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Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation Electron. J. Biotechnol.
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 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....
Tipo: Journal article Palavras-chave: Cutinase; Environmental application; Poly(ethylene terephthalate).
Ano: 2013 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000500003
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