Por favor, use este identificador para citar o enlazar este ítem: http://repositorio.ufc.br/handle/riufc/54437
Tipo: Artigo de Evento
Título : Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
Título en inglés: Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
Autor : Pinheiro, Maísa Pessoa
Cavalcante, Francisco Thálysson Tavares
Feitosa, Maria Rafaele Costa
Gonçalves, Luciana Rocha Barros
Santos, José Cleiton Sousa dos
Palabras clave : Enzimas;Lipase;Lipase B Candida antarctica
Fecha de publicación : 2017
Citación : PINHEIRO, 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.
Abstract: The 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.
URI : http://www.repositorio.ufc.br/handle/riufc/54437
ISSN : 2447 2816
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