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dc.contributor.authorPinheiro, Maísa Pessoa-
dc.contributor.authorCavalcante, Francisco Thálysson Tavares-
dc.contributor.authorFeitosa, Maria Rafaele Costa-
dc.contributor.authorGonçalves, Luciana Rocha Barros-
dc.contributor.authorSantos, José Cleiton Sousa dos-
dc.date.accessioned2020-10-02T18:29:16Z-
dc.date.available2020-10-02T18:29:16Z-
dc.date.issued2017-
dc.identifier.citationPINHEIRO, Maísa Pessoa; CAVALCANTE, Francisco Thálysson Tavares; FEITOSA, M. R. C.; GONÇALVES, Luciana Rocha Barros; SANTOS, José Cleiton Sousa dos. Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350. In: SIMPÓSIO NACIONAL DE BIOPROCESSOS, XXI; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, XII., 3 a 6 de set. 2017, Aracaju, Sergipe, Brasil. Anais [...] Aracaju, Sergipe, 2017.pt_BR
dc.identifier.issn2447 2816-
dc.identifier.urihttp://www.repositorio.ufc.br/handle/riufc/54437-
dc.description.abstractThe strategy of enzyme immobilization is studied with the objective of producing more stable biocatalysts that can be used in reactions of high industrial interest. Lipase B from Candida antarctica (CALB) has been covalently immobilized on epoxy Immobead-350 (IB-350) and some properties have been compared to glyoxyl-agarose-CALB and Novozym 435. The thermal and solvent stability was higher than that of the glyoxyl-agarose-CALB, and the CALB-IB350 preparation was more stable at pH 5,0 and 70 °C (t1⁄2 = 68 min). The activity of the new preparation versus tributyrin and triacetin was about 4 and 17 fold higher than that of Novozym 435, respectively. Thus, the covalent attachment between enzyme and support produced a stable and active biocatalyst under different conditions and substrates.pt_BR
dc.language.isopt_BRpt_BR
dc.subjectEnzimaspt_BR
dc.subjectLipasept_BR
dc.subjectLipase B Candida antarcticapt_BR
dc.titleStudy of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350pt_BR
dc.typeArtigo de Eventopt_BR
dc.title.enStudy of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350pt_BR
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