Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s00449-016-1667-9 http://hdl.handle.net/11449/173331 |
Resumo: | It is known that lipases may have their catalytic properties improved by the action of some salts or by the adsorption on hydrophobic supports. However, what we present in this work is more than that: we evaluate the combination of these two factors of hyperactivation of lipases from Acremonium-like ROG 2.1.9, a study that has not been done so far. This work proves that a synergistic effect occurs when the lipases are immobilized on hydrophobic supports at the presence of sodium chloride and are applied in triacylglycerol hydrolysis. This assay made it possible to achieve the highest hyperactivation of 500 % with the lipases immobilized on Phenyl-Sepharose and applied with 0.1 M of sodium chloride. Besides this positive effect on enzyme activity, the use of these two factors led to the thermal stability increasing of the immobilized lipases. For this derivative, the recovered activity was approximately 85 % after 6 h incubated at 55 °C and 1.0 M of the sodium chloride against 50 % of the same derivative without this salt. Furthermore, others assays were performed to prove the evidences about the synergistic effect, showing a promising method to improve the catalytic properties of the lipases from Acremonium-like ROG 2.1.9. |
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Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergismHydrolysisHyperactivationImmobilizationLipasesSynergismIt is known that lipases may have their catalytic properties improved by the action of some salts or by the adsorption on hydrophobic supports. However, what we present in this work is more than that: we evaluate the combination of these two factors of hyperactivation of lipases from Acremonium-like ROG 2.1.9, a study that has not been done so far. This work proves that a synergistic effect occurs when the lipases are immobilized on hydrophobic supports at the presence of sodium chloride and are applied in triacylglycerol hydrolysis. This assay made it possible to achieve the highest hyperactivation of 500 % with the lipases immobilized on Phenyl-Sepharose and applied with 0.1 M of sodium chloride. Besides this positive effect on enzyme activity, the use of these two factors led to the thermal stability increasing of the immobilized lipases. For this derivative, the recovered activity was approximately 85 % after 6 h incubated at 55 °C and 1.0 M of the sodium chloride against 50 % of the same derivative without this salt. Furthermore, others assays were performed to prove the evidences about the synergistic effect, showing a promising method to improve the catalytic properties of the lipases from Acremonium-like ROG 2.1.9.Department of Chemistry and Environmental Sciences IBILCE/UNESP, Rua Cristóvão Colombo, 2265Department of Biology IBILCE/UNESP, Rua Cristóvão Colombo, 2265Department of Biochemistry and Chemical Technology IQ/UNESP, Rua Prof. Francisco Degni, 55Department of Catalysis CSIC (Consejo Superior de Investigaciones CientÃficas), Campus Universidad Autônoma, CantoblancoDepartment of Chemistry and Environmental Sciences IBILCE/UNESP, Rua Cristóvão Colombo, 2265Department of Biology IBILCE/UNESP, Rua Cristóvão Colombo, 2265Department of Biochemistry and Chemical Technology IQ/UNESP, Rua Prof. Francisco Degni, 55Universidade Estadual Paulista (Unesp)CSIC (Consejo Superior de Investigaciones CientÃficas)Quilles Junior, José Carlos [UNESP]Ferrarezi, Ana Lúcia [UNESP]Borges, Janaina Pires [UNESP]Brito, Rafaela Rodrigues [UNESP]Gomes, Eleni [UNESP]da Silva, Roberto [UNESP]Guisán, José ManuelBoscolo, MaurÃcio [UNESP]2018-12-11T17:04:42Z2018-12-11T17:04:42Z2016-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1933-1943application/pdfhttp://dx.doi.org/10.1007/s00449-016-1667-9Bioprocess and Biosystems Engineering, v. 39, n. 12, p. 1933-1943, 2016.1615-76051615-7591http://hdl.handle.net/11449/17333110.1007/s00449-016-1667-92-s2.0-849812769762-s2.0-84981276976.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBioprocess and Biosystems Engineering0,6400,640info:eu-repo/semantics/openAccess2023-12-25T06:22:09Zoai:repositorio.unesp.br:11449/173331Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-25T06:22:09Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism |
title |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism |
spellingShingle |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism Quilles Junior, José Carlos [UNESP] Hydrolysis Hyperactivation Immobilization Lipases Synergism |
title_short |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism |
title_full |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism |
title_fullStr |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism |
title_full_unstemmed |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism |
title_sort |
Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism |
author |
Quilles Junior, José Carlos [UNESP] |
author_facet |
Quilles Junior, José Carlos [UNESP] Ferrarezi, Ana Lúcia [UNESP] Borges, Janaina Pires [UNESP] Brito, Rafaela Rodrigues [UNESP] Gomes, Eleni [UNESP] da Silva, Roberto [UNESP] Guisán, José Manuel Boscolo, MaurÃcio [UNESP] |
author_role |
author |
author2 |
Ferrarezi, Ana Lúcia [UNESP] Borges, Janaina Pires [UNESP] Brito, Rafaela Rodrigues [UNESP] Gomes, Eleni [UNESP] da Silva, Roberto [UNESP] Guisán, José Manuel Boscolo, MaurÃcio [UNESP] |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) CSIC (Consejo Superior de Investigaciones CientÃficas) |
dc.contributor.author.fl_str_mv |
Quilles Junior, José Carlos [UNESP] Ferrarezi, Ana Lúcia [UNESP] Borges, Janaina Pires [UNESP] Brito, Rafaela Rodrigues [UNESP] Gomes, Eleni [UNESP] da Silva, Roberto [UNESP] Guisán, José Manuel Boscolo, MaurÃcio [UNESP] |
dc.subject.por.fl_str_mv |
Hydrolysis Hyperactivation Immobilization Lipases Synergism |
topic |
Hydrolysis Hyperactivation Immobilization Lipases Synergism |
description |
It is known that lipases may have their catalytic properties improved by the action of some salts or by the adsorption on hydrophobic supports. However, what we present in this work is more than that: we evaluate the combination of these two factors of hyperactivation of lipases from Acremonium-like ROG 2.1.9, a study that has not been done so far. This work proves that a synergistic effect occurs when the lipases are immobilized on hydrophobic supports at the presence of sodium chloride and are applied in triacylglycerol hydrolysis. This assay made it possible to achieve the highest hyperactivation of 500 % with the lipases immobilized on Phenyl-Sepharose and applied with 0.1 M of sodium chloride. Besides this positive effect on enzyme activity, the use of these two factors led to the thermal stability increasing of the immobilized lipases. For this derivative, the recovered activity was approximately 85 % after 6 h incubated at 55 °C and 1.0 M of the sodium chloride against 50 % of the same derivative without this salt. Furthermore, others assays were performed to prove the evidences about the synergistic effect, showing a promising method to improve the catalytic properties of the lipases from Acremonium-like ROG 2.1.9. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-12-01 2018-12-11T17:04:42Z 2018-12-11T17:04:42Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1007/s00449-016-1667-9 Bioprocess and Biosystems Engineering, v. 39, n. 12, p. 1933-1943, 2016. 1615-7605 1615-7591 http://hdl.handle.net/11449/173331 10.1007/s00449-016-1667-9 2-s2.0-84981276976 2-s2.0-84981276976.pdf |
url |
http://dx.doi.org/10.1007/s00449-016-1667-9 http://hdl.handle.net/11449/173331 |
identifier_str_mv |
Bioprocess and Biosystems Engineering, v. 39, n. 12, p. 1933-1943, 2016. 1615-7605 1615-7591 10.1007/s00449-016-1667-9 2-s2.0-84981276976 2-s2.0-84981276976.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Bioprocess and Biosystems Engineering 0,640 0,640 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
1933-1943 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1799965403128004608 |