Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)

Polyphenol oxidase (PPO) and peroxidase (POD) were extracted from a table grape (Crimson Seedless) using Triton X-114 and characterized using spectrophotometric methods. Both PPO and POD were activated by acid shock. However, in the presence of the anionic detergent sodium dodecil sulphate (SDS), PP...

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Autores: Carreño, Juan, López Miranda, Santiago, Serrano Martínez, Ana Agustina, Núñez Delicado, Estrella, Fortea Gorbe, María Isabel
Tipo de recurso: artículo
Fecha de publicación:2009
País:España
Institución:Universidad Católica San Antonio de Murcia (UCAM)
Repositorio:RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
OAI Identifier:oai:repositorio.ucam.edu:10952/2381
Acceso en línea:http://hdl.handle.net/10952/2381
Access Level:acceso abierto
Palabra clave:Polyphenol oxidase
Peroxidase Grape
Thermal inactivation SDS
Crimson Seedless
Kinetic parameters
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spelling Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)Carreño, JuanLópez Miranda, SantiagoSerrano Martínez, Ana AgustinaNúñez Delicado, EstrellaFortea Gorbe, María IsabelPolyphenol oxidasePeroxidase GrapeThermal inactivation SDSCrimson SeedlessKinetic parametersPolyphenol oxidase (PPO) and peroxidase (POD) were extracted from a table grape (Crimson Seedless) using Triton X-114 and characterized using spectrophotometric methods. Both PPO and POD were activated by acid shock. However, in the presence of the anionic detergent sodium dodecil sulphate (SDS), PPO was activated whereas POD was inactivated. The enzymes were kinetically characterized and both followed Michaelis–Menten kinetics, although with different values of their kinetic parameters. The Vm/Km ratio showed that Crimson Seedless grape PPO presents a similar affinity for 4-tert-butyl-catechol (TBC) whether activated by acid shock (0.018 min1 ) or SDS (0.023 min1 ). With regards to POD, the Km and Vm values for 2,20 -azinobis(3-ethylbenzothiazolinesulphonic acid) (ABTS) were 0.79 mM and 1.20 lM/min, respectively. In the case of H2O2, the Km and Vm value were 0.4 mM and 0.93 lM/min, respectively. PPO and POD showed similar thermostability, losing >90% of relative activity after only 5 min of incubation at 78 C and 75 C, respectively. In addition, PPO´ s activation energy was similar to that obtained for POD (295.5 kJ/mol and 271.9 kJ/mol, respectively).Ciencias de la AlimentaciónElsevier Ltd2009info:eu-repo/semantics/articlehttp://hdl.handle.net/10952/2381reponame:RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murciainstname:Universidad Católica San Antonio de Murcia (UCAM)Inglésinfo:eu-repo/semantics/openAccessoai:repositorio.ucam.edu:10952/23812026-06-07T18:35:21Z
dc.title.none.fl_str_mv Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
title Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
spellingShingle Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
Carreño, Juan
Polyphenol oxidase
Peroxidase Grape
Thermal inactivation SDS
Crimson Seedless
Kinetic parameters
title_short Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
title_full Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
title_fullStr Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
title_full_unstemmed Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
title_sort Kinetic characterisation and thermal inactivation study of polyphenol oxidase and peroxidase from table grape (Crimson Seedless)
dc.creator.none.fl_str_mv Carreño, Juan
López Miranda, Santiago
Serrano Martínez, Ana Agustina
Núñez Delicado, Estrella
Fortea Gorbe, María Isabel
author Carreño, Juan
author_facet Carreño, Juan
López Miranda, Santiago
Serrano Martínez, Ana Agustina
Núñez Delicado, Estrella
Fortea Gorbe, María Isabel
author_role author
author2 López Miranda, Santiago
Serrano Martínez, Ana Agustina
Núñez Delicado, Estrella
Fortea Gorbe, María Isabel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Polyphenol oxidase
Peroxidase Grape
Thermal inactivation SDS
Crimson Seedless
Kinetic parameters
topic Polyphenol oxidase
Peroxidase Grape
Thermal inactivation SDS
Crimson Seedless
Kinetic parameters
description Polyphenol oxidase (PPO) and peroxidase (POD) were extracted from a table grape (Crimson Seedless) using Triton X-114 and characterized using spectrophotometric methods. Both PPO and POD were activated by acid shock. However, in the presence of the anionic detergent sodium dodecil sulphate (SDS), PPO was activated whereas POD was inactivated. The enzymes were kinetically characterized and both followed Michaelis–Menten kinetics, although with different values of their kinetic parameters. The Vm/Km ratio showed that Crimson Seedless grape PPO presents a similar affinity for 4-tert-butyl-catechol (TBC) whether activated by acid shock (0.018 min1 ) or SDS (0.023 min1 ). With regards to POD, the Km and Vm values for 2,20 -azinobis(3-ethylbenzothiazolinesulphonic acid) (ABTS) were 0.79 mM and 1.20 lM/min, respectively. In the case of H2O2, the Km and Vm value were 0.4 mM and 0.93 lM/min, respectively. PPO and POD showed similar thermostability, losing >90% of relative activity after only 5 min of incubation at 78 C and 75 C, respectively. In addition, PPO´ s activation energy was similar to that obtained for POD (295.5 kJ/mol and 271.9 kJ/mol, respectively).
publishDate 2009
dc.date.none.fl_str_mv 2009
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10952/2381
url http://hdl.handle.net/10952/2381
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier Ltd
publisher.none.fl_str_mv Elsevier Ltd
dc.source.none.fl_str_mv reponame:RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
instname:Universidad Católica San Antonio de Murcia (UCAM)
instname_str Universidad Católica San Antonio de Murcia (UCAM)
reponame_str RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
collection RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.301603

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