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dc.contributor.authordel Arco, Jon
dc.contributor.authorClemente-Suárez, Vicente Javier
dc.contributor.authorCorral, Octavio Jorge (1)
dc.contributor.authorJordaan, Justin
dc.contributor.authorHormigo, Daniel
dc.contributor.authorPerona, Almudena
dc.contributor.authorFernández-Lucas, Jesús
dc.contributor.authorMartínez-Pascual, Sara
dc.contributor.authorClemente-Suárez, Vicente Javier
dc.date2018-05
dc.date.accessioned2018-07-31T14:12:50Z
dc.date.available2018-07-31T14:12:50Z
dc.identifier.issn2073-4344
dc.identifier.urihttps://reunir.unir.net/handle/123456789/6720
dc.description.abstractThe enzymatic synthesis of nucleotides offers several advantages over traditional multistep chemical methods, such as stereoselectivity, regioselectivity, enantioselectivity, simple downstream processing, and the use of mild reaction conditions. However, in order to scale up these bioprocesses, several drawbacks, such as the low enzyme stability and recycling, must be considered. Enzyme immobilization may overcome these cost-related problems by enhancing protein stability and facilitating the separation of products. In this regard, tetrameric hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT) from Thermus thermophilus HB8 was covalently immobilized onto glutaraldehyde-activated MagReSyn (R) Amine magnetic iron oxide porous microparticles (MTtHGXPRT). In this context, two different strategies were followed: (a) an enzyme immobilization through its N-terminus residues at pH 8.5 (derivatives MTtHGXPRT1-3); and (b) a multipoint covalent immobilization through the surface lysine residues at pH 10 (derivatives MTtHGXPRT4-5). The immobilized derivatives of MTtHGXPRT3 (activity 1581 international units per gram of support, IU/g; retained activity 29%) and MTtHGXPRT5 (activity 1108 IU/g; retained activity 23%) displayed the best wet biocatalyst activity, and retained activity values in the enzymatic synthesis of inosine-5'-monophosphate (IMP). In addition, the dependence of the activities and stabilities of both derivatives on pH and temperature was tested, as well as their reusability potential. Taking these results into account, MTtHGXPRT3 was chosen as the best biocatalyst (negligible loss of activity at 60 degrees C during 24 h; reusable up to seven cycles). Finally, as proof of concept, the enzymatic production of dietary nucleotides from high concentrations of low soluble bases was achieved.es_ES
dc.language.isoenges_ES
dc.publisherCatalystses_ES
dc.relation.ispartofseries;vol. 8, nº5
dc.relation.urihttp://www.mdpi.com/2073-4344/8/5/184/htmes_ES
dc.rightsopenAccesses_ES
dc.subjectphosphoribosyltransferaseses_ES
dc.subjectenzyme immobilizationes_ES
dc.subjectgreen processes_ES
dc.subjectdietary nucleotideses_ES
dc.subjectJCRes_ES
dc.subjectScopuses_ES
dc.titleOne-Pot, One-Step Production of Dietary Nucleotides by Magnetic Biocatalystses_ES
dc.typeArticulo Revista Indexadaes_ES
reunir.tag~ARIes_ES
dc.identifier.doihttps://doi.org/10.3390/catal8050184


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