Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)

Autores
Goyeneche, Rosario; Di Scala, Karina Cecilia; Roura, Sara Ines
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Polyphenoloxidase (PPO) is the target for the development of several food antibrowning agents. Different substrates (pyrocatechol, gallic acid, chlorogenic acid, caffeic acid, 3,4 dihydroxybenzoic acid, p-cumaric acid, l-tyrosine, pyrogallic acid and phloroglucinol) were analyzed to determine their affinities with radish PPO. Pyrocatechol, gallic acid and pyrogallic acid were the substrates that showed high affinity based on Vmax/Km ratio. The optimum pH for the PPO using these three substrates were pH = 7 and the optimum temperatures were 20, 60 and 20–40 °C for pyrogallic acid, gallic acid and pyrocatechol, respectively. The kinetics of thermal inactivation was successfully modeled by a biphasic model (r2 > 0.888), attributed to the presence of two enzyme fractions, a heat-labile easily inactivated even at low blanching temperatures, and a heat-resistant fraction that requires blanching temperatures above 80 °C to reach 70% of inactivation. The kinetics constants of this model for both heat-labile and heat-resistant increased with temperature in the range from 60 to 90 °C. The activation energy ratio of resistant to labile fraction was found to be 6 (EaL = 142 kJ/mol).
Fil: Goyeneche, Rosario. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Agencia Nacional de Promoción Científica y Tecnológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Di Scala, Karina Cecilia. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Roura, Sara Ines. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Enzymatic Kinetics
Thermal Stability
Minimally Processing
Polyphenoloxidase
Radish
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/25322
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/25322
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)Goyeneche, RosarioDi Scala, Karina CeciliaRoura, Sara InesEnzymatic KineticsThermal StabilityMinimally ProcessingPolyphenoloxidaseRadishhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Polyphenoloxidase (PPO) is the target for the development of several food antibrowning agents. Different substrates (pyrocatechol, gallic acid, chlorogenic acid, caffeic acid, 3,4 dihydroxybenzoic acid, p-cumaric acid, l-tyrosine, pyrogallic acid and phloroglucinol) were analyzed to determine their affinities with radish PPO. Pyrocatechol, gallic acid and pyrogallic acid were the substrates that showed high affinity based on Vmax/Km ratio. The optimum pH for the PPO using these three substrates were pH = 7 and the optimum temperatures were 20, 60 and 20–40 °C for pyrogallic acid, gallic acid and pyrocatechol, respectively. The kinetics of thermal inactivation was successfully modeled by a biphasic model (r2 > 0.888), attributed to the presence of two enzyme fractions, a heat-labile easily inactivated even at low blanching temperatures, and a heat-resistant fraction that requires blanching temperatures above 80 °C to reach 70% of inactivation. The kinetics constants of this model for both heat-labile and heat-resistant increased with temperature in the range from 60 to 90 °C. The activation energy ratio of resistant to labile fraction was found to be 6 (EaL = 142 kJ/mol).Fil: Goyeneche, Rosario. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Agencia Nacional de Promoción Científica y Tecnológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Di Scala, Karina Cecilia. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Roura, Sara Ines. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Science2013-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/25322Goyeneche, Rosario; Di Scala, Karina Cecilia; Roura, Sara Ines; Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus); Elsevier Science; LWT - Food Science and Technology; 54; 1; 4-2013; 57-620023-6438CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0023643813001436info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2013.04.014info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:20:41Zoai:ri.conicet.gov.ar:11336/25322instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:20:41.744CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
title Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
spellingShingle Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
Goyeneche, Rosario
Enzymatic Kinetics
Thermal Stability
Minimally Processing
Polyphenoloxidase
Radish
title_short Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
title_full Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
title_fullStr Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
title_full_unstemmed Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
title_sort Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
dc.creator.none.fl_str_mv Goyeneche, Rosario
Di Scala, Karina Cecilia
Roura, Sara Ines
author Goyeneche, Rosario
author_facet Goyeneche, Rosario
Di Scala, Karina Cecilia
Roura, Sara Ines
author_role author
author2 Di Scala, Karina Cecilia
Roura, Sara Ines
author2_role author
author
dc.subject.none.fl_str_mv Enzymatic Kinetics
Thermal Stability
Minimally Processing
Polyphenoloxidase
Radish
topic Enzymatic Kinetics
Thermal Stability
Minimally Processing
Polyphenoloxidase
Radish
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Polyphenoloxidase (PPO) is the target for the development of several food antibrowning agents. Different substrates (pyrocatechol, gallic acid, chlorogenic acid, caffeic acid, 3,4 dihydroxybenzoic acid, p-cumaric acid, l-tyrosine, pyrogallic acid and phloroglucinol) were analyzed to determine their affinities with radish PPO. Pyrocatechol, gallic acid and pyrogallic acid were the substrates that showed high affinity based on Vmax/Km ratio. The optimum pH for the PPO using these three substrates were pH = 7 and the optimum temperatures were 20, 60 and 20–40 °C for pyrogallic acid, gallic acid and pyrocatechol, respectively. The kinetics of thermal inactivation was successfully modeled by a biphasic model (r2 > 0.888), attributed to the presence of two enzyme fractions, a heat-labile easily inactivated even at low blanching temperatures, and a heat-resistant fraction that requires blanching temperatures above 80 °C to reach 70% of inactivation. The kinetics constants of this model for both heat-labile and heat-resistant increased with temperature in the range from 60 to 90 °C. The activation energy ratio of resistant to labile fraction was found to be 6 (EaL = 142 kJ/mol).
Fil: Goyeneche, Rosario. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Agencia Nacional de Promoción Científica y Tecnológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Di Scala, Karina Cecilia. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Roura, Sara Ines. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química. Grupo de Inv En Ingeniería En Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Polyphenoloxidase (PPO) is the target for the development of several food antibrowning agents. Different substrates (pyrocatechol, gallic acid, chlorogenic acid, caffeic acid, 3,4 dihydroxybenzoic acid, p-cumaric acid, l-tyrosine, pyrogallic acid and phloroglucinol) were analyzed to determine their affinities with radish PPO. Pyrocatechol, gallic acid and pyrogallic acid were the substrates that showed high affinity based on Vmax/Km ratio. The optimum pH for the PPO using these three substrates were pH = 7 and the optimum temperatures were 20, 60 and 20–40 °C for pyrogallic acid, gallic acid and pyrocatechol, respectively. The kinetics of thermal inactivation was successfully modeled by a biphasic model (r2 > 0.888), attributed to the presence of two enzyme fractions, a heat-labile easily inactivated even at low blanching temperatures, and a heat-resistant fraction that requires blanching temperatures above 80 °C to reach 70% of inactivation. The kinetics constants of this model for both heat-labile and heat-resistant increased with temperature in the range from 60 to 90 °C. The activation energy ratio of resistant to labile fraction was found to be 6 (EaL = 142 kJ/mol).
publishDate 2013
dc.date.none.fl_str_mv 2013-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/25322
Goyeneche, Rosario; Di Scala, Karina Cecilia; Roura, Sara Ines; Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus); Elsevier Science; LWT - Food Science and Technology; 54; 1; 4-2013; 57-62
0023-6438
CONICET Digital
CONICET
url http://hdl.handle.net/11336/25322
identifier_str_mv Goyeneche, Rosario; Di Scala, Karina Cecilia; Roura, Sara Ines; Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus); Elsevier Science; LWT - Food Science and Technology; 54; 1; 4-2013; 57-62
0023-6438
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0023643813001436
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2013.04.014
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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