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RevistaINTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Año2019
Volumen 130
Páginas798-809.
Internacional

Chitosan activated with divinyl sulfone: a new heterofunctional support for enzyme immobilization. Application in the immobilization of lipase B from Candida antarctica

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
 
Bruna B. Pinheiro, Nathalia S. Rios, Elena Rodríguez Aguado, Roberto Fernandez-
Lafuente, Tiago M. Freire, Pierre B. A. Fechine, José C. S. dos Santos*, Luciana R.
6 B. Gonçalves*
 
A novel heterofunctional support for enzyme immobilization, chitosan-divinyl sulfone, was assessed in this study. The
activation of chitosan with DVS was carried out at three different pHs (10.0, 12.5 and 14.0) and a Candida antarctica
Lipase B (CALB) was selected as the model enzyme. After immobilization, the biocatalysts were incubated under
alkaline conditions in a buffer to facilitate the multipoint covalent attachment, followed by incubation in ethylenediamine
(EDA) aiming at blocking the remaining reactive groups. The highest thermal stability was obtained when pH 10.0 was
used during support activation. These results were shown to be better than those obtained when using glutaraldehyde
as the support-activating reagent. Subsequently, the immobilization pH was investigated (5.0, 7.0 and 10.0) prior to
alkaline incubation, with the highest enzyme stability levels found at pH 10.0. Finally, the selected biocatalyst was
used in the hydrolysis of ethyl hexanoate and presented an activity of 14,520.37 U/g of immobilized lipase at pH 5.0.
These results show that chitosan activated with divinyl sulfone is a very promising support for enzyme immobilization
and the proposed protocol is able to successfully improve enzyme stability.
Palabras clave:Immobilization, divinyl sulfone, Chitosan, Candida antarctica Lipase B, Multipoint covalent attachment.
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