Please use this identifier to cite or link to this item: https://repositorio.ufrn.br/handle/123456789/29631
Title: Nanopartículas de poli-hidroxibutirato-co-valerato como suporte para a imobilização da lipase de Candida antarctica fração B
Other Titles: Nanoparticles of poly(hydroxybutyrate-co-hydroxyvalerate) as support for the immobilization of Candida antarctica lipase (fraction B)
Authors: Fernandes, Ilizandra A.
Nyari, Nádia L. D.
Oliveira, José Vladimir de
Rigo, Elisandra
Souza, Maria Cristiane M. de
Gonçalves, Luciana R. B.
Pergher, Sibele Berenice Castellã
Oliveira, Débora de
Keywords: Nanoparticles;Immobilization;Lipases
Issue Date: Apr-2014
Publisher: Sociedade Brasileira de Química
Citation: FERNANDES, I. A.; NYARI, N. L. D.; OLIVEIRA, J. V. de; RIGO, E.; SOUZA, M. C. M. de; GONÇALVES, L. R. B.; PERGHER, Sibele Berenice Castellã; OLIVEIRA, D. de..Nanopartículas de poli-hidroxibutirato-co-valerato como suporte para a imobilização da lipase de Candida antarctica fração B. Química Nova (Impresso), v. 37, n. 2, p. 331-336, abr. 2014. ISSN 0100-4042. Disponível em: http://static.sites.sbq.org.br/quimicanova.sbq.org.br/pdf/v37n2a22.pdf. Acesso em 25 maio 2020. http://dx.doi.org/10.5935/0100-4042.20140055
Portuguese Abstract: This work evaluates the immobilization of Candida antarctica lipase (Fraction B) using poly(hydroxybutyrate-co-hydroxyvalerate) (PHBV) nanoparticles as support. The effects of immobilization time (30-150 min) and pH (5-10) on lipase loading were evaluated. The stability of the immobilized enzyme towards temperature (40, 60, and 80 ºC), reuse and storage (at 4 ºC) were also determined. Furthermore, to assess its potential application in a system of interest, the immobilized lipase was used as a catalyst in the esterification of geraniol with oleic acid. The results indicated a time of 120 minutes and pH of 7 as optimal for immobilization. A 21 hour exposure of the PHBV-lipase derivative to 60 ºC showed a 33% reduction of the initial activity while storage at 4 ºC led to a residual activity (5% of the original activity). The derivative was used without significant loss of activity for 4 successive cycles. The use of the immobilized lipase as a catalyst in the production of geranyl oleate led to about 88% conversion of the initial reactants to products
URI: https://repositorio.ufrn.br/jspui/handle/123456789/29631
ISSN: 0100-4042
Appears in Collections:IQ - Artigos publicados em periódicos

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