Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features
Eversa is an enzyme recently launched by Novozymes to be used in a free form as biocatalyst in biodiesel production. This paper shows for first time the immobilization of Eversa (a commercial lipase) on octyl and aminated agarose beads and the comparison of the enzyme properties to those of the most...
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Multidisciplinary Digital Publishing Institute
2018
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Online Access: | http://hdl.handle.net/10261/172534 https://doi.org/10.3390/catal8110511 https://doi.org/10.13039/501100003329 |
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ftcsic:oai:digital.csic.es:10261/172534 2024-02-11T09:55:53+01:00 Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features Arana-Peña, Sara Lokha, Yuliya Fernández-Lafuente, Roberto Colciencias (Colombia) Ministerio de Economía y Competitividad (España) 2018-11-02 http://hdl.handle.net/10261/172534 https://doi.org/10.3390/catal8110511 https://doi.org/10.13039/501100003329 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/CTQ2017-86170-R Publisher's version https://doi.org/10.3390/catal8110511 Sí Catalysts 8(11): 511 (2018) 2073-4344 http://hdl.handle.net/10261/172534 doi:10.3390/catal8110511 http://dx.doi.org/10.13039/501100003329 open Eversa Interfacial activation Lipase immobilization Enzyme stabilization Enzyme modulation artículo http://purl.org/coar/resource_type/c_6501 2018 ftcsic https://doi.org/10.3390/catal811051110.13039/501100003329 2024-01-16T10:34:13Z Eversa is an enzyme recently launched by Novozymes to be used in a free form as biocatalyst in biodiesel production. This paper shows for first time the immobilization of Eversa (a commercial lipase) on octyl and aminated agarose beads and the comparison of the enzyme properties to those of the most used lipase, the isoform B from Candida antarctica (CALB) immobilized on octyl agarose beads. Immobilization on octyl and aminated supports of Eversa has not had a significant effect on enzyme activity versus p-nitrophenyl butyrate (pNPB) under standard conditions (pH 7), but immobilization on octyl agarose beads greatly enhanced the stability of the enzyme under all studied conditions, much more than immobilization on aminated support. Octyl-Eversa was much more stable than octyl-CALB at pH 9, but it was less stable at pH 5. In the presence of 90% acetonitrile or dioxane, octyl-Eversa maintained the activity (even increased the activity) after 45 days of incubation in a similar way to octyl-CALB, but in 90% of methanol, results are much worse, and octyl-CALB became much more stable than Eversa. Coating with PEI has not a clear effect on octyl-Eversa stability, although it affected enzyme specificity and activity response to the changes in the pH. Eversa immobilized octyl supports was more active than CALB versus triacetin or pNPB, but much less active versus methyl mandelate esters. On the other hand, Eversa specificity and response to changes in the medium were greatly modulated by the immobilization protocol or by the coating of the immobilized enzyme with PEI. Thus, Eversa may be a promising biocatalyst for many processes different to the biodiesel production and its properties may be greatly improved following a suitable immobilization protocol, and in some cases is more stable and active than CALB. We gratefully recognize the support from the MINECO from Spanish Government, (project number CTQ2017-86170-R) and Colciencias (Colombia) (project number FP 44842-076-2016). Peer reviewed Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Catalysts 8 11 511 |
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Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
unknown |
topic |
Eversa Interfacial activation Lipase immobilization Enzyme stabilization Enzyme modulation |
spellingShingle |
Eversa Interfacial activation Lipase immobilization Enzyme stabilization Enzyme modulation Arana-Peña, Sara Lokha, Yuliya Fernández-Lafuente, Roberto Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features |
topic_facet |
Eversa Interfacial activation Lipase immobilization Enzyme stabilization Enzyme modulation |
description |
Eversa is an enzyme recently launched by Novozymes to be used in a free form as biocatalyst in biodiesel production. This paper shows for first time the immobilization of Eversa (a commercial lipase) on octyl and aminated agarose beads and the comparison of the enzyme properties to those of the most used lipase, the isoform B from Candida antarctica (CALB) immobilized on octyl agarose beads. Immobilization on octyl and aminated supports of Eversa has not had a significant effect on enzyme activity versus p-nitrophenyl butyrate (pNPB) under standard conditions (pH 7), but immobilization on octyl agarose beads greatly enhanced the stability of the enzyme under all studied conditions, much more than immobilization on aminated support. Octyl-Eversa was much more stable than octyl-CALB at pH 9, but it was less stable at pH 5. In the presence of 90% acetonitrile or dioxane, octyl-Eversa maintained the activity (even increased the activity) after 45 days of incubation in a similar way to octyl-CALB, but in 90% of methanol, results are much worse, and octyl-CALB became much more stable than Eversa. Coating with PEI has not a clear effect on octyl-Eversa stability, although it affected enzyme specificity and activity response to the changes in the pH. Eversa immobilized octyl supports was more active than CALB versus triacetin or pNPB, but much less active versus methyl mandelate esters. On the other hand, Eversa specificity and response to changes in the medium were greatly modulated by the immobilization protocol or by the coating of the immobilized enzyme with PEI. Thus, Eversa may be a promising biocatalyst for many processes different to the biodiesel production and its properties may be greatly improved following a suitable immobilization protocol, and in some cases is more stable and active than CALB. We gratefully recognize the support from the MINECO from Spanish Government, (project number CTQ2017-86170-R) and Colciencias (Colombia) (project number FP 44842-076-2016). Peer reviewed |
author2 |
Colciencias (Colombia) Ministerio de Economía y Competitividad (España) |
format |
Article in Journal/Newspaper |
author |
Arana-Peña, Sara Lokha, Yuliya Fernández-Lafuente, Roberto |
author_facet |
Arana-Peña, Sara Lokha, Yuliya Fernández-Lafuente, Roberto |
author_sort |
Arana-Peña, Sara |
title |
Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features |
title_short |
Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features |
title_full |
Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features |
title_fullStr |
Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features |
title_full_unstemmed |
Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features |
title_sort |
immobilization of eversa lipase on octyl agarose beads and preliminary characterization of stability and activity features |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2018 |
url |
http://hdl.handle.net/10261/172534 https://doi.org/10.3390/catal8110511 https://doi.org/10.13039/501100003329 |
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/CTQ2017-86170-R Publisher's version https://doi.org/10.3390/catal8110511 Sí Catalysts 8(11): 511 (2018) 2073-4344 http://hdl.handle.net/10261/172534 doi:10.3390/catal8110511 http://dx.doi.org/10.13039/501100003329 |
op_rights |
open |
op_doi |
https://doi.org/10.3390/catal811051110.13039/501100003329 |
container_title |
Catalysts |
container_volume |
8 |
container_issue |
11 |
container_start_page |
511 |
_version_ |
1790599344840245248 |