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dc.contributor.authorAcosta, Javierspa
dc.contributor.authorDel Arco, Jonspa
dc.contributor.authorMartínez Pascual, Saraspa
dc.contributor.authorClemente Suárez, Vicente Javierspa
dc.contributor.authorFernandez Lucas, Jesusspa
dc.date.accessioned2018-11-17T13:38:54Z
dc.date.available2018-11-17T13:38:54Z
dc.date.issued2018
dc.identifier.issn2073-4344spa
dc.identifier.urihttp://hdl.handle.net/11323/1211spa
dc.description.abstractBiocatalysis reproduce nature’s synthetic strategies in order to synthesize different organic compounds. Natural metabolic pathways usually involve complex networks to support cellular growth and survival. In this regard, multi-enzymatic systems are valuable tools for the production of a wide variety of organic compounds. Methods: The production of different purine nucleosides and nucleoside-50 -monophosphates has been performed for first time, catalyzed by the sequential action of 2 0 -deoxyribosyltransferase from Lactobacillus delbrueckii (LdNDT) and hypoxanthine-guanine-xanthine phosphoribosyltransferase from Thermus themophilus HB8 (TtHGXPRT). Results: The biochemical characterization of LdNDT reveals that the enzyme is active and stable in a broad range of pH, temperature, and ionic strength. Substrate specificity studies showed a high promiscuity in the recognition of purine analogues. Finally, the enzymatic production of different purine derivatives was performed to evaluate the efficiency of multi-enzymatic system LdNDT/TtHGXPRT. Conclusions: The production of different therapeutic purine nucleosides was efficiently catalyzed by LdNDT/TtHGXPRT. In addition, the resulting by-products were converted to IMP and GMP. Taking all of these features, this bioprocess entails an efficient, sustainable, and economical alternative to chemical synthetic methods.spa
dc.language.isoeng
dc.publisherCatalystsspa
dc.rightsAtribución – No comercial – Compartir igualspa
dc.subject2 0 -deoxyribosyltransferaseeng
dc.subjectphosphoribosyltransferaseseng
dc.subjectcascade reactionseng
dc.subjectpurine nucleoside analogueseng
dc.subjectdietary nucleotideseng
dc.titleOne-pot multi-enzymatic production of purine derivatives with application in pharmaceutical and food industryeng
dc.typeArtículo de revistaspa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.identifier.instnameCorporación Universidad de la Costaspa
dc.identifier.reponameREDICUC - Repositorio CUCspa
dc.identifier.repourlhttps://repositorio.cuc.edu.co/spa
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Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzym. Microb. Technol. 2007, 40, 1451–1463. [CrossRef] 23. Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680–685. [CrossRef] [PubMed] 24. Gill, S.C.; Von Hippel, P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 1989, 182, 319–326. [CrossRef]spa
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