Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.provenance | CONICET | - |
| dc.creator | Torres, Pedro | - |
| dc.creator | Manzo, Ricardo Martín | - |
| dc.creator | Rubiolo, Amelia Catalina | - |
| dc.creator | Batista Viera, Francisco | - |
| dc.creator | Mammarella, Enrique José | - |
| dc.date | 2016-12-12T21:11:14Z | - |
| dc.date | 2016-12-12T21:11:14Z | - |
| dc.date | 2014-03 | - |
| dc.date | 2016-12-12T13:47:56Z | - |
| dc.date.accessioned | 2019-04-29T15:31:09Z | - |
| dc.date.available | 2019-04-29T15:31:09Z | - |
| dc.date.issued | 2016-12-12T21:11:14Z | - |
| dc.date.issued | 2016-12-12T21:11:14Z | - |
| dc.date.issued | 2014-03 | - |
| dc.date.issued | 2016-12-12T13:47:56Z | - |
| dc.identifier | Torres, Pedro; Manzo, Ricardo Martín; Rubiolo, Amelia Catalina; Batista Viera, Francisco; Mammarella, Enrique José; Purification of an l-arabinose isomerase from Enterococcus faecium DBFIQ E36 employing a biospecific affinity strategy; Elsevier Science; Journal Of Molecular Catalysis B: Enzymatic; 102; 3-2014; 99-105 | - |
| dc.identifier | 1381-1177 | - |
| dc.identifier | http://hdl.handle.net/11336/9194 | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/295618 | - |
| dc.description | l-Arabinose isomerase is an intracellular enzyme that can convert l-arabinose to l-ribulose and d-galactose to d-tagatose, a promising but rare nutraceutical. Most of l-arabinose isomerases purified upto date employed the combination between DNA recombinant technology and affinity chromatographybased on poly-histidine tail recognition, but few of the enzymes were obtained and purified in a non-recombinant way. For these reasons, a specific affinity bioadsorbent containing l-arabitol as ligand, acompetitive inhibitor of the enzyme, was designed and synthesized for achieving pure preparations ofthe enzyme l-arabinose isomerase from wild-type Enterococcus faecium DBFIQ E36 strain, isolated fromraw cow milk.The two-step purification procedure consisted in fractionation by ammonium sulphate precipitationfollowed by affinity chromatography with obtained bioadsorbent, allowing the purification, to elec-trophoretical homogeneity, of target enzyme. Characterization studies were performed with purifiedl-arabinose isomerase in order to increase knowledge of their physicochemical properties. In this sense,enzyme exhibited an optimum temperature of 50?C and optimum pH of 7.0, maintaining good sta-bility in the ranges 20–45?C and pH 6.5–8. Kiwere calculated, employing d-galactose as substrate, forl-arabitol and l-ribitol, achieving values of 7.9 mM and 183 mM, respectively. Kmand Vmaxvalues obtainedwere 35 mM and 81 U mg-1at 50?C, respectively. Mass spectrometry assay revealed a 48 kDa monomerwhereas gel permeation chromatography achieved a 187 kDa molecular weight for native enzyme. Finally,2D-electrophoresis and isoelectrofocusing analysis revealed an isoelectric point value of 3.80. Resultshave unveiled both an acidic nature and promising properties for l-arabinose isomerase isolated from E.faecium DBFIQ E36. | - |
| dc.description | Fil: Torres, Pedro. Universidad de la Republica; Uruguay | - |
| dc.description | Fil: Manzo, Ricardo Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina | - |
| dc.description | Fil: Rubiolo, Amelia Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina | - |
| dc.description | Fil: Batista Viera, Francisco. Universidad de la Republica; Uruguay | - |
| dc.description | Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Elsevier Science | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.molcatb.2014.01.023 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117714000344 | - |
| dc.rights | info:eu-repo/semantics/restrictedAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.source.uri | http://hdl.handle.net/11336/9194 | - |
| dc.subject | l-Arabinose isomerase | - |
| dc.subject | d-Tagatose d-galactos | - |
| dc.subject | Affinity chromatography | - |
| dc.subject | Enterococcus faecium strain | - |
| dc.subject | Bioprocesamiento Tecnológico, Biocatálisis, Fermentación | - |
| dc.subject | Biotecnología Industrial | - |
| dc.subject | INGENIERÍAS Y TECNOLOGÍAS | - |
| dc.title | Purification of an l-arabinose isomerase from Enterococcus faecium DBFIQ E36 employing a biospecific affinity strategy | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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