The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support
Abstract In this article, we have analyzed the interactions between enzyme crowding on a given support and its chemical modification (ethylenediamine modification via the carbodiimide route and picryl sulfonic (TNBS) modification of the primary amino groups) on the enzyme activity and stability. Lip...
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crwiley:10.1002/btpr.3394 2024-09-15T17:48:45+00:00 The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support Abellanas‐Perez, Pedro Carballares, Diego Rocha‐Martin, Javier Fernandez‐Lafuente, Roberto Agencia Estatal de Investigación 2023 http://dx.doi.org/10.1002/btpr.3394 en eng Wiley http://creativecommons.org/licenses/by-nc/4.0/ Biotechnology Progress volume 40, issue 1 ISSN 8756-7938 1520-6033 journal-article 2023 crwiley https://doi.org/10.1002/btpr.3394 2024-08-20T04:17:23Z Abstract In this article, we have analyzed the interactions between enzyme crowding on a given support and its chemical modification (ethylenediamine modification via the carbodiimide route and picryl sulfonic (TNBS) modification of the primary amino groups) on the enzyme activity and stability. Lipase from Thermomyces lanuginosus (TLL) and lipase B from Candida antarctica (CALB) were immobilized on octyl‐agarose beads at two very different enzyme loadings, one of them exceeding the capacity of the support, one well under this capacity. Chemical modifications of the highly loaded and lowly loaded biocatalysts gave very different results in terms of activity and stability, which could increase or decrease enzyme activity depending on the enzyme support loading. For example, both lowly loaded biocatalysts increased their activity after modification while the effect was the opposite for the highly loaded biocatalysts. Additionally, the modification with TNBS of highly loaded CALB biocatalyst increased its stability while decrease the activity. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology Progress |
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Abstract In this article, we have analyzed the interactions between enzyme crowding on a given support and its chemical modification (ethylenediamine modification via the carbodiimide route and picryl sulfonic (TNBS) modification of the primary amino groups) on the enzyme activity and stability. Lipase from Thermomyces lanuginosus (TLL) and lipase B from Candida antarctica (CALB) were immobilized on octyl‐agarose beads at two very different enzyme loadings, one of them exceeding the capacity of the support, one well under this capacity. Chemical modifications of the highly loaded and lowly loaded biocatalysts gave very different results in terms of activity and stability, which could increase or decrease enzyme activity depending on the enzyme support loading. For example, both lowly loaded biocatalysts increased their activity after modification while the effect was the opposite for the highly loaded biocatalysts. Additionally, the modification with TNBS of highly loaded CALB biocatalyst increased its stability while decrease the activity. |
author2 |
Agencia Estatal de Investigación |
format |
Article in Journal/Newspaper |
author |
Abellanas‐Perez, Pedro Carballares, Diego Rocha‐Martin, Javier Fernandez‐Lafuente, Roberto |
spellingShingle |
Abellanas‐Perez, Pedro Carballares, Diego Rocha‐Martin, Javier Fernandez‐Lafuente, Roberto The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support |
author_facet |
Abellanas‐Perez, Pedro Carballares, Diego Rocha‐Martin, Javier Fernandez‐Lafuente, Roberto |
author_sort |
Abellanas‐Perez, Pedro |
title |
The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support |
title_short |
The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support |
title_full |
The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support |
title_fullStr |
The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support |
title_full_unstemmed |
The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support |
title_sort |
effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support |
publisher |
Wiley |
publishDate |
2023 |
url |
http://dx.doi.org/10.1002/btpr.3394 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology Progress volume 40, issue 1 ISSN 8756-7938 1520-6033 |
op_rights |
http://creativecommons.org/licenses/by-nc/4.0/ |
op_doi |
https://doi.org/10.1002/btpr.3394 |
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Biotechnology Progress |
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1810290261269413888 |