Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/27703 |
Resumo: | Background: The hydrolytic action of cutinases has been applied to the degradation of plastics. Polyethylene terephthalate (PET) have long half-life which constitutes a major problem for their treatment as urban solid residues. The aim of this work was to characterize and to improve stable the enzyme to optimize the process of degradation using enzymatic hydrolysis of PET by recombinant cutinases. Results: The wild type form of cutinase from Fusarium solani pisi and its C-terminal fusion to cellulose binding domain N1 from Cellulomonas fimi were produced by genetically modified Escherichia coli. The maximum activity of cutinases produced in Lactose Broth in the presence of ampicillin and isopropyl β- D-1-thiogalactopyranoside (IPTG) was 1.4 IU/mL. Both cutinases had an optimum pH around 7.0 and they were stable between 30 and 50ºC during 90 min. The addition of glycerol, PEG-200 and (NH4)2SO4 to the metabolic liquid, concentrated by ultra filtration, stabilized the activity during 60 days at 28ºC. The treatment of PET with cutinases during 48 hrs led to maxima weight loss of 0.90%. Conclusions: Recombinant microbial cutinases may present advantages in the treatment of poly(ethylene terephthalate) PET through enzymatic treatments. |
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Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradationcutinaseenvironmental applicationpoly(ethylene terephthalate).Science & TechnologyBackground: The hydrolytic action of cutinases has been applied to the degradation of plastics. Polyethylene terephthalate (PET) have long half-life which constitutes a major problem for their treatment as urban solid residues. The aim of this work was to characterize and to improve stable the enzyme to optimize the process of degradation using enzymatic hydrolysis of PET by recombinant cutinases. Results: The wild type form of cutinase from Fusarium solani pisi and its C-terminal fusion to cellulose binding domain N1 from Cellulomonas fimi were produced by genetically modified Escherichia coli. The maximum activity of cutinases produced in Lactose Broth in the presence of ampicillin and isopropyl β- D-1-thiogalactopyranoside (IPTG) was 1.4 IU/mL. Both cutinases had an optimum pH around 7.0 and they were stable between 30 and 50ºC during 90 min. The addition of glycerol, PEG-200 and (NH4)2SO4 to the metabolic liquid, concentrated by ultra filtration, stabilized the activity during 60 days at 28ºC. The treatment of PET with cutinases during 48 hrs led to maxima weight loss of 0.90%. Conclusions: Recombinant microbial cutinases may present advantages in the treatment of poly(ethylene terephthalate) PET through enzymatic treatments.This research study was financially supported by CAPES (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior), FACEPE (Fundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco) and CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnologico).Pontificia Universidad Católica de ValparaísoUniversidade do MinhoGomes, Daniela S.Matamá, Maria TeresaPaulo, Artur CavacoCampos-Takaki, Galba MariaSalgueiro, Alexandra A.20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/27703eng0717-345810.2225/vol16issue5-fulltext-12info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T11:54:09Zoai:repositorium.sdum.uminho.pt:1822/27703Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:43:35.890462Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation |
title |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation |
spellingShingle |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation Gomes, Daniela S. cutinase environmental application poly(ethylene terephthalate). Science & Technology |
title_short |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation |
title_full |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation |
title_fullStr |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation |
title_full_unstemmed |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation |
title_sort |
Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation |
author |
Gomes, Daniela S. |
author_facet |
Gomes, Daniela S. Matamá, Maria Teresa Paulo, Artur Cavaco Campos-Takaki, Galba Maria Salgueiro, Alexandra A. |
author_role |
author |
author2 |
Matamá, Maria Teresa Paulo, Artur Cavaco Campos-Takaki, Galba Maria Salgueiro, Alexandra A. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Gomes, Daniela S. Matamá, Maria Teresa Paulo, Artur Cavaco Campos-Takaki, Galba Maria Salgueiro, Alexandra A. |
dc.subject.por.fl_str_mv |
cutinase environmental application poly(ethylene terephthalate). Science & Technology |
topic |
cutinase environmental application poly(ethylene terephthalate). Science & Technology |
description |
Background: The hydrolytic action of cutinases has been applied to the degradation of plastics. Polyethylene terephthalate (PET) have long half-life which constitutes a major problem for their treatment as urban solid residues. The aim of this work was to characterize and to improve stable the enzyme to optimize the process of degradation using enzymatic hydrolysis of PET by recombinant cutinases. Results: The wild type form of cutinase from Fusarium solani pisi and its C-terminal fusion to cellulose binding domain N1 from Cellulomonas fimi were produced by genetically modified Escherichia coli. The maximum activity of cutinases produced in Lactose Broth in the presence of ampicillin and isopropyl β- D-1-thiogalactopyranoside (IPTG) was 1.4 IU/mL. Both cutinases had an optimum pH around 7.0 and they were stable between 30 and 50ºC during 90 min. The addition of glycerol, PEG-200 and (NH4)2SO4 to the metabolic liquid, concentrated by ultra filtration, stabilized the activity during 60 days at 28ºC. The treatment of PET with cutinases during 48 hrs led to maxima weight loss of 0.90%. Conclusions: Recombinant microbial cutinases may present advantages in the treatment of poly(ethylene terephthalate) PET through enzymatic treatments. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 2013-01-01T00:00:00Z |
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://hdl.handle.net/1822/27703 |
url |
http://hdl.handle.net/1822/27703 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0717-3458 10.2225/vol16issue5-fulltext-12 |
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.publisher.none.fl_str_mv |
Pontificia Universidad Católica de Valparaíso |
publisher.none.fl_str_mv |
Pontificia Universidad Católica de Valparaíso |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799132183617601536 |