Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica
Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl‐agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobi...
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Online Access: | http://dx.doi.org/10.1002/btpr.2735 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.2735 http://onlinelibrary.wiley.com/wol1/doi/10.1002/btpr.2735/fullpdf |
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crwiley:10.1002/btpr.2735 2024-09-15T17:47:08+00:00 Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica Arana‐Peña, Sara Lokha, Yuliya Fernández‐Lafuente, Roberto Departamento Administrativo de Ciencia, Tecnología e Innovación Ministerio de Economía y Competitividad Departamento Administrativo de Ciencia, Tecnología e Innovación 2018 http://dx.doi.org/10.1002/btpr.2735 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.2735 http://onlinelibrary.wiley.com/wol1/doi/10.1002/btpr.2735/fullpdf en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology Progress volume 35, issue 1 ISSN 8756-7938 1520-6033 journal-article 2018 crwiley https://doi.org/10.1002/btpr.2735 2024-08-27T04:31:59Z Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl‐agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p‐nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl‐CALA was less stable than octyl‐CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl‐CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl‐CALA permitted some stabilization. While octyl‐CALA was more active vs. pNPB, octyl‐CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog ., 35: e2735, 2019 Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology Progress 35 1 e2735 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl‐agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p‐nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl‐CALA was less stable than octyl‐CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl‐CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl‐CALA permitted some stabilization. While octyl‐CALA was more active vs. pNPB, octyl‐CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog ., 35: e2735, 2019 |
author2 |
Departamento Administrativo de Ciencia, Tecnología e Innovación Ministerio de Economía y Competitividad Departamento Administrativo de Ciencia, Tecnología e Innovación |
format |
Article in Journal/Newspaper |
author |
Arana‐Peña, Sara Lokha, Yuliya Fernández‐Lafuente, Roberto |
spellingShingle |
Arana‐Peña, Sara Lokha, Yuliya Fernández‐Lafuente, Roberto Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica |
author_facet |
Arana‐Peña, Sara Lokha, Yuliya Fernández‐Lafuente, Roberto |
author_sort |
Arana‐Peña, Sara |
title |
Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica |
title_short |
Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica |
title_full |
Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica |
title_fullStr |
Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica |
title_full_unstemmed |
Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica |
title_sort |
immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from candida antarctica (novocor adl): comparison with immobilized lipase b from candida antarctica |
publisher |
Wiley |
publishDate |
2018 |
url |
http://dx.doi.org/10.1002/btpr.2735 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.2735 http://onlinelibrary.wiley.com/wol1/doi/10.1002/btpr.2735/fullpdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology Progress volume 35, issue 1 ISSN 8756-7938 1520-6033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/btpr.2735 |
container_title |
Biotechnology Progress |
container_volume |
35 |
container_issue |
1 |
container_start_page |
e2735 |
_version_ |
1810495837302685696 |