English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/192554
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Immobilization and stabilization of commercial b-1,4-endoxylanase DepolTM 333MDP by multipoint covalent attachment for xylan hydrolysis: Production of prebiotics (xylo-oligosaccharides)

AuthorsMartins de Oliveira, Sandro; Moreno-Pérez, Sonia; Romero-Fernández, Maria; Fernández-Lorente, Gloria CSIC ORCID ; Rocha-Martín, Javier CSIC ORCID ; Guisán, José Manuel CSIC ORCID
KeywordsXylan hydrolysis
Enzyme immobilization-stabilization
Multipoint covalent immobilization
Xylooligosaccharides production
Issue Date2018
PublisherTaylor & Francis
CitationBiocatalysis and Biotransformation 36(2): 141-150 (2018)
AbstractThe commercial enzyme Depol™ 333MDP (D333MDP) was immobilized by multipoint covalent attachment onto 10% cross-linked agarose beads support highly activated with aldehyde groups. The enzyme immobilization process was very efficient, retaining 86% of its initial catalytic activity. Thermal stability of the immobilized D333MDP biocatalysts varied according to the incubation time of the enzyme-support. The optimal immobilized biocatalyst was produced after 24 h of incubation under alkaline conditions and longer incubation times resulted in a loss of stability. The optimal immobilized biocatalyst was 60- and 50-fold more stable at pH 5.5 and pH 7 at 50 °C than the soluble enzyme, respectively. Activity and stability at pH 5.5 were enhanced when the optimal immobilized biocatalyst was modified by chemical amination of the enzyme surface. The chemical amination of the immobilized enzyme surface was 5-fold more stable at pH 5.5 and 50 °C compared with the unmodified immobilized biocatalyst. The best immobilized biocatalysts (containing 100 UI/g of support) were evaluated in the beechwood xylan hydrolysis reaction at 50 °C and pH 5.5. 80% of the reducing sugars were released after 6 h of hydrolysis with the aminated biocatalyst. Xylan hydrolysis reaction with the aminated biocatalyst was 80% faster than with the non-aminated one. The final composition of the xylooligosaccharides (XOS) obtained was identified and quantified by HPAEC-PAD which showed it was composed of 90% of xylobiose and 5% of xylotriose and xylose. The aminated immobilized-stabilized biocatalyst was used for four cycles of hydrolysis with no loss of catalytic activity, resulting in highly active and stable derivative suitable for industrial processes.
Publisher version (URL)http://dx.doi.org/10.1080/10242422.2017.1308497
Appears in Collections:(ICP) Artículos
(CIAL) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf59,24 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

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