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dc.contributor.authorVidal, Luis-
dc.contributor.authorDurany, Olga-
dc.contributor.authorSuau, T.-
dc.contributor.authorFerrer, Pau-
dc.contributor.authorBenaiges, M. D.-
dc.contributor.authorCaminal, Glòria-
dc.date.accessioned2010-03-17T09:16:48Z-
dc.date.available2010-03-17T09:16:48Z-
dc.date.issued2003-09-18-
dc.identifier.citationJournal of Chemical Technology and Biotechnology 78(11): 1171-1179 (2003)en_US
dc.identifier.issn0268-2575 (Print)-
dc.identifier.issn1097-4660 (Online)-
dc.identifier.urihttp://hdl.handle.net/10261/22452-
dc.description9 pages, 8 figures, 2 tables.-- Printed version published Nov 2003.en_US
dc.description.abstractAn expression system based on Escherichia coli and the T5 promoter allowed the overproduction of a his-tagged rhamnulose-1-phosphate aldolase (RhuA; EC 4.1.2.19), an enzyme with applications in the production of deoxyazasugars and deoxysugars compounds. Shake flask and bioreactor cultivation with E coli M15 (pQErham) were performed under different media and inducing conditions for RhuA expression. A Defined Medium (DM) with glucose as carbon source gave a high volumetric and enzyme productivity (3460 AU dm-3 and 288 AU dm-3 h-1 respectively) compared with Luria-Bertoni (LB) medium (2292 AU dm- 3 and 255 AU dm-3 h-1). The minimum quantity of (isopropyl--D-thiogalactoside) IPTG for optimal induction was estimated in 18-20 ºmol IPTG gDCW-1. The highest volumetric production of RhuA (8333 AU dm-3) was obtained when IPTG was added in the late log-phase. No significant differences were found in specific RhuA activity for induction temperatures of 30 and 37 ºC. An effective two-step purification process comprising affinity chromatography and gel permeation has been developed (overall recovery 66.5%). These studies provide the basis for the further development of an integrated process for recombinant RhuA production suitable for biotransformation applications.en_US
dc.description.sponsorshipFinancial support from CICYT (Projects: BIO99-1219-C02-01 and PPQ 2002-04625-C02-01). The Department of Chemical Engineering is the Unit of Biochemical Engineering of the Centre de Referència en Biotecnologia de la Generalitat de Catalunya (CeRBa).en_US
dc.format.extent22195 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherWiley-Blackwellen_US
dc.rightsclosedAccessen_US
dc.subjectRecombinant aldolaseen_US
dc.subjectHis-taggeden_US
dc.subjectPurificationen_US
dc.subjectBioreactoren_US
dc.subjectE colien_US
dc.titleHigh-level production of recombinant His-tagged rhamnulose 1-phosphate aldolase in Escherichia colien_US
dc.typeArtículoen_US
dc.identifier.doi10.1002/jctb.909-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1002/jctb.909en_US
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