Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/65796
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Godoy, César A. | - |
dc.contributor.author | Romero, Óscar | - |
dc.contributor.author | Rivas, Blanca de las | - |
dc.contributor.author | Mateo González, César | - |
dc.contributor.author | Fernández-Lorente, Gloria | - |
dc.contributor.author | Guisán, José Manuel | - |
dc.contributor.author | Palomo, José Miguel | - |
dc.date.accessioned | 2013-02-04T10:36:42Z | - |
dc.date.available | 2013-02-04T10:36:42Z | - |
dc.date.issued | 2013 | - |
dc.identifier | doi: 10.1016/j.molcatb.2012.10.003 | - |
dc.identifier | issn: 1381-1177 | - |
dc.identifier.citation | Journal of Molecular Catalysis B: Enzymatic 87: 121-127 (2013) | - |
dc.identifier.uri | http://hdl.handle.net/10261/65796 | - |
dc.description.abstract | The enantioselectivity of a lipase from Geobacillus thermocatenulatus (BTL2) has been altered by a site-directed immobilization on tailor-made disulfide supports. The enzyme was genetically modified introducing a unique cysteine into different positions of the protein surface. These new enzyme variants (φ-BTL2) maintained the catalytic properties of the native enzyme. The φ-BTL2 was immobilized by different orientation on disulfide support at pH 7 via disulfide-exchange and additionally rigidification was introduced by the immobilization on disulfide-aldehyde support through the interaction of the reactive amino groups on the protein near to the position of the introduced cysteine with aldehydes on the support. The oriented immobilization of the φ-BTL2-S334C variant on disulfide-aldehyde supports generated a fully enantioselective biocatalyst (ee > 99%) in the kinetic resolution of rac-2-O-butyryl-2-phenylacetic acid and the asymmetric hydrolysis of phenylglutaric acid dimethyl diester. The simple orientation by the introduced cysteine on the lipase immobilization on disulfide supports was enough for good selectivity (ee > 99%) in the asymmetric hydrolysis but not in the kinetic resolution (ee = 27%). The rigidification of the oriented immobilized Q40C, T94C or S334C variants on disulfide-aldehyde support was key in the lipase selectivity improvement in the kinetic resolution process (ee from 27-50 to >99%). In this case, the oriented immobilization did not alter significantly the selectivity. A similar result was obtained for S196C variants in the asymmetric hydrolysis, which it selectivity was greatly altered depending on the immobilization method, no selectivity was observed after immobilization on disulfide support but a fully selective catalyst (ee > 99%) was achieved after immobilization on heterofunctional disulfide-aldehyde support. © 2012 Elsevier B.V. | - |
dc.description.sponsorship | The authors would like to thank the Spanish National Research Council (CSIC). We also gratefully acknowledge the Spanish Ministry of Science and Innovation for the “Ramon y Cajal” contract for Dr. Fernández-Lorente. Furthermore, O. Romero is thankful to CONICYT and “Programa Bicentenario Becas-Chile” for their financial support. | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier | - |
dc.rights | closedAccess | - |
dc.title | Changes on enantioselectivity of a genetically modified thermophilic lipase by site-directed oriented immobilization | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1016/j.molcatb.2012.10.003 | - |
dc.date.updated | 2013-02-04T10:36:42Z | - |
dc.description.version | Peer Reviewed | - |
dc.contributor.funder | Ministerio de Ciencia e Innovación (España) | - |
dc.contributor.funder | Consejo Superior de Investigaciones Científicas (España) | - |
dc.contributor.funder | European Commission | - |
dc.contributor.funder | Comisión Nacional de Investigación Científica y Tecnológica (Chile) | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100004837 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003339 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100000780 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100002848 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.languageiso639-1 | en | - |
item.fulltext | No Fulltext | - |
item.openairetype | artículo | - |
Aparece en las colecciones: | (ICTAN) Artículos (CIAL) Artículos (ICP) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
21
checked on 13-abr-2024
WEB OF SCIENCETM
Citations
19
checked on 27-feb-2024
Page view(s)
415
checked on 16-abr-2024
Download(s)
117
checked on 16-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.