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

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 immobili...

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Bibliographic Details
Published in:International journal of biological macromolecules 2019-06, Vol.130, p.798-809
Main Authors: Pinheiro, Bruna B., Rios, Nathalia S., Rodríguez Aguado, Elena, Fernandez-Lafuente, Roberto, Freire, Tiago M., Fechine, Pierre B.A., dos Santos, José C.S., Gonçalves, Luciana R.B.
Format: Article
Language:English
Subjects:
Candida antarctica lipase B
Chitosan
Divinyl sulfone
Immobilization
Multipoint covalent attachment
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Summary: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. [Display omitted] •Divinyl sulfone was used to activate chitosan.•Chitosan activated with divinyl sulfone had the best thermostability.•Biocatalyst was more active at pH 5 during hydrolysis of ethyl hexanoate.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2019.02.145