Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation

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 enzym...

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Autores principales:	Gomes,Daniela S, Matamá,Teresa, Cavaco-Paulo,Artur, Campos-Takaki,Galba M, Salgueiro,Alexandra A
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2013
Materias:	cutinase environmental application poly(ethylene terephthalate)
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000500003
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spelling	oai:scielo:S0717-345820130005000032014-09-17Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradationGomes,Daniela SMatamá,TeresaCavaco-Paulo,ArturCampos-Takaki,Galba MSalgueiro,Alexandra A cutinase environmental application poly(ethylene terephthalate) 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.16 n.5 20132013-09-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000500003en10.2225/vol16-issue5-fulltext-12
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	cutinase environmental application poly(ethylene terephthalate)
spellingShingle	cutinase environmental application poly(ethylene terephthalate) Gomes,Daniela S Matamá,Teresa Cavaco-Paulo,Artur Campos-Takaki,Galba M Salgueiro,Alexandra A Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation
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.
author	Gomes,Daniela S Matamá,Teresa Cavaco-Paulo,Artur Campos-Takaki,Galba M Salgueiro,Alexandra A
author_facet	Gomes,Daniela S Matamá,Teresa Cavaco-Paulo,Artur Campos-Takaki,Galba M Salgueiro,Alexandra A
author_sort	Gomes,Daniela S
title	Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation
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
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2013
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000500003
work_keys_str_mv	AT gomesdanielas productionofheterologouscutinasesbyecoliandimprovedenzymeformulationforapplicationonplasticdegradation AT matamateresa productionofheterologouscutinasesbyecoliandimprovedenzymeformulationforapplicationonplasticdegradation AT cavacopauloartur productionofheterologouscutinasesbyecoliandimprovedenzymeformulationforapplicationonplasticdegradation AT campostakakigalbam productionofheterologouscutinasesbyecoliandimprovedenzymeformulationforapplicationonplasticdegradation AT salgueiroalexandraa productionofheterologouscutinasesbyecoliandimprovedenzymeformulationforapplicationonplasticdegradation
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Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation

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