Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI)
Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on its surface. The enzyme activity was fully mainta...
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Multidisciplinary Digital Publishing Institute
2016
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Online Access: | http://hdl.handle.net/10261/142084 https://doi.org/10.3390/molecules21060751 https://doi.org/10.13039/501100003329 https://doi.org/10.13039/100007195 https://doi.org/10.13039/501100003141 https://doi.org/10.13039/501100003339 |
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ftcsic:oai:digital.csic.es:10261/142084 2024-02-11T09:57:35+01:00 Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI) Peirce, Sara Tacias-Pascacio, Veymar G. Russo, María Elena Marzocchella, Antonio Virgen-Ortíz, José J. Fernández-Lafuente, Roberto Ministerio de Economía y Competitividad (España) Università degli Studi di Napoli Federico II Consejo Nacional de Ciencia y Tecnología (México) Consejo Superior de Investigaciones Científicas (España) 2016-06-08 http://hdl.handle.net/10261/142084 https://doi.org/10.3390/molecules21060751 https://doi.org/10.13039/501100003329 https://doi.org/10.13039/100007195 https://doi.org/10.13039/501100003141 https://doi.org/10.13039/501100003339 unknown Multidisciplinary Digital Publishing Institute #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2013-41507-R doi:10.3390/molecules21060751 Molecules 21(6): 751 (2016) http://hdl.handle.net/10261/142084 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/100007195 http://dx.doi.org/10.13039/501100003141 http://dx.doi.org/10.13039/501100003339 27338317 open artículo http://purl.org/coar/resource_type/c_6501 2016 ftcsic https://doi.org/10.3390/molecules2106075110.13039/50110000332910.13039/10000719510.13039/50110000314110.13039/501100003339 2024-01-16T10:19:36Z Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on its surface. The enzyme activity was fully maintained during the coating and the thermal stability was marginally improved. The enzyme release from the support by incubation in the non-ionic detergent Triton X-100 was more difficult after the PEI-coating, suggesting that some intermolecular physical crosslinking had occurred, making this desorption more difficult. Thermal stability was marginally improved, but the stability of the OCCALB-PEI was significantly better than that of OCCALB during inactivation in mixtures of aqueous buffer and organic cosolvents. SDS-PAGE analysis of the inactivated biocatalyst showed the OCCALB released some enzyme to the medium during inactivation, and this was partially prevented by coating with PEI. This effect was obtained without preventing the possibility of reuse of the support by incubation in 2% ionic detergents. That way, this modified CALB not only has a strong anion exchange nature, while maintaining the activity, but it also shows improved stability under diverse reaction conditions without affecting the reversibility of the immobilization. We thank the support from MINECO, grant CTQ2013-41507-R. The predoctoral fellowships for Miss Peirce (Universita’ degli Studi di Napoli Federico II) and Miss Tacias-Pascacio (CONACyT, Mexico) are also gratefully recognized. Virgen-Ortíz thanks CONACyT Mexico for his Postdoctoral fellowship (No. 263815). We acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI). Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Triton ENVELOPE(-55.615,-55.615,49.517,49.517) Molecules 21 6 751 |
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Digital.CSIC (Spanish National Research Council) |
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ftcsic |
language |
unknown |
description |
Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on its surface. The enzyme activity was fully maintained during the coating and the thermal stability was marginally improved. The enzyme release from the support by incubation in the non-ionic detergent Triton X-100 was more difficult after the PEI-coating, suggesting that some intermolecular physical crosslinking had occurred, making this desorption more difficult. Thermal stability was marginally improved, but the stability of the OCCALB-PEI was significantly better than that of OCCALB during inactivation in mixtures of aqueous buffer and organic cosolvents. SDS-PAGE analysis of the inactivated biocatalyst showed the OCCALB released some enzyme to the medium during inactivation, and this was partially prevented by coating with PEI. This effect was obtained without preventing the possibility of reuse of the support by incubation in 2% ionic detergents. That way, this modified CALB not only has a strong anion exchange nature, while maintaining the activity, but it also shows improved stability under diverse reaction conditions without affecting the reversibility of the immobilization. We thank the support from MINECO, grant CTQ2013-41507-R. The predoctoral fellowships for Miss Peirce (Universita’ degli Studi di Napoli Federico II) and Miss Tacias-Pascacio (CONACyT, Mexico) are also gratefully recognized. Virgen-Ortíz thanks CONACyT Mexico for his Postdoctoral fellowship (No. 263815). We acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI). |
author2 |
Ministerio de Economía y Competitividad (España) Università degli Studi di Napoli Federico II Consejo Nacional de Ciencia y Tecnología (México) Consejo Superior de Investigaciones Científicas (España) |
format |
Article in Journal/Newspaper |
author |
Peirce, Sara Tacias-Pascacio, Veymar G. Russo, María Elena Marzocchella, Antonio Virgen-Ortíz, José J. Fernández-Lafuente, Roberto |
spellingShingle |
Peirce, Sara Tacias-Pascacio, Veymar G. Russo, María Elena Marzocchella, Antonio Virgen-Ortíz, José J. Fernández-Lafuente, Roberto Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI) |
author_facet |
Peirce, Sara Tacias-Pascacio, Veymar G. Russo, María Elena Marzocchella, Antonio Virgen-Ortíz, José J. Fernández-Lafuente, Roberto |
author_sort |
Peirce, Sara |
title |
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI) |
title_short |
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI) |
title_full |
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI) |
title_fullStr |
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI) |
title_full_unstemmed |
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI) |
title_sort |
stabilization of candida antarctica lipase b (calb) immobilized on octyl agarose by treatment with polyethyleneimine (pei) |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2016 |
url |
http://hdl.handle.net/10261/142084 https://doi.org/10.3390/molecules21060751 https://doi.org/10.13039/501100003329 https://doi.org/10.13039/100007195 https://doi.org/10.13039/501100003141 https://doi.org/10.13039/501100003339 |
long_lat |
ENVELOPE(-55.615,-55.615,49.517,49.517) |
geographic |
Triton |
geographic_facet |
Triton |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
#PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2013-41507-R doi:10.3390/molecules21060751 Molecules 21(6): 751 (2016) http://hdl.handle.net/10261/142084 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/100007195 http://dx.doi.org/10.13039/501100003141 http://dx.doi.org/10.13039/501100003339 27338317 |
op_rights |
open |
op_doi |
https://doi.org/10.3390/molecules2106075110.13039/50110000332910.13039/10000719510.13039/50110000314110.13039/501100003339 |
container_title |
Molecules |
container_volume |
21 |
container_issue |
6 |
container_start_page |
751 |
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1790593135286419456 |