CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability
In this study, an immobilization strategy for magnetic cross-linking enzyme aggregates of lipase B from Candida antarctica (CALB) was developed and investigated. Magnetic particles were prepared by conventional co-precipitation. The magnetic nanoparticles were modified with 3-aminopropyltriethoxysil...
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ftmdpi:oai:mdpi.com:/1420-3049/24/3/490/ 2023-08-20T04:00:23+02:00 CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability Xiu Xing Jun-Qi Jia Jing-Fan Zhang Zi-Wen Zhou Jun Li Na Wang Xiao-Qi Yu agris 2019-01-30 application/pdf https://doi.org/10.3390/molecules24030490 EN eng Multidisciplinary Digital Publishing Institute Chemical Biology https://dx.doi.org/10.3390/molecules24030490 https://creativecommons.org/licenses/by/4.0/ Molecules; Volume 24; Issue 3; Pages: 490 CALB magnetic nanoparticles cross-linked enzyme aggregates resolution secondary alcohols Text 2019 ftmdpi https://doi.org/10.3390/molecules24030490 2023-07-31T22:00:32Z In this study, an immobilization strategy for magnetic cross-linking enzyme aggregates of lipase B from Candida antarctica (CALB) was developed and investigated. Magnetic particles were prepared by conventional co-precipitation. The magnetic nanoparticles were modified with 3-aminopropyltriethoxysilane (APTES) to obtain surface amino-functionalized magnetic nanoparticles (APTES–Fe3O4) as immobilization materials. Glutaraldehyde was used as a crosslinker to covalently bind CALB to APTES–Fe3O4. The optimal conditions of immobilization of lipase and resolution of racemic 1-phenylethanol were investigated. Under optimal conditions, esters could be obtained with conversion of 50%, enantiomeric excess of product (eep) > 99%, enantiomeric excess of substrate (ees) > 99%, and enantiomeric ratio (E) > 1000. The magnetic CALB CLEAs were successfully used for enzymatic kinetic resolution of fifteen secondary alcohols. Compared with Novozym 435, the magnetic CALB CLEAs exhibited a better enantioselectivity for most substrates. The conversion was still greater than 49% after the magnetic CALB CLEAs had been reused 10 times in a 48 h reaction cycle; both ees and eep were close to 99%. Furthermore, there was little decrease in catalytic activity and enantioselectivity after being stored at −20 °C for 90 days. Text Antarc* Antarctica MDPI Open Access Publishing Molecules 24 3 490 |
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Open Polar |
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MDPI Open Access Publishing |
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ftmdpi |
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English |
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CALB magnetic nanoparticles cross-linked enzyme aggregates resolution secondary alcohols |
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CALB magnetic nanoparticles cross-linked enzyme aggregates resolution secondary alcohols Xiu Xing Jun-Qi Jia Jing-Fan Zhang Zi-Wen Zhou Jun Li Na Wang Xiao-Qi Yu CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability |
topic_facet |
CALB magnetic nanoparticles cross-linked enzyme aggregates resolution secondary alcohols |
description |
In this study, an immobilization strategy for magnetic cross-linking enzyme aggregates of lipase B from Candida antarctica (CALB) was developed and investigated. Magnetic particles were prepared by conventional co-precipitation. The magnetic nanoparticles were modified with 3-aminopropyltriethoxysilane (APTES) to obtain surface amino-functionalized magnetic nanoparticles (APTES–Fe3O4) as immobilization materials. Glutaraldehyde was used as a crosslinker to covalently bind CALB to APTES–Fe3O4. The optimal conditions of immobilization of lipase and resolution of racemic 1-phenylethanol were investigated. Under optimal conditions, esters could be obtained with conversion of 50%, enantiomeric excess of product (eep) > 99%, enantiomeric excess of substrate (ees) > 99%, and enantiomeric ratio (E) > 1000. The magnetic CALB CLEAs were successfully used for enzymatic kinetic resolution of fifteen secondary alcohols. Compared with Novozym 435, the magnetic CALB CLEAs exhibited a better enantioselectivity for most substrates. The conversion was still greater than 49% after the magnetic CALB CLEAs had been reused 10 times in a 48 h reaction cycle; both ees and eep were close to 99%. Furthermore, there was little decrease in catalytic activity and enantioselectivity after being stored at −20 °C for 90 days. |
format |
Text |
author |
Xiu Xing Jun-Qi Jia Jing-Fan Zhang Zi-Wen Zhou Jun Li Na Wang Xiao-Qi Yu |
author_facet |
Xiu Xing Jun-Qi Jia Jing-Fan Zhang Zi-Wen Zhou Jun Li Na Wang Xiao-Qi Yu |
author_sort |
Xiu Xing |
title |
CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability |
title_short |
CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability |
title_full |
CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability |
title_fullStr |
CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability |
title_full_unstemmed |
CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability |
title_sort |
calb immobilized onto magnetic nanoparticles for efficient kinetic resolution of racemic secondary alcohols: long-term stability and reusability |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2019 |
url |
https://doi.org/10.3390/molecules24030490 |
op_coverage |
agris |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Molecules; Volume 24; Issue 3; Pages: 490 |
op_relation |
Chemical Biology https://dx.doi.org/10.3390/molecules24030490 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/molecules24030490 |
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Molecules |
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24 |
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3 |
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490 |
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1774717870098350080 |