Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis.
Abstract Very recently, several successful enzymatic processes performed with mechanical activation have been disclosed; that is, despite the mechanical stress caused by High‐Speed Ball‐Milling, immobilized enzymes can retain activity. In the present study, the effect of thermal and mechanical stres...
Published in: | ChemCatChem |
---|---|
Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2019
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1002/cctc.201901714 https://onlinelibrary.wiley.com/doi/pdf/10.1002/cctc.201901714 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/cctc.201901714 |
id |
crwiley:10.1002/cctc.201901714 |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1002/cctc.201901714 2024-03-17T08:54:05+00:00 Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis. Pérez‐Venegas, Mario Tellez‐Cruz, Miriam M. Solorza‐Feria, Omar López‐Munguía, Agustín Castillo, Edmundo Juaristi, Eusebio 2019 http://dx.doi.org/10.1002/cctc.201901714 https://onlinelibrary.wiley.com/doi/pdf/10.1002/cctc.201901714 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/cctc.201901714 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor ChemCatChem volume 12, issue 3, page 803-811 ISSN 1867-3880 1867-3899 Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Catalysis journal-article 2019 crwiley https://doi.org/10.1002/cctc.201901714 2024-02-22T00:25:16Z Abstract Very recently, several successful enzymatic processes performed with mechanical activation have been disclosed; that is, despite the mechanical stress caused by High‐Speed Ball‐Milling, immobilized enzymes can retain activity. In the present study, the effect of thermal and mechanical stress was examined as potential inducers of enzymatic denaturation, when using either free, immobilized, or ground immobilized enzyme. The recorded observations show a remarkable stability of ground immobilized enzyme. Moreover, ground biocatalyst turns out to exhibit an increase of one order of magnitude in the efficiency of the catalytic process, maintaining excellent enantiodiscrimination, without significant activity loss even after four milling cycles. These observations rule out enzyme inactivation as direct consequence of the milling process. Additionally, boosted enzyme efficiency was used to optimize a relatively inefficient chiral amine resolution reaction, achieving a 25 % faster biotransformation (in 45 min) and yielding essentially enantiopure products ( ee >99%, E >500). Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library ChemCatChem 12 3 803 811 |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
topic |
Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Catalysis |
spellingShingle |
Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Catalysis Pérez‐Venegas, Mario Tellez‐Cruz, Miriam M. Solorza‐Feria, Omar López‐Munguía, Agustín Castillo, Edmundo Juaristi, Eusebio Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis. |
topic_facet |
Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Catalysis |
description |
Abstract Very recently, several successful enzymatic processes performed with mechanical activation have been disclosed; that is, despite the mechanical stress caused by High‐Speed Ball‐Milling, immobilized enzymes can retain activity. In the present study, the effect of thermal and mechanical stress was examined as potential inducers of enzymatic denaturation, when using either free, immobilized, or ground immobilized enzyme. The recorded observations show a remarkable stability of ground immobilized enzyme. Moreover, ground biocatalyst turns out to exhibit an increase of one order of magnitude in the efficiency of the catalytic process, maintaining excellent enantiodiscrimination, without significant activity loss even after four milling cycles. These observations rule out enzyme inactivation as direct consequence of the milling process. Additionally, boosted enzyme efficiency was used to optimize a relatively inefficient chiral amine resolution reaction, achieving a 25 % faster biotransformation (in 45 min) and yielding essentially enantiopure products ( ee >99%, E >500). |
format |
Article in Journal/Newspaper |
author |
Pérez‐Venegas, Mario Tellez‐Cruz, Miriam M. Solorza‐Feria, Omar López‐Munguía, Agustín Castillo, Edmundo Juaristi, Eusebio |
author_facet |
Pérez‐Venegas, Mario Tellez‐Cruz, Miriam M. Solorza‐Feria, Omar López‐Munguía, Agustín Castillo, Edmundo Juaristi, Eusebio |
author_sort |
Pérez‐Venegas, Mario |
title |
Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis. |
title_short |
Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis. |
title_full |
Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis. |
title_fullStr |
Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis. |
title_full_unstemmed |
Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis. |
title_sort |
thermal and mechanical stability of immobilized candida antarctica lipase b: an approximation to mechanochemical energetics in enzyme catalysis. |
publisher |
Wiley |
publishDate |
2019 |
url |
http://dx.doi.org/10.1002/cctc.201901714 https://onlinelibrary.wiley.com/doi/pdf/10.1002/cctc.201901714 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/cctc.201901714 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ChemCatChem volume 12, issue 3, page 803-811 ISSN 1867-3880 1867-3899 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/cctc.201901714 |
container_title |
ChemCatChem |
container_volume |
12 |
container_issue |
3 |
container_start_page |
803 |
op_container_end_page |
811 |
_version_ |
1793770914919219200 |