β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness

Autores
Bustamante, Claudia Anabel; Rosli, Hernan Guillermo; Añon, Maria Cristina; Civello, Pedro Marcos; Martinez, Gustavo Adolfo
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Strawberry is a non-climateric fleshy fruit, which softens quickly and has short post-harvest life. Ripening is associated with an increment of pectin solubility and a reduction of the content of hemicelluloses. In this work, we have cloned the full-length cDNA encoding a β-xylosidase (FaXyl1) from Fragaria × ananassa and we have characterized its expression in two strawberry cultivars with contrasting fruit firmness. The analysis of the predicted protein showed that FaXyl1 is closely related to other β-xylosidases from higher plants. The recombinant protein obtained by over-expressing FaXyl1 in Escherichia coli had β-xylosidase activity against the artificial substrate p-nitrophenyl β-d-xilopyranoside. Differently from other bifunctional xylosidases, no α-l-arabinofuranosidase activity was detected in the recombinant enzyme. The expression of FaXyl1 gene was analyzed by northern-blot in Camarosa and Toyonaka strawberry cultivars, and compared with the corresponding protein data obtained by Western-blot and with the β-xylosidase activity during ripening. The softest cultivar (Toyonaka) showed an early accumulation of FaXyl1 transcript and a higher expression of the corresponding protein during ripening, which correlates with a higher β-xylosidase activity in all ripening stages analyzed. © 2006 Elsevier Ireland Ltd. All rights reserved.
Fil: Bustamante, Claudia Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Rosli, Hernan Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Civello, Pedro Marcos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Martinez, Gustavo Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Materia
CELL WALL
FRAGARIA
RIPENING
SOFTENING
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/152059
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/152059
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network_name_str CONICET Digital (CONICET)
spelling β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmnessBustamante, Claudia AnabelRosli, Hernan GuillermoAñon, Maria CristinaCivello, Pedro MarcosMartinez, Gustavo AdolfoCELL WALLFRAGARIARIPENINGSOFTENINGhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Strawberry is a non-climateric fleshy fruit, which softens quickly and has short post-harvest life. Ripening is associated with an increment of pectin solubility and a reduction of the content of hemicelluloses. In this work, we have cloned the full-length cDNA encoding a β-xylosidase (FaXyl1) from Fragaria × ananassa and we have characterized its expression in two strawberry cultivars with contrasting fruit firmness. The analysis of the predicted protein showed that FaXyl1 is closely related to other β-xylosidases from higher plants. The recombinant protein obtained by over-expressing FaXyl1 in Escherichia coli had β-xylosidase activity against the artificial substrate p-nitrophenyl β-d-xilopyranoside. Differently from other bifunctional xylosidases, no α-l-arabinofuranosidase activity was detected in the recombinant enzyme. The expression of FaXyl1 gene was analyzed by northern-blot in Camarosa and Toyonaka strawberry cultivars, and compared with the corresponding protein data obtained by Western-blot and with the β-xylosidase activity during ripening. The softest cultivar (Toyonaka) showed an early accumulation of FaXyl1 transcript and a higher expression of the corresponding protein during ripening, which correlates with a higher β-xylosidase activity in all ripening stages analyzed. © 2006 Elsevier Ireland Ltd. All rights reserved.Fil: Bustamante, Claudia Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Rosli, Hernan Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Civello, Pedro Marcos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Martinez, Gustavo Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaElsevier Ireland2006-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/152059Bustamante, Claudia Anabel; Rosli, Hernan Guillermo; Añon, Maria Cristina; Civello, Pedro Marcos; Martinez, Gustavo Adolfo; β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness; Elsevier Ireland; Plant Science; 171; 4; 10-2006; 497-5040168-94521873-2259CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.plantsci.2006.05.011info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0168945206001683?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:20:40Zoai:ri.conicet.gov.ar:11336/152059instacron: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:34982025-10-22 11:20:41.025CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
title β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
spellingShingle β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
Bustamante, Claudia Anabel
CELL WALL
FRAGARIA
RIPENING
SOFTENING
title_short β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
title_full β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
title_fullStr β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
title_full_unstemmed β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
title_sort β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness
dc.creator.none.fl_str_mv Bustamante, Claudia Anabel
Rosli, Hernan Guillermo
Añon, Maria Cristina
Civello, Pedro Marcos
Martinez, Gustavo Adolfo
author Bustamante, Claudia Anabel
author_facet Bustamante, Claudia Anabel
Rosli, Hernan Guillermo
Añon, Maria Cristina
Civello, Pedro Marcos
Martinez, Gustavo Adolfo
author_role author
author2 Rosli, Hernan Guillermo
Añon, Maria Cristina
Civello, Pedro Marcos
Martinez, Gustavo Adolfo
author2_role author
author
author
author
dc.subject.none.fl_str_mv CELL WALL
FRAGARIA
RIPENING
SOFTENING
topic CELL WALL
FRAGARIA
RIPENING
SOFTENING
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Strawberry is a non-climateric fleshy fruit, which softens quickly and has short post-harvest life. Ripening is associated with an increment of pectin solubility and a reduction of the content of hemicelluloses. In this work, we have cloned the full-length cDNA encoding a β-xylosidase (FaXyl1) from Fragaria × ananassa and we have characterized its expression in two strawberry cultivars with contrasting fruit firmness. The analysis of the predicted protein showed that FaXyl1 is closely related to other β-xylosidases from higher plants. The recombinant protein obtained by over-expressing FaXyl1 in Escherichia coli had β-xylosidase activity against the artificial substrate p-nitrophenyl β-d-xilopyranoside. Differently from other bifunctional xylosidases, no α-l-arabinofuranosidase activity was detected in the recombinant enzyme. The expression of FaXyl1 gene was analyzed by northern-blot in Camarosa and Toyonaka strawberry cultivars, and compared with the corresponding protein data obtained by Western-blot and with the β-xylosidase activity during ripening. The softest cultivar (Toyonaka) showed an early accumulation of FaXyl1 transcript and a higher expression of the corresponding protein during ripening, which correlates with a higher β-xylosidase activity in all ripening stages analyzed. © 2006 Elsevier Ireland Ltd. All rights reserved.
Fil: Bustamante, Claudia Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Rosli, Hernan Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Civello, Pedro Marcos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Martinez, Gustavo Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
description Strawberry is a non-climateric fleshy fruit, which softens quickly and has short post-harvest life. Ripening is associated with an increment of pectin solubility and a reduction of the content of hemicelluloses. In this work, we have cloned the full-length cDNA encoding a β-xylosidase (FaXyl1) from Fragaria × ananassa and we have characterized its expression in two strawberry cultivars with contrasting fruit firmness. The analysis of the predicted protein showed that FaXyl1 is closely related to other β-xylosidases from higher plants. The recombinant protein obtained by over-expressing FaXyl1 in Escherichia coli had β-xylosidase activity against the artificial substrate p-nitrophenyl β-d-xilopyranoside. Differently from other bifunctional xylosidases, no α-l-arabinofuranosidase activity was detected in the recombinant enzyme. The expression of FaXyl1 gene was analyzed by northern-blot in Camarosa and Toyonaka strawberry cultivars, and compared with the corresponding protein data obtained by Western-blot and with the β-xylosidase activity during ripening. The softest cultivar (Toyonaka) showed an early accumulation of FaXyl1 transcript and a higher expression of the corresponding protein during ripening, which correlates with a higher β-xylosidase activity in all ripening stages analyzed. © 2006 Elsevier Ireland Ltd. All rights reserved.
publishDate 2006
dc.date.none.fl_str_mv 2006-10
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/11336/152059
Bustamante, Claudia Anabel; Rosli, Hernan Guillermo; Añon, Maria Cristina; Civello, Pedro Marcos; Martinez, Gustavo Adolfo; β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness; Elsevier Ireland; Plant Science; 171; 4; 10-2006; 497-504
0168-9452
1873-2259
CONICET Digital
CONICET
url http://hdl.handle.net/11336/152059
identifier_str_mv Bustamante, Claudia Anabel; Rosli, Hernan Guillermo; Añon, Maria Cristina; Civello, Pedro Marcos; Martinez, Gustavo Adolfo; β-Xylosidase in strawberry fruit: Isolation of a full-length gene and analysis of its expression and enzymatic activity in cultivars with contrasting firmness; Elsevier Ireland; Plant Science; 171; 4; 10-2006; 497-504
0168-9452
1873-2259
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plantsci.2006.05.011
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0168945206001683?via%3Dihub
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Ireland
publisher.none.fl_str_mv Elsevier Ireland
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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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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