Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://www.sciencedirect.com/science/article/pii/S1369703X14002939 http://hdl.handle.net/11449/122852 |
Resumo: | Most of lipases are in equilibrium between a majority inactive closed form and a minority active open form in aqueous media. Perhaps, a certain stabilization of these open forms of lipases could be achieved in the presence of cosolvents or surfactants in the reaction medium. Three commercial lipases were studied (from Thermomyces lanuginosa (TLL), Candida Antarctica fraction B (CALB) and Lecitase (LEC)). Different derivatives were tested: TLL and LEC were adsorbed on an anionic exchanger and their activity strongly depends on the equilibrium between their open and closed form and CALB was adsorbed on a hydrophobic support when the open form was already stabilized by the support. Derivatives ionically adsorbed were hyperactivated by surfactans as well as by cosolvents: the activity of LEC increased 12 times in the presence of 15–20% of ethanol. CALB adsorbed on hydrophobic supports was hardly hyperactivated and even it was inhibited. The modification of the rate of covalent modification of the catalytic Ser seems to confirm that the observed hyperactivations were due to a stabilization of the open form of the adsorbed lipases (TLL and LEC). The hydrolysis of sardine oil was also studied in the presence or absence of surfactants and cosolvents. An interesting improvement in the ability of derivatives to discriminate the release of eicosipentaenic acid (EPA) and docosahexaenicacid (DHA) was found. |
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Modulation of the activity and selectivity of the immobilized lipases by surfactants and solventsLipasesImmobilizationStabilitySelectivitySurfactantsHydrolysis of fish oilMost of lipases are in equilibrium between a majority inactive closed form and a minority active open form in aqueous media. Perhaps, a certain stabilization of these open forms of lipases could be achieved in the presence of cosolvents or surfactants in the reaction medium. Three commercial lipases were studied (from Thermomyces lanuginosa (TLL), Candida Antarctica fraction B (CALB) and Lecitase (LEC)). Different derivatives were tested: TLL and LEC were adsorbed on an anionic exchanger and their activity strongly depends on the equilibrium between their open and closed form and CALB was adsorbed on a hydrophobic support when the open form was already stabilized by the support. Derivatives ionically adsorbed were hyperactivated by surfactans as well as by cosolvents: the activity of LEC increased 12 times in the presence of 15–20% of ethanol. CALB adsorbed on hydrophobic supports was hardly hyperactivated and even it was inhibited. The modification of the rate of covalent modification of the catalytic Ser seems to confirm that the observed hyperactivations were due to a stabilization of the open form of the adsorbed lipases (TLL and LEC). The hydrolysis of sardine oil was also studied in the presence or absence of surfactants and cosolvents. An interesting improvement in the ability of derivatives to discriminate the release of eicosipentaenic acid (EPA) and docosahexaenicacid (DHA) was found.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Universidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Biologia, Instituto de Biociências Letras e Ciências Exatas de São José do Rio Preto, Sao Jose do Rio Preto, RUA CRISTOVAO COLOMBO, 2265, JARDIM NAZARETH, CEP 15054-000, SP, BrasilUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Biologia, Instituto de Biociências Letras e Ciências Exatas de São José do Rio Preto, Sao Jose do Rio Preto, RUA CRISTOVAO COLOMBO, 2265, JARDIM NAZARETH, CEP 15054-000, SP, BrasilIQ/UNESP, Departament of Biochemistry and Chemical Technology—Rua Prof. Francisco Degni, 55—CEP, 14800-060 Araraquara, SP, BrazilDepartament of Biotechnology and Food Microbiology, Research Institute for Food Science, CIAL-CSIC, Campus UAM, 28049 Madrid, SpainDepartament of Catalysis, CSIC (Consejo Superior de Investigaciones Científicas), Campus UAM, 28049 Madrid, SpainFAPESP: 2013/00530-0Universidade Estadual Paulista (Unesp)Quilles Júnior, José Carlos [UNESP]Brito, R. R. [UNESP]Borges, J. P. [UNESP]Aragon, C. C. [UNESP]Fernandez-Lorente, G.Bocchini-Martins, D. A. [UNESP]Gomes, Eleni [UNESP]Silva, Roberto da [UNESP]Boscolo, Mauricio [UNESP]Guisan, J. M.2015-04-27T11:56:06Z2015-04-27T11:56:06Z2015info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article274-280http://www.sciencedirect.com/science/article/pii/S1369703X14002939Biochemical Engineering Journal, v. 93, p. 274-280, 2015.1369-703Xhttp://hdl.handle.net/11449/12285210.1016/j.bej.2014.10.009709124174285192094241756882065458880074921989984Currículo Lattesreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiochemical Engineering Journal3.226info:eu-repo/semantics/openAccess2021-10-23T21:56:33Zoai:repositorio.unesp.br:11449/122852Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T21:56:33Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents |
title |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents |
spellingShingle |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents Quilles Júnior, José Carlos [UNESP] Lipases Immobilization Stability Selectivity Surfactants Hydrolysis of fish oil |
title_short |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents |
title_full |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents |
title_fullStr |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents |
title_full_unstemmed |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents |
title_sort |
Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents |
author |
Quilles Júnior, José Carlos [UNESP] |
author_facet |
Quilles Júnior, José Carlos [UNESP] Brito, R. R. [UNESP] Borges, J. P. [UNESP] Aragon, C. C. [UNESP] Fernandez-Lorente, G. Bocchini-Martins, D. A. [UNESP] Gomes, Eleni [UNESP] Silva, Roberto da [UNESP] Boscolo, Mauricio [UNESP] Guisan, J. M. |
author_role |
author |
author2 |
Brito, R. R. [UNESP] Borges, J. P. [UNESP] Aragon, C. C. [UNESP] Fernandez-Lorente, G. Bocchini-Martins, D. A. [UNESP] Gomes, Eleni [UNESP] Silva, Roberto da [UNESP] Boscolo, Mauricio [UNESP] Guisan, J. M. |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Quilles Júnior, José Carlos [UNESP] Brito, R. R. [UNESP] Borges, J. P. [UNESP] Aragon, C. C. [UNESP] Fernandez-Lorente, G. Bocchini-Martins, D. A. [UNESP] Gomes, Eleni [UNESP] Silva, Roberto da [UNESP] Boscolo, Mauricio [UNESP] Guisan, J. M. |
dc.subject.por.fl_str_mv |
Lipases Immobilization Stability Selectivity Surfactants Hydrolysis of fish oil |
topic |
Lipases Immobilization Stability Selectivity Surfactants Hydrolysis of fish oil |
description |
Most of lipases are in equilibrium between a majority inactive closed form and a minority active open form in aqueous media. Perhaps, a certain stabilization of these open forms of lipases could be achieved in the presence of cosolvents or surfactants in the reaction medium. Three commercial lipases were studied (from Thermomyces lanuginosa (TLL), Candida Antarctica fraction B (CALB) and Lecitase (LEC)). Different derivatives were tested: TLL and LEC were adsorbed on an anionic exchanger and their activity strongly depends on the equilibrium between their open and closed form and CALB was adsorbed on a hydrophobic support when the open form was already stabilized by the support. Derivatives ionically adsorbed were hyperactivated by surfactans as well as by cosolvents: the activity of LEC increased 12 times in the presence of 15–20% of ethanol. CALB adsorbed on hydrophobic supports was hardly hyperactivated and even it was inhibited. The modification of the rate of covalent modification of the catalytic Ser seems to confirm that the observed hyperactivations were due to a stabilization of the open form of the adsorbed lipases (TLL and LEC). The hydrolysis of sardine oil was also studied in the presence or absence of surfactants and cosolvents. An interesting improvement in the ability of derivatives to discriminate the release of eicosipentaenic acid (EPA) and docosahexaenicacid (DHA) was found. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-04-27T11:56:06Z 2015-04-27T11:56:06Z 2015 |
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://www.sciencedirect.com/science/article/pii/S1369703X14002939 Biochemical Engineering Journal, v. 93, p. 274-280, 2015. 1369-703X http://hdl.handle.net/11449/122852 10.1016/j.bej.2014.10.009 7091241742851920 9424175688206545 8880074921989984 |
url |
http://www.sciencedirect.com/science/article/pii/S1369703X14002939 http://hdl.handle.net/11449/122852 |
identifier_str_mv |
Biochemical Engineering Journal, v. 93, p. 274-280, 2015. 1369-703X 10.1016/j.bej.2014.10.009 7091241742851920 9424175688206545 8880074921989984 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biochemical Engineering Journal 3.226 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
274-280 |
dc.source.none.fl_str_mv |
Currículo Lattes 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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1792962203909881856 |