Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B

New Candida antarctica lipase B derivatives with higher activity than the free enzyme were obtained by occlusion in an organogel of an ionic liquid (ionogel) based on the ionic liquid [Omim][PF 6 ] and polyvinyl chloride. The inclusion of glutaraldehyde as a crosslinker improved the properties of th...

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Published in:Molecules
Main Authors: Alfonso Escudero, Antonia Pérez de los Ríos, Carlos Godínez, Francisca Tomás, Francisco José Hernández-Fernández
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2020
Subjects:
Online Access:https://doi.org/10.3390/molecules25143233
https://doaj.org/article/386c923abc3c43e98bd93c649d242610
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spelling ftdoajarticles:oai:doaj.org/article:386c923abc3c43e98bd93c649d242610 2023-05-15T13:54:42+02:00 Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B Alfonso Escudero Antonia Pérez de los Ríos Carlos Godínez Francisca Tomás Francisco José Hernández-Fernández 2020-07-01T00:00:00Z https://doi.org/10.3390/molecules25143233 https://doaj.org/article/386c923abc3c43e98bd93c649d242610 EN eng MDPI AG https://www.mdpi.com/1420-3049/25/14/3233 https://doaj.org/toc/1420-3049 doi:10.3390/molecules25143233 1420-3049 https://doaj.org/article/386c923abc3c43e98bd93c649d242610 Molecules, Vol 25, Iss 3233, p 3233 (2020) enzymatic immobilization organogels ionogels ionic liquid ester synthesis enzyme Organic chemistry QD241-441 article 2020 ftdoajarticles https://doi.org/10.3390/molecules25143233 2022-12-31T15:02:07Z New Candida antarctica lipase B derivatives with higher activity than the free enzyme were obtained by occlusion in an organogel of an ionic liquid (ionogel) based on the ionic liquid [Omim][PF 6 ] and polyvinyl chloride. The inclusion of glutaraldehyde as a crosslinker improved the properties of the ionogel, allowing the enzymatic derivative to reach 5-fold higher activity than the free enzyme and also allowing it to be reused at 70 °C. The new methodology allows enzymatic derivatives to be designed by changing the ionic liquid, thus providing a suitable microenvironment for the enzyme. The ionic liquid may act on substrates to increase their local concentration, while reducing water activity in the enzyme’s microenvironment. All this allows the activity and selectivity of the enzyme to be improved and greener processes to be developed. The chemical composition and morphology of the ionogel were also studied by scanning electron microscopy–energy dispersive X-ray spectroscopy, finding that porosity, which was related with the chemical composition, was a key factor for the enzyme activity. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Molecules 25 14 3233
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic enzymatic immobilization
organogels
ionogels
ionic liquid
ester synthesis
enzyme
Organic chemistry
QD241-441
spellingShingle enzymatic immobilization
organogels
ionogels
ionic liquid
ester synthesis
enzyme
Organic chemistry
QD241-441
Alfonso Escudero
Antonia Pérez de los Ríos
Carlos Godínez
Francisca Tomás
Francisco José Hernández-Fernández
Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B
topic_facet enzymatic immobilization
organogels
ionogels
ionic liquid
ester synthesis
enzyme
Organic chemistry
QD241-441
description New Candida antarctica lipase B derivatives with higher activity than the free enzyme were obtained by occlusion in an organogel of an ionic liquid (ionogel) based on the ionic liquid [Omim][PF 6 ] and polyvinyl chloride. The inclusion of glutaraldehyde as a crosslinker improved the properties of the ionogel, allowing the enzymatic derivative to reach 5-fold higher activity than the free enzyme and also allowing it to be reused at 70 °C. The new methodology allows enzymatic derivatives to be designed by changing the ionic liquid, thus providing a suitable microenvironment for the enzyme. The ionic liquid may act on substrates to increase their local concentration, while reducing water activity in the enzyme’s microenvironment. All this allows the activity and selectivity of the enzyme to be improved and greener processes to be developed. The chemical composition and morphology of the ionogel were also studied by scanning electron microscopy–energy dispersive X-ray spectroscopy, finding that porosity, which was related with the chemical composition, was a key factor for the enzyme activity.
format Article in Journal/Newspaper
author Alfonso Escudero
Antonia Pérez de los Ríos
Carlos Godínez
Francisca Tomás
Francisco José Hernández-Fernández
author_facet Alfonso Escudero
Antonia Pérez de los Ríos
Carlos Godínez
Francisca Tomás
Francisco José Hernández-Fernández
author_sort Alfonso Escudero
title Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B
title_short Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B
title_full Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B
title_fullStr Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B
title_full_unstemmed Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B
title_sort immobilization in ionogel: a new way to improve the activity and stability of candida antarctica lipase b
publisher MDPI AG
publishDate 2020
url https://doi.org/10.3390/molecules25143233
https://doaj.org/article/386c923abc3c43e98bd93c649d242610
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Molecules, Vol 25, Iss 3233, p 3233 (2020)
op_relation https://www.mdpi.com/1420-3049/25/14/3233
https://doaj.org/toc/1420-3049
doi:10.3390/molecules25143233
1420-3049
https://doaj.org/article/386c923abc3c43e98bd93c649d242610
op_doi https://doi.org/10.3390/molecules25143233
container_title Molecules
container_volume 25
container_issue 14
container_start_page 3233
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