Chitosan activated with divinyl sulfone: a new heterofunctional support for enzyme immobilization. Application in the immobilization of lipase B from Candida antarctica.
Int J Biol Macromol
; 130: 798-809, 2019 Jun 01.
Article
en En
| MEDLINE
| ID: mdl-30817969
ABSTRACT
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 pHâ¯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 pHâ¯10.0. Finally, the selected biocatalyst was used in the hydrolysis of ethyl hexanoate and presented an activity of 14,520.37â¯U/g of immobilized lipase at pHâ¯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.
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Banco de datos:
MEDLINE
Asunto principal:
Sulfonas
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Proteínas Fúngicas
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Quitosano
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Enzimas Inmovilizadas
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Lipasa
Idioma:
En
Año:
2019
Tipo del documento:
Article