Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification
Candida antarctica lipase B (CalB) enzyme was encapsulated and cross-linked by silica matrix to enhance its thermal stability and reusability, and demonstrated an enzymatic ability for rapid hydrolysis and esterification. Silica encapsulated CalB particles (Si-E-CPs) and silica cross-linked CalB par...
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ftmdpi:oai:mdpi.com:/1422-0067/23/5/2459/ 2023-08-20T04:02:22+02:00 Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification Min Song Jeong-Ho Chang agris 2022-02-23 application/pdf https://doi.org/10.3390/ijms23052459 EN eng Multidisciplinary Digital Publishing Institute Materials Science https://dx.doi.org/10.3390/ijms23052459 https://creativecommons.org/licenses/by/4.0/ International Journal of Molecular Sciences; Volume 23; Issue 5; Pages: 2459 thermal stability reusability silica encapsulation cross-linking CalB enzyme benzyl benzoate Text 2022 ftmdpi https://doi.org/10.3390/ijms23052459 2023-08-01T04:15:51Z Candida antarctica lipase B (CalB) enzyme was encapsulated and cross-linked by silica matrix to enhance its thermal stability and reusability, and demonstrated an enzymatic ability for rapid hydrolysis and esterification. Silica encapsulated CalB particles (Si-E-CPs) and silica cross-linked CalB particles (Si-CL-CPs) were prepared as a function of TEOS concentration. The particle size analysis, thermal stability, catalytic activity in different pHs, and reusability of Si-E-CPs and Si-CL-CPs were demonstrated. Furthermore, the determination of the CalB enzyme in Si-E-CPs and Si-CL-CPs was achieved by Bradford assay and TGA analysis. Enzymatic hydrolysis was performed against the p-nitrophenyl butyrate and the catalytic parameters (Km, Vmax, and Kcat) were calculated by the Michaelis–Menten equation and a Lineweaver–Burk plot. Moreover, enzymatic synthesis for benzyl benzoate was demonstrated by esterification with an acyl donor of benzoic acid and two acyl donors of benzoic anhydride. Although the conversion efficiency of Si-CL-CPs was not much higher than that of native CalB, it has an efficiency of 91% compared to native CalB and is expected to be very useful because it has high thermal and pH stability and excellent reusability. Text Antarc* Antarctica MDPI Open Access Publishing International Journal of Molecular Sciences 23 5 2459 |
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MDPI Open Access Publishing |
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ftmdpi |
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English |
topic |
thermal stability reusability silica encapsulation cross-linking CalB enzyme benzyl benzoate |
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thermal stability reusability silica encapsulation cross-linking CalB enzyme benzyl benzoate Min Song Jeong-Ho Chang Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification |
topic_facet |
thermal stability reusability silica encapsulation cross-linking CalB enzyme benzyl benzoate |
description |
Candida antarctica lipase B (CalB) enzyme was encapsulated and cross-linked by silica matrix to enhance its thermal stability and reusability, and demonstrated an enzymatic ability for rapid hydrolysis and esterification. Silica encapsulated CalB particles (Si-E-CPs) and silica cross-linked CalB particles (Si-CL-CPs) were prepared as a function of TEOS concentration. The particle size analysis, thermal stability, catalytic activity in different pHs, and reusability of Si-E-CPs and Si-CL-CPs were demonstrated. Furthermore, the determination of the CalB enzyme in Si-E-CPs and Si-CL-CPs was achieved by Bradford assay and TGA analysis. Enzymatic hydrolysis was performed against the p-nitrophenyl butyrate and the catalytic parameters (Km, Vmax, and Kcat) were calculated by the Michaelis–Menten equation and a Lineweaver–Burk plot. Moreover, enzymatic synthesis for benzyl benzoate was demonstrated by esterification with an acyl donor of benzoic acid and two acyl donors of benzoic anhydride. Although the conversion efficiency of Si-CL-CPs was not much higher than that of native CalB, it has an efficiency of 91% compared to native CalB and is expected to be very useful because it has high thermal and pH stability and excellent reusability. |
format |
Text |
author |
Min Song Jeong-Ho Chang |
author_facet |
Min Song Jeong-Ho Chang |
author_sort |
Min Song |
title |
Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification |
title_short |
Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification |
title_full |
Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification |
title_fullStr |
Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification |
title_full_unstemmed |
Thermally Stable and Reusable Ceramic Encapsulated and Cross-Linked CalB Enzyme Particles for Rapid Hydrolysis and Esterification |
title_sort |
thermally stable and reusable ceramic encapsulated and cross-linked calb enzyme particles for rapid hydrolysis and esterification |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2022 |
url |
https://doi.org/10.3390/ijms23052459 |
op_coverage |
agris |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
International Journal of Molecular Sciences; Volume 23; Issue 5; Pages: 2459 |
op_relation |
Materials Science https://dx.doi.org/10.3390/ijms23052459 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/ijms23052459 |
container_title |
International Journal of Molecular Sciences |
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23 |
container_issue |
5 |
container_start_page |
2459 |
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1774712795825176576 |