English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/162733
Share/Impact:
Statistics
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Exploiting the Versatility of Aminated Supports Activated with Glutaraldehyde to Immobilize β-galactosidase from Aspergillus oryzae

AuthorsZaak, Hadjer; Peirce, Sara; Albuquerque, Tiago L.; Sassi, Mohamed; Fernández-Lafuente, Roberto
Issue Date25-Aug-2017
PublisherMultidisciplinary Digital Publishing Institute
CitationCatalysts 7 (9): 250 (2017)
AbstractThe enzyme β-galactosidase from <i>Aspergillus oryzae</i> has been immobilized in aminated (MANAE)-agarose beads via glutaraldehyde chemistry using different strategies. The immobilization on MANAE-supports was first assayed at different pH values (this gave different stabilities to the immobilized enzymes) and further modified with glutaraldehyde. Dramatic drops in activity were found, even using 0.1% (<i>v</i>/<i>v</i>) glutaraldehyde. The use of a support with lower activation permitted to get a final activity of 30%, but stability was almost identical to that of the just adsorbed enzyme. Next, the immobilization on pre-activated glutaraldehyde beads was assayed at pH 5, 7 and 9. At pH 7, full, rapid immobilization and a high expressed enzyme activity were accomplished. At pH 9, some decrease in enzyme activity was observed. Direct covalent immobilization of the enzyme was very slow; even reducing the volume of enzyme/support ratio, the yield was not complete after 24 h. The stability of the biocatalyst using pre-activated supports was about 4–6 folds more stable than that of the enzyme immobilized via ion exchange at pH 5, with small differences among them. Thus, the immobilization of the enzyme at pH 7 at low ionic strength on pre-activated glutaraldehyde supports seems to be the most adequate in terms of activity, stability and immobilization rate.
Publisher version (URL)https://doi.org/10.3390/catal7090250
URIhttp://hdl.handle.net/10261/162733
Identifiershttps://doi.org/10.3390/catal7090250
Appears in Collections:(ICP) Artículos
Files in This Item:
File Description SizeFormat 
catalysts-07-00250-v2.pdf1,69 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.