Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus

Detalhes bibliográficos
Autor(a) principal: Araújo, Francisco Jonathan dos Santos
Data de Publicação: 2018
Outros Autores: Gomes, Brenda Suellen Rodrigues, Bessa, Claudiane Carvalho, Soares Júnior, João Alberto de Oliveira, Hissa, Denise Cavalcante, Melo, Vânia Maria Maciel
Tipo de documento: Artigo de conferência
Idioma: eng
Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
Texto Completo: http://www.repositorio.ufc.br/handle/riufc/54419
Resumo: Esterases are lipolytic enzymes widely used in industrial applications. This work aimed the overexpression and purification of the esterase LipG7 identified from a metagenomic library constructed from mangrove sediments, which gene sequence shares 80% amino acid identity to 1,4-butanediol diacrylate esterase from the bacterium Porticoccus hydrocarbonoclasticus. LipG7 was expressed in three commercial Escherichia coli strains, Rosetta-gami, ArcticExpress and BL21 and the activity evaluated against 4-nitrophenyl butyrate substract. Recombinante esterase was obtained in soluble form only in Rosetta-gami after treatment with guanidine hydrochloride. It was active against 4-nitrophenyl butyrate at 30 °C with specific activity of 216.3 ± 16.4 U/mg that was significantly enhanced in presence of Mg2+ ion.
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spelling Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticusEsterasesEsterase LipG7EnzimasEsterases are lipolytic enzymes widely used in industrial applications. This work aimed the overexpression and purification of the esterase LipG7 identified from a metagenomic library constructed from mangrove sediments, which gene sequence shares 80% amino acid identity to 1,4-butanediol diacrylate esterase from the bacterium Porticoccus hydrocarbonoclasticus. LipG7 was expressed in three commercial Escherichia coli strains, Rosetta-gami, ArcticExpress and BL21 and the activity evaluated against 4-nitrophenyl butyrate substract. Recombinante esterase was obtained in soluble form only in Rosetta-gami after treatment with guanidine hydrochloride. It was active against 4-nitrophenyl butyrate at 30 °C with specific activity of 216.3 ± 16.4 U/mg that was significantly enhanced in presence of Mg2+ ion.2020-10-01T17:42:38Z2020-10-01T17:42:38Z2018info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectapplication/pdfARAÚJO, Francisco Jonathan dos Santos; GOMES, Brenda Suellen Rodrigues; BESSA, Claudiane Carvalho; SOARES JÚNIOR, João Alberto de Oliveira; HISSA, Denise Cavalcante; MELO, Vânia Maria Maciel. Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus. In: CONGRESSO BRASILEIRO DE ENGENHARIA QUÍMICA, XXII., 23 a 26 set. 2018; ENCONTRO BRASILEIRO SOBRE O ENSINO DE ENGENHARIA QUÍMICA, XVII., 27 a 28 set. 2018, São Paulo, Brasil. Anais […] São Paulo, 2018.2359-1757http://www.repositorio.ufc.br/handle/riufc/54419Araújo, Francisco Jonathan dos SantosGomes, Brenda Suellen RodriguesBessa, Claudiane CarvalhoSoares Júnior, João Alberto de OliveiraHissa, Denise CavalcanteMelo, Vânia Maria Macielengreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFCinfo:eu-repo/semantics/openAccess2020-10-01T17:43:22Zoai:repositorio.ufc.br:riufc/54419Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2024-09-11T19:02:31.584728Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false
dc.title.none.fl_str_mv Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
title Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
spellingShingle Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
Araújo, Francisco Jonathan dos Santos
Esterases
Esterase LipG7
Enzimas
title_short Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
title_full Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
title_fullStr Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
title_full_unstemmed Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
title_sort Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus
author Araújo, Francisco Jonathan dos Santos
author_facet Araújo, Francisco Jonathan dos Santos
Gomes, Brenda Suellen Rodrigues
Bessa, Claudiane Carvalho
Soares Júnior, João Alberto de Oliveira
Hissa, Denise Cavalcante
Melo, Vânia Maria Maciel
author_role author
author2 Gomes, Brenda Suellen Rodrigues
Bessa, Claudiane Carvalho
Soares Júnior, João Alberto de Oliveira
Hissa, Denise Cavalcante
Melo, Vânia Maria Maciel
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Araújo, Francisco Jonathan dos Santos
Gomes, Brenda Suellen Rodrigues
Bessa, Claudiane Carvalho
Soares Júnior, João Alberto de Oliveira
Hissa, Denise Cavalcante
Melo, Vânia Maria Maciel
dc.subject.por.fl_str_mv Esterases
Esterase LipG7
Enzimas
topic Esterases
Esterase LipG7
Enzimas
description Esterases are lipolytic enzymes widely used in industrial applications. This work aimed the overexpression and purification of the esterase LipG7 identified from a metagenomic library constructed from mangrove sediments, which gene sequence shares 80% amino acid identity to 1,4-butanediol diacrylate esterase from the bacterium Porticoccus hydrocarbonoclasticus. LipG7 was expressed in three commercial Escherichia coli strains, Rosetta-gami, ArcticExpress and BL21 and the activity evaluated against 4-nitrophenyl butyrate substract. Recombinante esterase was obtained in soluble form only in Rosetta-gami after treatment with guanidine hydrochloride. It was active against 4-nitrophenyl butyrate at 30 °C with specific activity of 216.3 ± 16.4 U/mg that was significantly enhanced in presence of Mg2+ ion.
publishDate 2018
dc.date.none.fl_str_mv 2018
2020-10-01T17:42:38Z
2020-10-01T17:42:38Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/conferenceObject
format conferenceObject
status_str publishedVersion
dc.identifier.uri.fl_str_mv ARAÚJO, Francisco Jonathan dos Santos; GOMES, Brenda Suellen Rodrigues; BESSA, Claudiane Carvalho; SOARES JÚNIOR, João Alberto de Oliveira; HISSA, Denise Cavalcante; MELO, Vânia Maria Maciel. Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus. In: CONGRESSO BRASILEIRO DE ENGENHARIA QUÍMICA, XXII., 23 a 26 set. 2018; ENCONTRO BRASILEIRO SOBRE O ENSINO DE ENGENHARIA QUÍMICA, XVII., 27 a 28 set. 2018, São Paulo, Brasil. Anais […] São Paulo, 2018.
2359-1757
http://www.repositorio.ufc.br/handle/riufc/54419
identifier_str_mv ARAÚJO, Francisco Jonathan dos Santos; GOMES, Brenda Suellen Rodrigues; BESSA, Claudiane Carvalho; SOARES JÚNIOR, João Alberto de Oliveira; HISSA, Denise Cavalcante; MELO, Vânia Maria Maciel. Expression and purification of a new esterase from metagenomic clone similar to bacterial esterase of the Porticoccus hydrocarbonoclasticus. In: CONGRESSO BRASILEIRO DE ENGENHARIA QUÍMICA, XXII., 23 a 26 set. 2018; ENCONTRO BRASILEIRO SOBRE O ENSINO DE ENGENHARIA QUÍMICA, XVII., 27 a 28 set. 2018, São Paulo, Brasil. Anais […] São Paulo, 2018.
2359-1757
url http://www.repositorio.ufc.br/handle/riufc/54419
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Institucional da Universidade Federal do Ceará (UFC)
instname:Universidade Federal do Ceará (UFC)
instacron:UFC
instname_str Universidade Federal do Ceará (UFC)
instacron_str UFC
institution UFC
reponame_str Repositório Institucional da Universidade Federal do Ceará (UFC)
collection Repositório Institucional da Universidade Federal do Ceará (UFC)
repository.name.fl_str_mv Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)
repository.mail.fl_str_mv bu@ufc.br || repositorio@ufc.br
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