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dc.creatorAlvarenga, Adriana Elizabet-
dc.creatorAmoroso, Maria Julia del R.-
dc.creatorIllanes, Andrés-
dc.creatorCastro, Guillermo Raul-
dc.date2017-05-08T18:09:17Z-
dc.date2017-05-08T18:09:17Z-
dc.date2014-05-
dc.date2017-05-08T15:31:35Z-
dc.date.accessioned2019-04-29T15:32:01Z-
dc.date.available2019-04-29T15:32:01Z-
dc.date.issued2017-05-08T18:09:17Z-
dc.date.issued2017-05-08T18:09:17Z-
dc.date.issued2014-05-
dc.date.issued2017-05-08T15:31:35Z-
dc.identifierAlvarenga, Adriana Elizabet; Amoroso, Maria Julia del R.; Illanes, Andrés; Castro, Guillermo Raul; Cross‑linked α‑l‑rhamnosidase aggregates with potential application in food industry; Springer; European Food Research And Technology; 238; 5; 5-2014; 797-801-
dc.identifier1438-2377-
dc.identifierhttp://hdl.handle.net/11336/16078-
dc.identifier1438-2385-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/295912-
dc.descriptionα-l-Rhamnosidase (E.C. 3.2.1.40) from Brevundimonas sp. Ci19 was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with acetone followed by glutaraldehyde cross-linking. The effects of precipitation and cross-linking on CLEA activity were investigated and characterized. Sixty percent acetone solution and 2.0 % glutaraldehyde were used at pH 7.0 for 1-h cross-linking reaction. The yield of rhamnosidase-CLEA was approximately 80 % starting from crude extracts or pure enzyme suggesting non-purification steps are required for extended use. No significant differences in optimum pH and temperature values of the enzyme were recorded after immobilization. The rham-CLEA recycled 4 times showed about 80 % rhamnosidase activity; meanwhile, in the fifth and six recycled time, the enzyme activity was reduced to about 40 and 20 %, respectively.-
dc.descriptionFil: Alvarenga, Adriana Elizabet. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina-
dc.descriptionFil: Amoroso, Maria Julia del R.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina. Universidad del Norte Santo Tomás de Aquino; Argentina. Universidad Nacional de Tucumán; Argentina-
dc.descriptionFil: Illanes, Andrés. Pontificia Universidad Catolica de Valparaiso; Chile-
dc.descriptionFil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherSpringer-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00217-014-2157-4-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00217-014-2157-4-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectAlpha-l-rhamnosidase-
dc.subjectCLEA-
dc.subjectBiotransformation-
dc.subjectImmobilization-
dc.subjectBioprocesamiento Tecnológico, Biocatálisis, Fermentación-
dc.subjectBiotecnología Industrial-
dc.subjectINGENIERÍAS Y TECNOLOGÍAS-
dc.titleCross‑linked α‑l‑rhamnosidase aggregates with potential application in food industry-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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