Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism

Detalhes bibliográficos
Autor(a) principal: Quilles Junior, José Carlos [UNESP]
Data de Publicação: 2016
Outros Autores: Ferrarezi, Ana Lúcia [UNESP], Borges, Janaina Pires [UNESP], Brito, Rafaela Rodrigues [UNESP], Gomes, Eleni [UNESP], da Silva, Roberto [UNESP], Guisán, José Manuel, Boscolo, Maurício [UNESP]
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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spelling 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 Científicas), 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 Científicas)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, Maurício [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, Maurício [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, Maurício [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 Científicas)
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, Maurício [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
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