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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Online Access: | http://hdl.handle.net/11588/637542 https://doi.org/10.3390/molecules21060751 http://www.mdpi.com/1420-3049/21/6/751/pdf |
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ftunivnapoliiris:oai:www.iris.unina.it:11588/637542 2024-09-09T19:02:33+00:00 Stabilization of Candida antarctica Lipase B (CALB) immobilized on octyl agarose by treatment with polyethyleneimine (PEI) PEIRCE, SARA MARZOCCHELLA, ANTONIO Tacias Pascacio, Veymar G. Russo, Maria Elena Virgen Ortíz, José J Fernandez Lafuente, Roberto Peirce, Sara Tacias Pascacio, Veymar G. Russo, Maria Elena Marzocchella, Antonio Virgen Ortíz, José J Fernandez Lafuente, Roberto 2016 http://hdl.handle.net/11588/637542 https://doi.org/10.3390/molecules21060751 http://www.mdpi.com/1420-3049/21/6/751/pdf eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000378757600077 volume:21 issue:6 firstpage:751 journal:MOLECULES http://hdl.handle.net/11588/637542 doi:10.3390/molecules21060751 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84976386594 http://www.mdpi.com/1420-3049/21/6/751/pdf Enzyme physical intermolecular crosslinking Enzyme stabilization Interfacial adsorption PEI modification Reversible immobilization Organic Chemistry info:eu-repo/semantics/article 2016 ftunivnapoliiris https://doi.org/10.3390/molecules21060751 2024-06-17T15:19:32Z 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. © 2016 by the authors; licensee MDPI. Article in Journal/Newspaper Antarc* Antarctica IRIS Università degli Studi di Napoli Federico II Triton ENVELOPE(-55.615,-55.615,49.517,49.517) Molecules 21 6 751 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
Enzyme physical intermolecular crosslinking Enzyme stabilization Interfacial adsorption PEI modification Reversible immobilization Organic Chemistry |
spellingShingle |
Enzyme physical intermolecular crosslinking Enzyme stabilization Interfacial adsorption PEI modification Reversible immobilization Organic Chemistry PEIRCE, SARA MARZOCCHELLA, ANTONIO Tacias Pascacio, Veymar G. Russo, Maria Elena Virgen Ortíz, José J Fernandez Lafuente, Roberto Stabilization of Candida antarctica Lipase B (CALB) immobilized on octyl agarose by treatment with polyethyleneimine (PEI) |
topic_facet |
Enzyme physical intermolecular crosslinking Enzyme stabilization Interfacial adsorption PEI modification Reversible immobilization Organic Chemistry |
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. © 2016 by the authors; licensee MDPI. |
author2 |
Peirce, Sara Tacias Pascacio, Veymar G. Russo, Maria Elena Marzocchella, Antonio Virgen Ortíz, José J Fernandez Lafuente, Roberto |
format |
Article in Journal/Newspaper |
author |
PEIRCE, SARA MARZOCCHELLA, ANTONIO Tacias Pascacio, Veymar G. Russo, Maria Elena Virgen Ortíz, José J Fernandez Lafuente, Roberto |
author_facet |
PEIRCE, SARA MARZOCCHELLA, ANTONIO Tacias Pascacio, Veymar G. Russo, Maria Elena Virgen Ortíz, José J Fernandez 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) |
publishDate |
2016 |
url |
http://hdl.handle.net/11588/637542 https://doi.org/10.3390/molecules21060751 http://www.mdpi.com/1420-3049/21/6/751/pdf |
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 |
info:eu-repo/semantics/altIdentifier/wos/WOS:000378757600077 volume:21 issue:6 firstpage:751 journal:MOLECULES http://hdl.handle.net/11588/637542 doi:10.3390/molecules21060751 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84976386594 http://www.mdpi.com/1420-3049/21/6/751/pdf |
op_doi |
https://doi.org/10.3390/molecules21060751 |
container_title |
Molecules |
container_volume |
21 |
container_issue |
6 |
container_start_page |
751 |
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1809816628004651008 |