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: Escudero, Alfonso, de los Ríos, Antonia Pérez, Godínez, Carlos, Tomás, Francisca, Hernández-Fernández, Francisco José
Format: Text
Language:English
Published: MDPI 2020
Subjects:
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397261/
http://www.ncbi.nlm.nih.gov/pubmed/32679875
https://doi.org/10.3390/molecules25143233
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spelling ftpubmed:oai:pubmedcentral.nih.gov:7397261 2023-05-15T14:04:13+02:00 Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B Escudero, Alfonso de los Ríos, Antonia Pérez Godínez, Carlos Tomás, Francisca Hernández-Fernández, Francisco José 2020-07-15 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397261/ http://www.ncbi.nlm.nih.gov/pubmed/32679875 https://doi.org/10.3390/molecules25143233 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397261/ http://www.ncbi.nlm.nih.gov/pubmed/32679875 http://dx.doi.org/10.3390/molecules25143233 © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Molecules Article Text 2020 ftpubmed https://doi.org/10.3390/molecules25143233 2020-08-23T00:18:20Z 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. Text Antarc* Antarctica PubMed Central (PMC) Molecules 25 14 3233
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Article
spellingShingle Article
Escudero, Alfonso
de los Ríos, Antonia Pérez
Godínez, Carlos
Tomás, Francisca
Hernández-Fernández, Francisco José
Immobilization in Ionogel: A New Way to Improve the Activity and Stability of Candida antarctica Lipase B
topic_facet Article
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 Text
author Escudero, Alfonso
de los Ríos, Antonia Pérez
Godínez, Carlos
Tomás, Francisca
Hernández-Fernández, Francisco José
author_facet Escudero, Alfonso
de los Ríos, Antonia Pérez
Godínez, Carlos
Tomás, Francisca
Hernández-Fernández, Francisco José
author_sort Escudero, Alfonso
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
publishDate 2020
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397261/
http://www.ncbi.nlm.nih.gov/pubmed/32679875
https://doi.org/10.3390/molecules25143233
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Molecules
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397261/
http://www.ncbi.nlm.nih.gov/pubmed/32679875
http://dx.doi.org/10.3390/molecules25143233
op_rights © 2020 by the authors.
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
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container_title Molecules
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