Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
Lipase stability in organic solvent is crucial for its application in many biotechnological processes as biocatalyst. One way to improve lipase’s activity and stability in unusual reaction medium is its immobilization on inert supports. Here, lipases from different sources and immobilized through we...
Published in: | Bioprocess and Biosystems Engineering |
---|---|
Main Authors: | , , , , , , , , |
Other Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Springer Nature
2020
|
Subjects: | |
Online Access: | http://hdl.handle.net/10261/220089 https://doi.org/10.1007/s00449-020-02399-1 https://doi.org/10.13039/501100001807 https://doi.org/10.13039/501100002322 |
id |
ftcsic:oai:digital.csic.es:10261/220089 |
---|---|
record_format |
openpolar |
spelling |
ftcsic:oai:digital.csic.es:10261/220089 2024-02-11T09:57:40+01:00 Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents Pires Borges, Janaina Quilles Junior, José Carlos Moreno-Pérez, Sonia Fernández-Lorente, Gloria Boscolo, Mauricio Gomes, Eleni Silva, Roberto da Alonso Bocchini, Daniela Guisán, José Manuel Fundação de Amparo à Pesquisa do Estado de São Paulo Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) 2020 http://hdl.handle.net/10261/220089 https://doi.org/10.1007/s00449-020-02399-1 https://doi.org/10.13039/501100001807 https://doi.org/10.13039/501100002322 en eng Springer Nature https://doi.org/10.1007/s00449-020-02399-1 Sí Bioprocess and Biosystems Engineering 43: 2107–2115 (2020) 1615-7591 http://hdl.handle.net/10261/220089 doi:10.1007/s00449-020-02399-1 1615-7605 http://dx.doi.org/10.13039/501100001807 http://dx.doi.org/10.13039/501100002322 none artículo http://purl.org/coar/resource_type/c_6501 2020 ftcsic https://doi.org/10.1007/s00449-020-02399-110.13039/50110000180710.13039/501100002322 2024-01-16T10:58:03Z Lipase stability in organic solvent is crucial for its application in many biotechnological processes as biocatalyst. One way to improve lipase’s activity and stability in unusual reaction medium is its immobilization on inert supports. Here, lipases from different sources and immobilized through weak chemical interactions on hydrophobic and ionic supports had their transesterification ability dramatically dependent on the support and also on the solvent that had been used. The ethanolysis of sardine oil was carried out at the presence of cyclohexane and tert-amyl alcohol, in which Duolite A568-Thermomyces lanuginosa lipase derivative achieved 49% of ethyl esters production after 24 h in cyclohexane. The selectivity of immobilized lipases was also studied and, after 3 h of synthesis, the reaction with Duolite A568-Thermomyces lanuginosa derivative in cyclohexane produced 24% ethyl ester of eicosapentaenoic acid and 1.2% ethyl ester of docosahexaenoic acid, displaying a selectivity index of 20 times the ethyl ester of eicosapentaenoic acid. Different derivatives of Candida antarctica lipases fraction B (CALB) and phospholipase Lecitase® Ultra (Lecitase) were also investigated. Along these lines, a combination between these factors may be applied to improve the activity and selectivity of immobilized lipases, decreasing the total cost of the process. The authors thank the financial support from the São Paulo Research Foundation (FAPESP – grants 2012/09054-3 and 2013/00530-0), and the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior—Brasil (CAPES – grant number 3894/13-4). Peer reviewed Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Bioprocess and Biosystems Engineering 43 11 2107 2115 |
institution |
Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
English |
description |
Lipase stability in organic solvent is crucial for its application in many biotechnological processes as biocatalyst. One way to improve lipase’s activity and stability in unusual reaction medium is its immobilization on inert supports. Here, lipases from different sources and immobilized through weak chemical interactions on hydrophobic and ionic supports had their transesterification ability dramatically dependent on the support and also on the solvent that had been used. The ethanolysis of sardine oil was carried out at the presence of cyclohexane and tert-amyl alcohol, in which Duolite A568-Thermomyces lanuginosa lipase derivative achieved 49% of ethyl esters production after 24 h in cyclohexane. The selectivity of immobilized lipases was also studied and, after 3 h of synthesis, the reaction with Duolite A568-Thermomyces lanuginosa derivative in cyclohexane produced 24% ethyl ester of eicosapentaenoic acid and 1.2% ethyl ester of docosahexaenoic acid, displaying a selectivity index of 20 times the ethyl ester of eicosapentaenoic acid. Different derivatives of Candida antarctica lipases fraction B (CALB) and phospholipase Lecitase® Ultra (Lecitase) were also investigated. Along these lines, a combination between these factors may be applied to improve the activity and selectivity of immobilized lipases, decreasing the total cost of the process. The authors thank the financial support from the São Paulo Research Foundation (FAPESP – grants 2012/09054-3 and 2013/00530-0), and the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior—Brasil (CAPES – grant number 3894/13-4). Peer reviewed |
author2 |
Fundação de Amparo à Pesquisa do Estado de São Paulo Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) |
format |
Article in Journal/Newspaper |
author |
Pires Borges, Janaina Quilles Junior, José Carlos Moreno-Pérez, Sonia Fernández-Lorente, Gloria Boscolo, Mauricio Gomes, Eleni Silva, Roberto da Alonso Bocchini, Daniela Guisán, José Manuel |
spellingShingle |
Pires Borges, Janaina Quilles Junior, José Carlos Moreno-Pérez, Sonia Fernández-Lorente, Gloria Boscolo, Mauricio Gomes, Eleni Silva, Roberto da Alonso Bocchini, Daniela Guisán, José Manuel Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents |
author_facet |
Pires Borges, Janaina Quilles Junior, José Carlos Moreno-Pérez, Sonia Fernández-Lorente, Gloria Boscolo, Mauricio Gomes, Eleni Silva, Roberto da Alonso Bocchini, Daniela Guisán, José Manuel |
author_sort |
Pires Borges, Janaina |
title |
Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents |
title_short |
Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents |
title_full |
Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents |
title_fullStr |
Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents |
title_full_unstemmed |
Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents |
title_sort |
ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents |
publisher |
Springer Nature |
publishDate |
2020 |
url |
http://hdl.handle.net/10261/220089 https://doi.org/10.1007/s00449-020-02399-1 https://doi.org/10.13039/501100001807 https://doi.org/10.13039/501100002322 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
https://doi.org/10.1007/s00449-020-02399-1 Sí Bioprocess and Biosystems Engineering 43: 2107–2115 (2020) 1615-7591 http://hdl.handle.net/10261/220089 doi:10.1007/s00449-020-02399-1 1615-7605 http://dx.doi.org/10.13039/501100001807 http://dx.doi.org/10.13039/501100002322 |
op_rights |
none |
op_doi |
https://doi.org/10.1007/s00449-020-02399-110.13039/50110000180710.13039/501100002322 |
container_title |
Bioprocess and Biosystems Engineering |
container_volume |
43 |
container_issue |
11 |
container_start_page |
2107 |
op_container_end_page |
2115 |
_version_ |
1790593207721000960 |