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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/5680
Ver los metadatos del registro completo
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3498 |
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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 Técnicas2025-09-29T10:34:35Zoai: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:34982025-09-29 10:34:35.3CONICET 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 |
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1844614363362623488 |
score |
13.070432 |