.Silva, Cristina L. M.2010-10-11T22:29:42Z20062006-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/2854eng0260-877410.1016/j.jfoodeng.2004.11.007info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2025-03-13T11:41:31Zoai:repositorio.ucp.pt:10400.14/2854Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-29T01:43:48.003816Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse |
| dc.title.none.fl_str_mv |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) |
| title |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) |
| spellingShingle |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) Cruz, Rui M. S. Watercress (Nasturtium officinale) Heat Ultrasound Inactivation Peroxidase Kinetics Modelling |
| title_short |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) |
| title_full |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) |
| title_fullStr |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) |
| title_full_unstemmed |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) |
| title_sort |
Effect of heat and thermosonication treatments on peroxidise inactivation kinetics in watercress (nasturtium officinale) |
| author |
Cruz, Rui M. S. |
| author_facet |
Cruz, Rui M. S. Vieira, Margarida C. Silva, Cristina L. M. |
| author_role |
author |
| author2 |
Vieira, Margarida C. Silva, Cristina L. M. |
| author2_role |
author author |
| dc.contributor.none.fl_str_mv |
Veritati |
| dc.contributor.author.fl_str_mv |
Cruz, Rui M. S. Vieira, Margarida C. Silva, Cristina L. M. |
| dc.subject.por.fl_str_mv |
Watercress (Nasturtium officinale) Heat Ultrasound Inactivation Peroxidase Kinetics Modelling |
| topic |
Watercress (Nasturtium officinale) Heat Ultrasound Inactivation Peroxidase Kinetics Modelling |
| description |
The effect of heat and the combined heat/ultrasound (thermosonication) treatment on the inactivation kinetics of peroxidase in watercress (Nasturtium officinale) was studied in the temperature range of 40-92.5 degrees C. In the heat blanching processes, the enzyme kinetics showed a first-order biphasic inactivation model. The activation energies and the rates of the reaction at a reference temperature for both the heat-labile and heat-resistant fractions were, respectively, E-a1 = 421 +/- 115 kJmol(-1) and E-a2 = 352 +/- 81 kJmol(-1), k(184.6 degrees C) = 18 +/- 14min(-1) and k(284.6 degrees C) = 0.24 +/- 0.14min(-1). The initial relative specific activity for both isoenzyme fractions were also estimated, being C-01 = 0.5 +/- 0.08 mu mol min(-1)mg protein(-1) and C-02 = 0.5 +/- 0.06 mu mol min(-1)mg protein(-1), respectively. The application of thermosonication was studied to enable less severe thermal treatments and, therefore, improving the quality of the blanched product. In this treatment the enzyme kinetics showed a first-order model. The activation energy, the rate of reaction at a reference temperature and the initial relative specific activity were, respectively, E-a3 = 496 +/- 65 kJmol(-1), k(387.5 degrees C) = 10 +/- 2min(-1) and C-03 = 1 +/- 0.05 mu mol min(-1)mg protein(-1), proving that the enzyme became more heat labile. The present findings will help to design the blanching conditions for the production of a new and healthy frozen product, watercress (Nasturtium officinale), with minimized colour or flavour changes along its shelf life. |
| publishDate |
2006 |
| dc.date.none.fl_str_mv |
2006 2006-01-01T00:00:00Z 2010-10-11T22:29:42Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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article |
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publishedVersion |
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http://hdl.handle.net/10400.14/2854 |
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eng |
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eng |
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0260-8774 10.1016/j.jfoodeng.2004.11.007 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
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Elsevier |
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Elsevier |
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