English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/150585
Share/Impact:
Statistics
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
Exportar a otros formatos:
Title

Biosynthesis of an antiviral compound using a stabilized phosphopentomutase by multipoint covalent immobilization

AuthorsRivero, Cintia W.; López-Gallego, Fernando; Pessela, Benevides C. ; Guisán, José Manuel ; Trelles, Jorge A.
KeywordsEscherichia coli
Stabilizing agents
Glyoxyl-agarose
Ribavirin
Issue Date2017
PublisherElsevier
CitationJournal of Biotechnology 249: 34-41 (2017)
AbstractRibavirin is a synthetic guanosine analogue with a broad-spectrum of antiviral activity. It is clinically effective against several viruses, such as respiratory syncytial virus, several hemorrhagic fever viruses and HCV when combined with pegylated interferon-α. Phosphopentomutase (PPM) catalyzes the transfer of intramolecular phosphate (from C1 to C5) on ribose, and is involved in pentose phosphate pathway and in purine metabolism. Reactions catalyzed by this enzyme are useful for nucleoside analogues production. However, out of its natural environment PPM is unstable and its stability is affected by parameters such as pH and temperature. Therefore, to irreversibly immobilize this enzyme, it needs to be stabilized. In this work, PPM from Escherichia coli ATCC 4157 was overexpressed, purified, stabilized at alkaline pH and immobilized on several supports. The activity of different additives as stabilizing agents was evaluated, and the best result was found using 10% (v/v) glycerol. Under this condition, PPM maintained 86% of its initial activity at pH 10 after 18 h incubation, which allowed further covalent immobilization of this enzyme on glyoxyl-agarose with a high yield. This is the first time that PPM has been immobilized by multipoint covalent attachment on glyoxyl support, this derivative being able to biosynthesize ribavirin from α-D-ribose-5-phosphate.
URIhttp://hdl.handle.net/10261/150585
DOI10.1016/j.jbiotec.2017.03.027
Identifiersdoi: 10.1016/j.jbiotec.2017.03.027
issn: 1873-4863
e-issn: 0168-1656
Appears in Collections:(CIAL) Artículos
(ICP) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
 

Related articles:


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