A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease

Autores
Obregon, Walter David; Cisneros, José Sebastián; Ceccacci, Florencia; Quiroga, Evelina
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized on glyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilized enzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilized araujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C and in the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetate in buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate that immobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applications of araujiain in hydrolytic and synthetic processes.
Fil: Obregon, Walter David. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigación de Proteinas Vegetales; Argentina
Fil: Cisneros, José Sebastián. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Ceccacci, Florencia. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Física Aplicada; Argentina
Materia
ARAUJIAIN
PROTEASE
ENZYME
IMMOBILIZED
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/5680
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/5680
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoproteaseObregon, Walter DavidCisneros, José SebastiánCeccacci, FlorenciaQuiroga, EvelinaARAUJIAINPROTEASEENZYMEIMMOBILIZEDhttps://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2In this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized on glyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilized enzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilized araujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C and in the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetate in buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate that immobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applications of araujiain in hydrolytic and synthetic processes.Fil: Obregon, Walter David. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigación de Proteinas Vegetales; ArgentinaFil: Cisneros, José Sebastián. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Ceccacci, Florencia. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Física Aplicada; ArgentinaOMICS2015-05info: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/11336/5680Obregon, Walter David; Cisneros, José Sebastián; Ceccacci, Florencia; Quiroga, Evelina; A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease; OMICS; Journal of Bioprocessing & Biotechniques; 5; 3; 5-2015; 1000211-10002112155-9821enginfo:eu-repo/semantics/altIdentifier/url/http://goo.gl/uwtLDhinfo:eu-repo/semantics/altIdentifier/doi/10.4172/2155-9821.1000211info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:07:04Zoai:ri.conicet.gov.ar:11336/5680instacron: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 12:07:04.384CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
title A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
spellingShingle A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
Obregon, Walter David
ARAUJIAIN
PROTEASE
ENZYME
IMMOBILIZED
title_short A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
title_full A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
title_fullStr A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
title_full_unstemmed A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
title_sort A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
dc.creator.none.fl_str_mv Obregon, Walter David
Cisneros, José Sebastián
Ceccacci, Florencia
Quiroga, Evelina
author Obregon, Walter David
author_facet Obregon, Walter David
Cisneros, José Sebastián
Ceccacci, Florencia
Quiroga, Evelina
author_role author
author2 Cisneros, José Sebastián
Ceccacci, Florencia
Quiroga, Evelina
author2_role author
author
author
dc.subject.none.fl_str_mv ARAUJIAIN
PROTEASE
ENZYME
IMMOBILIZED
topic ARAUJIAIN
PROTEASE
ENZYME
IMMOBILIZED
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.10
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv In this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized on glyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilized enzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilized araujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C and in the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetate in buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate that immobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applications of araujiain in hydrolytic and synthetic processes.
Fil: Obregon, Walter David. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigación de Proteinas Vegetales; Argentina
Fil: Cisneros, José Sebastián. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Ceccacci, Florencia. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Física Aplicada; Argentina
description In this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized on glyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilized enzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilized araujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C and in the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetate in buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate that immobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applications of araujiain in hydrolytic and synthetic processes.
publishDate 2015
dc.date.none.fl_str_mv 2015-05
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/11336/5680
Obregon, Walter David; Cisneros, José Sebastián; Ceccacci, Florencia; Quiroga, Evelina; A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease; OMICS; Journal of Bioprocessing & Biotechniques; 5; 3; 5-2015; 1000211-1000211
2155-9821
url http://hdl.handle.net/11336/5680
identifier_str_mv Obregon, Walter David; Cisneros, José Sebastián; Ceccacci, Florencia; Quiroga, Evelina; A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease; OMICS; Journal of Bioprocessing & Biotechniques; 5; 3; 5-2015; 1000211-1000211
2155-9821
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://goo.gl/uwtLDh
info:eu-repo/semantics/altIdentifier/doi/10.4172/2155-9821.1000211
info:eu-repo/semantics/altIdentifier/doi/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv OMICS
publisher.none.fl_str_mv OMICS
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
_version_ 1846782432115687424
score 12.982451

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