Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System
A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microsco...
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ftmdpi:oai:mdpi.com:/2073-4344/7/1/14/ 2023-08-20T04:02:34+02:00 Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System Jakub Zdarta Lukasz Klapiszewski Artur Jedrzak Marek Nowicki Dariusz Moszynski Teofil Jesionowski 2016-12-31 application/pdf https://doi.org/10.3390/catal7010014 EN eng Multidisciplinary Digital Publishing Institute Biocatalysis https://dx.doi.org/10.3390/catal7010014 https://creativecommons.org/licenses/by/4.0/ Catalysts; Volume 7; Issue 1; Pages: 14 silica-lignin matrix lipase immobilized enzymes enzyme activity and stability Text 2016 ftmdpi https://doi.org/10.3390/catal7010014 2023-07-31T21:01:15Z A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM), as well as the determination of changes in porous structure parameters, confirmed the effective immobilization of the enzyme on the surface of the composite matrix. Based on a hydrolysis reaction, a determination was made of the retention of activity of the immobilized lipase, found to be 92% of that of the native enzyme. Immobilization on a silica-lignin matrix produces systems with maximum activity at pH = 8 and at a temperature of 40 °C. The immobilized enzyme exhibited increased thermal and chemical stability and retained more than 80% of its activity after 20 reaction cycles. Moreover immobilized lipase exhibited over 80% of its activity at pH range 7–9 and temperature from 30 °C to 60 °C, while native Candida antarctica lipase B (CALB) exhibited the same only at pH = 7 and temperature of 30 °C. Text Antarc* Antarctica MDPI Open Access Publishing Catalysts 7 12 14 |
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Open Polar |
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MDPI Open Access Publishing |
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English |
topic |
silica-lignin matrix lipase immobilized enzymes enzyme activity and stability |
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silica-lignin matrix lipase immobilized enzymes enzyme activity and stability Jakub Zdarta Lukasz Klapiszewski Artur Jedrzak Marek Nowicki Dariusz Moszynski Teofil Jesionowski Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System |
topic_facet |
silica-lignin matrix lipase immobilized enzymes enzyme activity and stability |
description |
A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM), as well as the determination of changes in porous structure parameters, confirmed the effective immobilization of the enzyme on the surface of the composite matrix. Based on a hydrolysis reaction, a determination was made of the retention of activity of the immobilized lipase, found to be 92% of that of the native enzyme. Immobilization on a silica-lignin matrix produces systems with maximum activity at pH = 8 and at a temperature of 40 °C. The immobilized enzyme exhibited increased thermal and chemical stability and retained more than 80% of its activity after 20 reaction cycles. Moreover immobilized lipase exhibited over 80% of its activity at pH range 7–9 and temperature from 30 °C to 60 °C, while native Candida antarctica lipase B (CALB) exhibited the same only at pH = 7 and temperature of 30 °C. |
format |
Text |
author |
Jakub Zdarta Lukasz Klapiszewski Artur Jedrzak Marek Nowicki Dariusz Moszynski Teofil Jesionowski |
author_facet |
Jakub Zdarta Lukasz Klapiszewski Artur Jedrzak Marek Nowicki Dariusz Moszynski Teofil Jesionowski |
author_sort |
Jakub Zdarta |
title |
Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System |
title_short |
Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System |
title_full |
Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System |
title_fullStr |
Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System |
title_full_unstemmed |
Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System |
title_sort |
lipase b from candida antarctica immobilized on a silica-lignin matrix as a stable and reusable biocatalytic system |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2016 |
url |
https://doi.org/10.3390/catal7010014 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Catalysts; Volume 7; Issue 1; Pages: 14 |
op_relation |
Biocatalysis https://dx.doi.org/10.3390/catal7010014 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/catal7010014 |
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Catalysts |
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7 |
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12 |
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14 |
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1774713078525460480 |