Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/79417

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dc.contributor.authorContato, Alex Graçapor
dc.contributor.authorVici, Ana Claudiapor
dc.contributor.authorAranha, Guilherme Mauropor
dc.contributor.authorPinheiro, Vanessa Elisapor
dc.contributor.authorOliveira, Tássio Brito depor
dc.contributor.authorFreitas, Emanuelle Neiverth depor
dc.contributor.authorValvassora Junior, Almir Luiz Aparecidopor
dc.contributor.authorMichelin, Michelepor
dc.contributor.authorTeixeira, J. A.por
dc.contributor.authorPolizeli, Maria de Lourdes T. M.por
dc.date.accessioned2022-09-06T10:25:45Z-
dc.date.available2022-09-06T10:25:45Z-
dc.date.issued2022-04-07-
dc.identifier.citationContato, Alex Graça; Vici, Ana Claudia; Aranha, Guilherme Mauro; Pinheiro, Vanessa Elisa; Oliveira, Tássio Brito de; Freitas, Emanuelle Neiverth de; Valvassora Junior, Almir Luiz Aparecido; Michelin, Michele; Teixeira, José A.; Polizeli, Maria de Lourdes T. M., Comparison in the Trichoderma longibrachiatum xyloglucanase production using tamarind (Tamarindus indica) and jatobá (Hymenaea courbaril) seeds: factorial design and immobilization on ionic supports. BioIberoAmerica 2022 - 3rd IberoAmerican Congress on Biotechnology. No. PO - (736), Braga, Portugal, Apr 7-9, 333, 2022.por
dc.identifier.urihttps://hdl.handle.net/1822/79417-
dc.description.abstractin the control of the stretching and expansion of the plant cell wall. There are five types of enzymes known to be capable of cleaving the linear chain of xyloglucan, the most famous of them being the xyloglucanase (XEG). The immobilization can be used to solve problems related to stability, besides the economic benefits brought by the possibility of repeated use and recovery, decreasing the costs of production. Therefore, this study aims the optimization of the production of a xyloglucanase from Trichoderma longibrachiatum, with the aid of factorial design, using tamarind (Tamarindus indica) and jatobá (Hymenaea courbaril) seeds as carbon source; and the immobilization of the enzyme on ionic supports, such as MANAE (monoamino-N-aminoethyl), DEAE (diethylaminoethyl)-cellulose, CM (carboxymethyl)-cellulose and PEI (polyethyleneimine). High concentrations of carbon source in the culture medium, especially tamarind seeds, were the most favorable conditions for the greater activity of the xyloglucanase from T. longibrachiatum. The scaling up from Erlenmeyer flasks to the bioreactor was an essential strategy to increase the content of secreted enzyme. Regarding the biochemical characterization of the crude extract, the optimal temperature was 50-55 °C and the optimal pH 5.0. Regarding the stabilities to pH and to temperature, the enzyme was not stable for prolonged periods, which was crucial for the performing of immobilization on ionic resins (CM-cellulose, DEAE-cellulose, MANAE, and PEI), being the first time described in literature the immobilization of a xyloglucanase on these supports.por
dc.description.sponsorshipWe thank the Fundação de Amparo à Pesquisa do estado de São Paulo (process 2018/07522-6; 2014/50884-5), and Conselho Nacional de Dsenvolvimento Científico (process 301963/2017-7; 465319/2014-9).por
dc.language.isoengpor
dc.rightsopenAccesspor
dc.subjectxyloglucanasepor
dc.subjectTrichoderma longibrachiatumpor
dc.subjectHymenaea courbarilpor
dc.subjectTamarindus indicapor
dc.subjectenzyme immobilizationpor
dc.titleComparison in the Trichoderma longibrachiatum xyloglucanase production using tamarind (Tamarindus indica) and jatobá (Hymenaea courbaril) seeds: factorial design and immobilization on ionic supportspor
dc.typeconferenceAbstractpor
dc.peerreviewedyespor
dc.relation.publisherversionhttps://www.bioiberoamerica2022.com/por
dc.commentsCEB55715por
oaire.citationStartPage333por
oaire.citationIssuePO - (736)-
oaire.citationConferencePlaceBraga, Portugalpor
dc.date.updated2022-09-03T09:46:41Z-
dc.description.publicationversioninfo:eu-repo/semantics/publishedVersion-
sdum.conferencePublicationBioIberoAmerica 2022 - 3rd IberoAmerican Congress on Biotechnologypor
Aparece nas coleções:CEB - Resumos em Livros de Atas / Abstracts in Proceedings

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