Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/238332
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Stabilization of glycosylated β-glucosidase by intramolecular crosslinking between oxidized glycosidic chains and lysine residues |
Autor: | Pinotti, Laura Marina; Tardioli, Paulo W.; Sanchez Farinas, Cristiane; Fernández-Lorente, Gloria CSIC ORCID ; Orrego, Alejandro H. CSIC ORCID; Guisán, José Manuel CSIC ORCID ; Pessela, Benevides C. CSIC ORCID | Fecha de publicación: | 2020 | Editor: | Springer Nature | Citación: | Applied Biochemistry and Biotechnology 192: 325–337 (2020) | Resumen: | Many industrial enzymes can be highly glycosylated, including the β-glucosidase enzymes. Although glycosylation plays an important role in many biological processes, such chains can cause problems in the multipoint immobilization techniques of the enzymes, since the glycosylated chains can cover the reactive groups of the protein (e.g., Lys) and do not allow those groups to react with reactive groups of the support (e.g., aldehyde and epoxy groups). Nevertheless, the activated glycosylated chains can be used as excellent crosslinking agents. The glycosylated chains when oxidized with periodate can generate aldehyde groups capable of reacting with the amino groups of the protein itself. Such intramolecular crosslinks may have significant stabilizing effects. In this study, we investigated if the intramolecular crosslinking occurs in the oxidized β-glucosidase and its effect on the stability of the enzyme. For this, the oxidation of glycosidic chains of β-glucosidase was carried out, allowing to demonstrate the formation of aldehyde groups and subsequent interaction with the amine groups and to verify the stability of the different forms of free enzyme (glycosylated and oxidized). Furthermore, we verified the influence of the glycosidic chains on the immobilization of β-glucosidase from Aspergillus niger and on the consequent stabilization. The results suggest that intramolecular crosslinking occurred and consequently the oxidized enzyme showed a much greater stabilization than the native enzyme (glycosylated). When the multipoint immobilization was performed in amino-epoxy-agarose supports, the stabilization of the oxidized enzyme increases by a 6-fold factor. The overall stabilization strategy was capable to promote an enzyme stabilization of 120-fold regarding to the soluble unmodified enzyme. | Versión del editor: | https://doi.org/10.1007/s12010-020-03321-x | URI: | http://hdl.handle.net/10261/238332 | DOI: | 10.1007/s12010-020-03321-x | E-ISSN: | 1559-0291 |
Aparece en las colecciones: | (CIAL) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 59,24 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
6
checked on 22-abr-2024
WEB OF SCIENCETM
Citations
7
checked on 26-feb-2024
Page view(s)
48
checked on 24-abr-2024
Download(s)
10
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.