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dc.contributor.authorMartínez Gómez, Ana Isabel 
dc.contributor.authorMartínez Rodríguez, Sergio 
dc.contributor.authorClemente Jiménez, Josefa María 
dc.contributor.authorPozo Dengra, Joaquín 
dc.contributor.authorRodríguez Vico, Felipe 
dc.contributor.authorLas Heras Vázquez, Francisco Javier 
dc.date.accessioned2024-05-23T10:23:36Z
dc.date.available2024-05-23T10:23:36Z
dc.date.issued2007
dc.identifier.issn1098-5336
dc.identifier.urihttp://hdl.handle.net/10835/16559
dc.description.abstractTwo recombinant reaction systems for the production of optically pure D-amino acids from different D,L-5-monosubstituted hydantoins were constructed. Each system contained three enzymes, two of which were D-hydantoinase and D-carbamoylase from Agrobacterium tumefaciens BQL9. The third enzyme was hydantoin racemase 1 for the first system and hydantoin racemase 2 for the second system, both from A. tumefaciens C58. Each system was formed by using a recombinant Escherichia coli strain with one plasmid harboring three genes coexpressed with one promoter in a polycistronic structure. The D-carbamoylase gene was cloned closest to the promoter in order to obtain the highest level of synthesis of the enzyme, thus avoiding intermediate accumulation, which decreases the reaction rate. Both systems were able to produce 100% conversion and 100% optically pure D-methionine, D-leucine, D-norleucine, D-norvaline, D-aminobutyric acid, D-valine, D-phenylalanine, D-tyrosine, and D-tryptophan from the corresponding hydantoin racemic mixture. For the production of almost all D-amino acids studied in this work, system 1 hydrolyzed the 5-monosubstituted hydantoins faster than system 2.es_ES
dc.language.isoenes_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectHydantoinase processes_ES
dc.subjectD-amino acidses_ES
dc.titleRecombinant Polycistronic Structure of Hydantoinase Process Genes in Escherichia coli for the Production of Optically Pure D-Amino Acidses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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