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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 16, No. 5, 2013
Bioline Code: ej13053
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 16, No. 5, 2013

 en Production of heterologous cutinases by E. coli check for this species in other resources and improved enzyme formulation for application on plastic degradation
Gomes, Daniela S.; Matamá, Teresa; Cavaco-Paulo, Artur; Campos-Takaki, Galba M. & Salgueiro, Alexandra A.


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 check for this species in other resources and its C-terminal fusion to cellulose binding domain N1 from Cellulomonas fimi check for this species in other resources were produced by genetically modified Escherichia coli check for this species in other resources . 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.

cutinase; environmental application; poly(ethylene terephthalate)

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