A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease

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 act...

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Autores principales: Obregón, Walter David, Cisneros, José Sebastián, Ceccacci, Florencia, Quiroga, Evelina
Formato: Articulo
Lenguaje:Inglés
Publicado: 2015
Materias:
Biología
Araujiain
Protease
Enzyme technology
Immobilized enzymes;
Enzymatic stabilization
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/96593
https://ri.conicet.gov.ar/11336/5680
http://goo.gl/uwtLDh
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-96593
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Araujiain
Protease
Enzyme technology
Immobilized enzymes;
Enzymatic stabilization
spellingShingle Biología
Araujiain
Protease
Enzyme technology
Immobilized enzymes;
Enzymatic stabilization
Obregón, Walter David
Cisneros, José Sebastián
Ceccacci, Florencia
Quiroga, Evelina
A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease
topic_facet Biología
Araujiain
Protease
Enzyme technology
Immobilized enzymes;
Enzymatic stabilization
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.
format Articulo
Articulo
author Obregón, Walter David
Cisneros, José Sebastián
Ceccacci, Florencia
Quiroga, Evelina
author_facet Obregón, Walter David
Cisneros, José Sebastián
Ceccacci, Florencia
Quiroga, Evelina
author_sort Obregón, Walter David
title A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease
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 highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
publishDate 2015
url http://sedici.unlp.edu.ar/handle/10915/96593
https://ri.conicet.gov.ar/11336/5680
http://goo.gl/uwtLDh
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